Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2'-deoxy-ATP + L-methionine + H2O
?
3'-deoxy-ATP + L-methionine + H2O
?
ATP + (2S)-2-amino-4-(but-3-yn-1-ylselanyl)butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-(but-3-yn-1-ylselanyl)butanoic acid
ATP + (2S)-2-amino-4-(but-3-yn-1-ylsulfanyl)butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-(but-3-yn-1-ylsulfanyl)butanoic acid
ATP + (2S)-2-amino-4-(butylselanyl)butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-(butylselanyl)butanoic acid
ATP + (2S)-2-amino-4-(butylsulfanyl)butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-(butylsulfanyl)butanoic acid
27% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-(ethylselanyl)butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-(ethylselanyl)butanoic acid
76% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-(ethylsulfanyl)butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-(ethylsulfanyl)butanoic acid
84% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-(prop-2-en-1-ylselanyl)butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-(prop-2-en-1-ylselanyl)butanoic acid
30% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-(prop-2-en-1-ylsulfanyl)butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-(prop-2-en-1-ylsulfanyl)butanoic acid
27% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-(prop-2-yn-1-ylselanyl)butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-(prop-2-yn-1-ylselanyl)butanoic acid
28% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-(prop-2-yn-1-ylsulfanyl)butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-(prop-2-yn-1-ylsulfanyl)butanoic acid
36% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-(propan-2-ylselanyl)butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-(propan-2-ylselanyl)butanoic acid
40% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-(propan-2-ylsulfanyl)butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-(propan-2-ylsulfanyl)butanoic acid
53% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-(propylselanyl)butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-(propylselanyl)butanoic acid
66% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-(propylsulfanyl)butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-(propylsulfanyl)butanoic acid
44% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-[(2-azido ethyl)sulfanyl]butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-[(2-azido ethyl)sulfanyl]butanoic acid
50% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-[(2-methyl propyl)sulfanyl] butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-[(2-methyl propyl)sulfanyl]butanoic acid
57% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-[(2-methylprop-2-en-1-yl)selanyl]butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-[(2-methylprop-2-en-1-yl)selanyl]butanoic acid
46% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-[(2-methylprop-2-en-1-yl)sulfanyl]butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-[(2-methylprop-2-en-1-yl)sulfanyl]butanoic acid
15% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-[(2E)-but-2-en-1-ylsulfanyl]butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-[(2E)-but-2-en-1-ylsulfanyl]butanoic acid
27% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-[(2E)-penta-2,4-dien-1-ylsulfanyl]butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-[(2E)-penta-2,4-dien-1-ylsulfanyl]butanoic acid
25% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-[(3-azido propyl)sulfanyl]butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-[(3-azido propyl)sulfanyl]butanoic acid
60% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-[(3-methyl butyl)sulfanyl]butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-[(3-methyl butyl)sulfanyl] butanoic acid
36% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-[(3-methylbut-2-en-1-yl)selanyl]butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-[(3-methylbut-2-en-1-yl)selanyl]butanoic acid
44% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-[(3-methylbut-2-en-1-yl)sulfanyl]butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-[(3-methylbut-2-en-1-yl)sulfanyl]butanoic acid
12% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-[(cyanomethyl) sulfanyl]butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-[(cyanomethyl)sulfanyl]butanoic acid
68% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-[(cyanomethyl)selanyl]butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-[(cyanomethyl)selanyl]butanoic acid
12% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-[[(2E)-4-aminobut-2-en-1-yl]selanyl]butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-[[(2E)-4-aminobut-2-en-1-yl]selanyl]butanoic acid
38% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-[[(2E)-4-azidobut-2-en-1-yl]selanyl]butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-[[(2E)-4-azidobut-2-en-1-yl]selanyl]butanoic acid
24% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-[[(2E)-4-azidobut-2-en-1-yl]sulfanyl]butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-[[(2E)-4-azidobut-2-en-1-yl]sulfanyl]butanoic acid
28% of the turnover rate compared to L-methionine
-
-
?
ATP + (3S)-3-amino-5-(methylthio)pentan-2-ol + H2O
phosphate + diphosphate + ?
-
-
-
?
ATP + D,L-methionine-(methyl-D3) + H2O
?
ATP + D-methionine + H2O
S-adenosyl-D-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-ethionine + H2O
phosphate + diphosphate + S-adenosyl-L-ethionine
-
-
-
?
ATP + L-ethionine + H2O
S-adenosyl-L-ethionine + phosphate + diphosphate
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
ATP + L-methionine ethyl ester + H2O
?
ATP + L-methionine methyl ester + H2O
?
ATP + L-methionine methyl ester + H2O
S-adenosyl-L-methionine methyl ester + phosphate + diphosphate
-
-
-
?
ATP + L-selenomethionine + H2O
phosphate + diphosphate + Se-adenosyl-L-selenomethionine
as active as L-methionine
-
-
?
ATP + methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
ATP + S-(-)-methioninol + H2O
?
-
-
-
?
CTP + L-methionine + H2O
S-cytosyl-L-methionine + phosphate + diphosphate
-
-
-
?
GTP + L-methionine + H2O
S-guanosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ITP + L-methionine + H2O
?
tripolyphosphate + H2O
diphosphate + phosphate
UTP + L-methionine + H2O
S-urasyl-L-methionine + phosphate + diphosphate
-
-
-
?
additional information
?
-
2'-deoxy-ATP + L-methionine + H2O
?
-
-
-
-
?
2'-deoxy-ATP + L-methionine + H2O
?
-
-
-
-
?
2'-deoxy-ATP + L-methionine + H2O
?
-
-
-
-
?
2'-deoxy-ATP + L-methionine + H2O
?
-
-
-
-
ir
2'-deoxy-ATP + L-methionine + H2O
?
-
-
-
-
?
2'-deoxy-ATP + L-methionine + H2O
?
-
-
-
-
?
2'-deoxy-ATP + L-methionine + H2O
?
-
-
-
-
?
2'-deoxy-ATP + L-methionine + H2O
?
-
-
-
-
?
2'-deoxy-ATP + L-methionine + H2O
?
-
-
-
-
?
2'-deoxy-ATP + L-methionine + H2O
?
-
-
-
-
?
2'-deoxy-ATP + L-methionine + H2O
?
-
completely specific for ATP
-
-
?
2'-deoxy-ATP + L-methionine + H2O
?
-
-
-
-
?
3'-deoxy-ATP + L-methionine + H2O
?
-
-
-
-
?
3'-deoxy-ATP + L-methionine + H2O
?
-
-
-
-
?
3'-deoxy-ATP + L-methionine + H2O
?
-
-
-
-
?
3'-deoxy-ATP + L-methionine + H2O
?
-
-
-
-
ir
3'-deoxy-ATP + L-methionine + H2O
?
-
-
-
-
?
3'-deoxy-ATP + L-methionine + H2O
?
-
-
-
-
?
3'-deoxy-ATP + L-methionine + H2O
?
-
-
-
-
?
3'-deoxy-ATP + L-methionine + H2O
?
-
-
-
-
?
3'-deoxy-ATP + L-methionine + H2O
?
-
-
-
-
?
3'-deoxy-ATP + L-methionine + H2O
?
-
-
-
-
?
3'-deoxy-ATP + L-methionine + H2O
?
-
completely specific for ATP
-
-
?
3'-deoxy-ATP + L-methionine + H2O
?
-
-
-
-
?
ATP + (2S)-2-amino-4-(but-3-yn-1-ylselanyl)butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-(but-3-yn-1-ylselanyl)butanoic acid
10% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-(but-3-yn-1-ylselanyl)butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-(but-3-yn-1-ylselanyl)butanoic acid
10% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-(but-3-yn-1-ylsulfanyl)butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-(but-3-yn-1-ylsulfanyl)butanoic acid
30% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-(but-3-yn-1-ylsulfanyl)butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-(but-3-yn-1-ylsulfanyl)butanoic acid
30% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-(butylselanyl)butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-(butylselanyl)butanoic acid
70% of the turnover rate compared to L-methionine
-
-
?
ATP + (2S)-2-amino-4-(butylselanyl)butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-(butylselanyl)butanoic acid
70% of the turnover rate compared to L-methionine
-
-
?
ATP + D,L-methionine-(methyl-D3) + H2O
?
-
-
-
-
?
ATP + D,L-methionine-(methyl-D3) + H2O
?
-
-
-
-
?
ATP + L-ethionine + H2O
S-adenosyl-L-ethionine + phosphate + diphosphate
-
-
-
?
ATP + L-ethionine + H2O
S-adenosyl-L-ethionine + phosphate + diphosphate
-
-
-
?
ATP + L-ethionine + H2O
S-adenosyl-L-ethionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
aspartate family biosynthesis pathway and methionine metabolism, regulation, S-adenosyl-L-methionine activates threonine synthase expression and negatively regulates the transcript level of the cystathionine gamma-synthase, overview
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
S-adenosylmethionine synthetase 3 is important for pollen tube growth
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
S-adenosyl-L-methionine is required for betaine synthesis and also for the synthesis of other compounds, especially lignin, transcript levels of the enzyme are co-regulated with those of phosphoethanolamine N-methyltransferase and choline monooxygenase to supply S-adenosyl-L-methionine for betaine synthesis in the leaves, overview, enzyme regulation pattern in plant tissues, overview
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
biosynthesis of the key compound in the trans-methylation reactions
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
the S(MK) box, a conserved RNA motif in the 5'-untranslated region of the metK gene, is a SAM-binding RNA responsible for translational regulation of the enzyme, it binds specifically to S-adenosyl-L-methionine in vitro and in vivo causing a structural RNA rearrangement that causes a sequestration of the Shine-Dalgarno sequence, structural mapping and mechanism, overview
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
an essential enzyme that catalyzes the formation of the principal methyl donor S-adenosylmethionine, S-adenosyl-L-methionine is also a key metabolite that regulates hepatocyte growth, death and differentiation, molecular mechanism, overview, abnormalities in MAT and decreased S-adenosyl-L-methionine levels occur in humans with alcoholic liver disease, chronic hepatic S-adenosyl-L-methionine deficiency can result in the spontaneous development of steatohepatitis and hepatocellular carcinoma, overview, hepatic S-adenosyl-L-methionine biosynthesis and methionine metabolism, overview
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
rate-limiting enzyme of the S-adenosyl-L-methionine synthesis pathway, cell methionine and S-adenosylmethionine contents increase in response to hyperoxia in SAE and A549 cells, overview
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
the enzyme is involved in S-adenosylmethionine synthesis in liver
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
a post-translational mechanism is involved in MAT regulation, the enzyme is down-regulated in pathological processes such as liver cirrhosis, overview
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
biosynthesis of S-adenosyl-L-methionine
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
two-step reaction in which reaction of ATP and methionine initially yields the S-adenosyl-L-methionine and tripolyphosphate. The tripolyphosphate remains enzyme-bound and is cleaved to diphosphate and phosphate before product release
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
biosynthesis of S-adenosyl-L-methionine
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
two-step reaction in which reaction of ATP and methionine initially yields the S-adenosyl-L-methionine and tripolyphosphate. The tripolyphosphate remains enzyme-bound and is cleaved to diphosphate and phosphate before product release
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
regulation of methionine metabolism, S-adenosyl-L-methionine metabolic pathway, overview
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
the enzyme is involved in S-adenosylmethionine synthesis in liver
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
aspartate family biosynthesis pathway and methionine metabolism,regulation, S-adenosyl-L.methionine activates threonine synthase expression and negatively regulates the transcript level of the cystathionine gamma-synthase, overview
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
the enzyme plays a key role in the biogenesis of S-adenosyl-L-methionine
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
the enzyme catalyse the biosynthesis of S-adenosylmethionine, the primary methyl group donor in biochemical reactions
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
the enzyme catalyse the biosynthesis of S-adenosylmethionine, the primary methyl group donor in biochemical reactions
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
typhus group rickettsiae have the capability of synthesizing as well as transporting SAM
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
the product S-adenosyl-L-methionine plays important roles in trans-methylation, transsulfuration, and polyamine synthesis in all living cells
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
the product S-adenosyl-L-methionine plays important roles in trans-methylation, transsulfuration, and polyamine synthesis in all living cells
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
ir
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
methyl donor in transmethylation reactions and as propylamine donor for polyamine biosynthesis
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
mechanism
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
the product S-adenosylmethionine is important as a direct metabolic donor of methyl and alpha-amino-n-butyryl groups
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
two reaction steps: S-adenosylmethionine synthesis and tripolyphosphate hydrolysis. Tripolyphosphate hydrolysis is the rate determining reaction
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
MAT activity controls cellular glutathione levels, polyamine synthesis and folate cycling
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
completely specific for ATP
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
used as aminopropyl group donor in synthesis of polyamines and is also the methyl group donor for most cellular methyltransferase reactions
-
?
ATP + L-methionine ethyl ester + H2O
?
-
excellent substrate
-
-
?
ATP + L-methionine ethyl ester + H2O
?
-
excellent substrate
-
-
?
ATP + L-methionine methyl ester + H2O
?
-
-
-
-
?
ATP + L-methionine methyl ester + H2O
?
-
-
-
-
?
ATP + methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ITP + L-methionine + H2O
?
-
-
-
?
ITP + L-methionine + H2O
?
-
-
-
?
tripolyphosphate + H2O
diphosphate + phosphate
-
-
?
tripolyphosphate + H2O
diphosphate + phosphate
-
tripolyphosphatase activity
-
?
tripolyphosphate + H2O
diphosphate + phosphate
-
tripolyphosphatase activity
-
?
tripolyphosphate + H2O
diphosphate + phosphate
-
-
?
tripolyphosphate + H2O
diphosphate + phosphate
-
tripolyphosphatase activity
-
?
tripolyphosphate + H2O
diphosphate + phosphate
-
-
-
?
tripolyphosphate + H2O
diphosphate + phosphate
-
-
-
-
?
tripolyphosphate + H2O
diphosphate + phosphate
-
tripolyphosphatase activity
-
?
tripolyphosphate + H2O
diphosphate + phosphate
-
tripolyphosphatase activity
-
?
tripolyphosphate + H2O
diphosphate + phosphate
-
tripolyphosphatase activity
-
?
tripolyphosphate + H2O
diphosphate + phosphate
-
two isoenzymes with different behavior on exogenous S-adenosylmethionine addition
-
?
additional information
?
-
-
protein S-nitrosylation by NO represents a redox-based regulation mechanism playing a pivotal role in plants, MAT catalyzes the synthesis of the ethylene precursor S-adenosylmethionine and NO influences ethylene production in plants, the enzyme probably mediates the cross-talk between ethylene and NO signaling, overview
-
-
?
additional information
?
-
-
genes in the S-box family are regulated by binding of S-adenosylmethionine to the 5' region of the mRNA of the regulated gene, SAM binding promotes a rearrangement of the RNA structure that results in premature termination of transcription in vitro and repression of expression of the downstream coding sequence, the S-box RNA element therefore acts as a SAM-binding riboswitch in vitro
-
-
?
additional information
?
-
-
N-acetyl-L-methionine and N,N-dimethyl-L-methionine are very poor substrates
-
-
?
additional information
?
-
-
ATP can be substituted by 3'-deoxy-ATP,8-bromo-ATP, formycin triphosphate, adenyl-5'yl imidodiphosphate
-
-
?
additional information
?
-
-
ATP can be substituted by 3'-deoxy-ATP,8-bromo-ATP, formycin triphosphate, adenyl-5'yl imidodiphosphate
-
-
?
additional information
?
-
S-adenosylmethionine synthesis and tripolyphosphatase activity messured for six aspartate-mutants
-
-
?
additional information
?
-
-
S-adenosylmethionine synthesis and tripolyphosphatase activity messured for six aspartate-mutants
-
-
?
additional information
?
-
S-adenosylmethionine synthesis and tripolyphosphatase activity messured for six aspartate-mutants
-
-
?
additional information
?
-
transmethylation and transsulfuration pathways, overview
-
-
?
additional information
?
-
-
transmethylation and transsulfuration pathways, overview
-
-
?
additional information
?
-
-
no activity with methional, methioninol, 3-methylthiopropylamine
-
-
?
additional information
?
-
-
N-acetyl-L-methionine and N,N-dimethyl-L-methionine are very poor substrates
-
-
?
additional information
?
-
-
S-adenosylmethionine synthetase A exhibits tripolyphosphatase activity
-
-
?
additional information
?
-
-
S-adenosylmethionine synthetase B exhibits tripolyphosphatase activity
-
-
?
additional information
?
-
the enzyme has the ability to produce a range of differentially alkylated AdoMet analogs in the presence of non-native methionine analogs and ATP
-
-
?
additional information
?
-
the enzyme has the ability to produce a range of differentially alkylated AdoMet analogs in the presence of non-native methionine analogs and ATP
-
-
?
additional information
?
-
-
ATP can be substituted by 3'-deoxy-ATP,8-bromo-ATP, formycin triphosphate, adenyl-5'yl imidodiphosphate
-
-
?
additional information
?
-
-
methionine can be substituted by selenomethionine, alpha-methyl-DL-methionine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
additional information
?
-
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
aspartate family biosynthesis pathway and methionine metabolism, regulation, S-adenosyl-L-methionine activates threonine synthase expression and negatively regulates the transcript level of the cystathionine gamma-synthase, overview
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
S-adenosylmethionine synthetase 3 is important for pollen tube growth
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
S-adenosyl-L-methionine is required for betaine synthesis and also for the synthesis of other compounds, especially lignin, transcript levels of the enzyme are co-regulated with those of phosphoethanolamine N-methyltransferase and choline monooxygenase to supply S-adenosyl-L-methionine for betaine synthesis in the leaves, overview, enzyme regulation pattern in plant tissues, overview
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
biosynthesis of the key compound in the trans-methylation reactions
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
the S(MK) box, a conserved RNA motif in the 5'-untranslated region of the metK gene, is a SAM-binding RNA responsible for translational regulation of the enzyme, it binds specifically to S-adenosyl-L-methionine in vitro and in vivo causing a structural RNA rearrangement that causes a sequestration of the Shine-Dalgarno sequence, structural mapping and mechanism, overview
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
an essential enzyme that catalyzes the formation of the principal methyl donor S-adenosylmethionine, S-adenosyl-L-methionine is also a key metabolite that regulates hepatocyte growth, death and differentiation, molecular mechanism, overview, abnormalities in MAT and decreased S-adenosyl-L-methionine levels occur in humans with alcoholic liver disease, chronic hepatic S-adenosyl-L-methionine deficiency can result in the spontaneous development of steatohepatitis and hepatocellular carcinoma, overview, hepatic S-adenosyl-L-methionine biosynthesis and methionine metabolism, overview
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
rate-limiting enzyme of the S-adenosyl-L-methionine synthesis pathway, cell methionine and S-adenosylmethionine contents increase in response to hyperoxia in SAE and A549 cells, overview
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
the enzyme is involved in S-adenosylmethionine synthesis in liver
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
a post-translational mechanism is involved in MAT regulation, the enzyme is down-regulated in pathological processes such as liver cirrhosis, overview
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
biosynthesis of S-adenosyl-L-methionine
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
biosynthesis of S-adenosyl-L-methionine
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
regulation of methionine metabolism, S-adenosyl-L-methionine metabolic pathway, overview
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
the enzyme is involved in S-adenosylmethionine synthesis in liver
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
aspartate family biosynthesis pathway and methionine metabolism,regulation, S-adenosyl-L.methionine activates threonine synthase expression and negatively regulates the transcript level of the cystathionine gamma-synthase, overview
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
the enzyme plays a key role in the biogenesis of S-adenosyl-L-methionine
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
the enzyme catalyse the biosynthesis of S-adenosylmethionine, the primary methyl group donor in biochemical reactions
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
the enzyme catalyse the biosynthesis of S-adenosylmethionine, the primary methyl group donor in biochemical reactions
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
typhus group rickettsiae have the capability of synthesizing as well as transporting SAM
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
the product S-adenosyl-L-methionine plays important roles in trans-methylation, transsulfuration, and polyamine synthesis in all living cells
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
the product S-adenosyl-L-methionine plays important roles in trans-methylation, transsulfuration, and polyamine synthesis in all living cells
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
ir
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
methyl donor in transmethylation reactions and as propylamine donor for polyamine biosynthesis
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
the product S-adenosylmethionine is important as a direct metabolic donor of methyl and alpha-amino-n-butyryl groups
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
two reaction steps: S-adenosylmethionine synthesis and tripolyphosphate hydrolysis. Tripolyphosphate hydrolysis is the rate determining reaction
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
MAT activity controls cellular glutathione levels, polyamine synthesis and folate cycling
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
used as aminopropyl group donor in synthesis of polyamines and is also the methyl group donor for most cellular methyltransferase reactions
-
?
additional information
?
-
-
protein S-nitrosylation by NO represents a redox-based regulation mechanism playing a pivotal role in plants, MAT catalyzes the synthesis of the ethylene precursor S-adenosylmethionine and NO influences ethylene production in plants, the enzyme probably mediates the cross-talk between ethylene and NO signaling, overview
-
-
?
additional information
?
-
-
genes in the S-box family are regulated by binding of S-adenosylmethionine to the 5' region of the mRNA of the regulated gene, SAM binding promotes a rearrangement of the RNA structure that results in premature termination of transcription in vitro and repression of expression of the downstream coding sequence, the S-box RNA element therefore acts as a SAM-binding riboswitch in vitro
-
-
?
additional information
?
-
transmethylation and transsulfuration pathways, overview
-
-
?
additional information
?
-
-
transmethylation and transsulfuration pathways, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2S,4S)-amino-4,5-epoxypentanoic acid
-
1-(3-(2-ethoxyphenyl)ureidoacetyl)-4-(2-methyl-5-nitrophenyl)semicarbazide
binding to adenosyl region of the active site
1-(4-chloro-2-nitrophenyl)-3-(4-sulfamoylphenyl)-urea
binding to adenosyl region of the active site
1-aminocyclopentanecarboxylic acid
-
-
1-methyluric acid
10 mM, 43.4% inhibition
1-Methylxanthine
10 mM, 35.9% inhibition
2,6-diaminopurine
10 mM, 29.3% inhibition
2,6-dichloropurine
10 mM, 35.5% inhibition
2-amino-6-carboxyethylmercaptopurine
10 mM, 31.9% inhibition
2-amino-6-chloropurine riboside
10 mM, 17.2% inhibition
2-amino-6-chloropurine-9-acetic acid
10 mM, 23.5% inhibition
2-Aminopurine
10 mM, 11.0% inhibition
2-Hydroxypurine
10 mM, 33.8% inhibition
3,7-dimethyluric acid
10 mM, 27.9% inhibition
3-morpholinosydnoniimide
-
loss of liver MAT activity in vivo
5-amino-L-norvaline
10-25% inhibition with 5 mM; 10-25% inhibition with 5 mM; 10-25% inhibition with 5 mM
5-azacytidine
-
0.2 mM leads to significant reduction of AdoMetS protein expression
6-benzyloxypurine
10 mM, 17.7% inhibition
6-bromopurine
10 mM, 31.4% inhibition
6-Chloropurine
10 mM, 31.4% inhibition
6-Chloropurine riboside
10 mM, 17.1% inhibition
6-Cyanopurine
10 mM, 24.2% inhibition
6-dimethylallylaminopurine riboside
10 mM, 41.6% inhibition
6-Dimethylaminopurine
10 mM, 28.0% inhibition
6-Mercaptopurine
10 mM, 40.1% inhibition
6-mercaptopurine riboside
10 mM, 30.0% inhibition
6-propoxypurine
10 mM, 27.9% inhibition
7-hydroxypropyl theophylline
10 mM, 16.1% inhibition
7-Methyluric acid
10 mM, 11.4% inhibition
7-methylxanthine
10 mM, 36.3% inhibition
8-aza-2,6-diaminopurine
10 mM, 40.0% inhibition
8-Azaguanine
10 mM, 81.7% inhibition
8-chlorotheophylline
10 mM, 7.0% inhibition
Adenyl-5'-ylimidodiphosphate
-
competitive with ATP
ADP
35-50% inhibition with 5 mM; 35-50% inhibition with 5 mM; 35-50% inhibition with 5 mM
alpha,beta-methylene-adenosine tetraphosphate
-
-
alpha,beta-methylene-ATP
-
-
alpha-methyl-DL-methionine
10 mM, 18.8% inhibition
AMP
causes complete inactivation of the enzyme
Azathioprine
10 mM, 75.5% inhibition
Ba2+
70.70% residual activity at 5 mM
bacterial lipopolysaccharide
-
beta,gamma-methylene-ATP
-
-
Br-
93.33% residual activity at 5 mM
carbon tetrachloride
-
depletion of glutathione levels reduces MAT I/III activities in vivo
CH3COO-
92.25% residual activity at 5 mM
Cl-
85.27% residual activity at 5 mM
Co2+
-
about 45% residual activity at 10 mM
diimidotriphosphate
mechanism
DL-2-Amino-trans-4-hexenoic acid
-
-
ethanol
25 mM ethanol substantially decreases the enzymatic activity of MAT II
Ethionine
32-38% inhibition with 5 mM; 32-38% inhibition with 5 mM; 32-38% inhibition with 5 mM
F-
88.84% residual activity at 5 mM
fluorinated N,N-dialkylaminostilbene-5
-
i.e. FIDAS
-
Fumarylacetoacetate
-
reduces MAT I/III activity
glycerol
-
inhibits kidney isoenzyme gamma
GSH
causes complete inactivation of the enzyme
I-
87.91% residual activity at 5 mM
L-2-Amino-4-hexynoic acid
-
-
L-2-Amino-4-methoxy-cis-but-3-enoic acid
L-2-Amino-4-methylthio-cis-but-3-enoic acid
-
-
L-buthionine-(S,R)-sulfoximine
L-ethioninamide
10 mM, 23.9% inhibition
L-methionine methyl ester
10 mM, 17.7% inhibition
L-methionine sulfone
10 mM, 9.2% inhibition
L-methionine sulfoxide
10 mM, 4.0% inhibition
L-methionine sulfoximine
10 mM, 12.6% inhibition
L-Penicillamine
10 mM, 15.0% inhibition
Li+
81.40% residual activity at 5 mM
methanol
2.4% methanol depresses methionine adenosyltransferase specific activity, this effect is not observed with 0.8% methanol
methylthio propionaldehyde
10 mM, 18.4% inhibition
Mg2+
-
inhibitory above 8.5 mM
N-ethylmaleimide
time-dependent inactivation of both MAT activities
Ni2+
-
about 1% residual activity at 10 mM
nitrosoglutathione
-
reversibly inhibits the isozyme MAT1 via NO binding to Cys114, no inhibition of isozymes MAT2 and MAT3, molecular mechanism for S-nitrosylation of the enzyme
NO
the enzyme is inhibited upon S-nitrosylation. S-Nitrosylation of the enzyme is mediated via several cysteine residues, including Cys52, Cys113 and Cys187. Nitrosylation is a reversible posttranslational modification upon nitrosative stress
O-methylguanine
10 mM, 60.3% inhibition
putrescine
15-25% inhibition with 5 mM; 15-25% inhibition with 5 mM; 15-25% inhibition with 5 mM
S-adenosyl-L-ethionine
-
-
S-adenosyl-L-homocysteine
S-carbamylcysteine
-
competitive with methionine
S-nitrosoglutathione monoethyl ester
-
inactivates
S-nitrosylated glutathione
-
rapid and dose-dependent loss of enzymatic activity of MAT I/III
S-Trifluoromethyl-L-homocysteine
-
-
SIN-1
-
rapid and dose-dependent loss of enzymatic activity of MAT I/III
spermidine
15-34% inhibition with 5 mM; 15-34% inhibition with 5 mM; 15-34% inhibition with 5 mM
spermine
30-40% inhibition with 5 mM; 30-40% inhibition with 5 mM; 30-40% inhibition with 5 mM
uric acid
10 mM, 45.6% inhibition
xanthine
10 mM, 35.4% inhibition
ATP
-
-
ATP
-
ATP and methionine act as a switch between two different MAT III isoforms
ATP
causes complete inactivation of the enzyme
bacterial lipopolysaccharide
-
decreases MAT activity in vivo
-
bacterial lipopolysaccharide
-
results in the accumulation of nitrites and nitrates in serum and in the inactivation of MAT I/III
-
Ca2+
-
about 5% residual activity at 10 mM
Ca2+
86.36% residual activity at 5 mM
CTP
60-70% inhibition with 5 mM; 60-70% inhibition with 5 mM; 60-70% inhibition with 5 mM
CTP
-
20 mM, 37% inhibition, S-adenosylmethionine synthetase B; 20 mM, 40% inhibition, S-adenosylmethionine synthetase A
Cu2+
-
complete inhibition at 10 mM
Cu2+
isozyme subunit MATalpha2 is inhibited by 0.25 mM Cu2+ in the presence or absence of dithiothreitol, strong reduction in MAT2B gene expression induced by Cu2+ (60%), copper effects can only be prevented by buthionine sulfoximine, whereas N-acetylcysteine and neocuproine are ineffective
Cu2+
25.74% residual activity at 5 mM
cycloleucine
-
competitive
cycloleucine
1-aminocyclopentane-1-carboxylic acid, specific MAT inhibitor
cycloleucine
10 mM, 25.8% inhibition
cycloleucine
-
25 mM, 56% inhibition, S-adenosylmethionine synthetase A; inhibits only at sub saturating concentrations of methionine
Dimethylsulfoxide
-
-
Dimethylsulfoxide
-
weak inhibition of liver isoenzyme
Dimethylsulfoxide
-
slight inhibition of gamma isoenzyme from kidney
diphosphate
-
-
diphosphate
-
inhibition for S-adenosylmethionine and L-methonine
diphosphate
-
individually a weak inhibitor, in combination with phosphate there is a marked synergistic effect
diphosphate
-
inhibits high-MW isoenzyme, no effect on low-MW enzyme
diphosphate
-
20 mM, 30% inhibition, S-adenosylmethionine synthetase A; 20 mM, 49% inhibition, S-adenosylmethionine synthetase B
Fe2+
-
about 15% residual activity at 10 mM
Fe2+
59.22% residual activity at 5 mM
GTP
not accepted as a substrate but inhibits the reaction in the presence of ATP, 70-80% inhibition with 5 mM; not accepted as a substrate but inhibits the reaction in the presence of ATP, 70-80% inhibition with 5 mM; not accepted as a substrate but inhibits the reaction in the presence of ATP, 70-80% inhibition with 5 mM
GTP
-
competitive with respect to ATP and noncompetitive with L-methionine
GTP
-
20 mM, 50% inhibition, S-adenosylmethionine synthetase B; 20 mM, 56% inhibition, S-adenosylmethionine synthetase A
hydrogen peroxide
-
reduces MAT I/III activity
hydrogen peroxide
-
inactives CHO cells-MAT, prevented by desferoxamine. Time- and dose-dependent inactivation of MAT I/III, activity recovered by addition of glutathione
K+
-
-
K+
85.27% residual activity at 5 mM
L-2-Amino-4-methoxy-cis-but-3-enoic acid
-
-
L-2-Amino-4-methoxy-cis-but-3-enoic acid
-
-
L-buthionine-(S,R)-sulfoximine
-
inhibits glutathione synthesis and this decreases MAT activity in vivo. Prevented by the administration of glutathione-ethyl ester
L-buthionine-(S,R)-sulfoximine
-
inactivates hepatic MAT, prevented by the administration of glutathione-ethyl ester
L-ethionine
-
1.2 mM leads to significant reduction of AdoMetS protein expression
L-ethionine
-
competitive with respect to methionine for S-adenosylmethionine formation and noncompetitive with respect to ATP
L-ethionine
10 mM, 20.4% inhibition
L-methionine
-
-
L-methionine
-
ATP and methionine act as a switch between two different MAT III isoforms
L-methionine
30% reduction in total activity is detected at 5 mM L-methionine; 30% reduction in total activity is detected at 5 mM L-methionine; 30% reduction in total activity is detected at 5 mM L-methionine
methylthioadenosine
-
lowers expression of MAT2A and MAT2beta
methylthioadenosine
1 mM downregulates MAT2A expression
Mn2+
-
about 80% residual activity at 10 mM
Mn2+
73.49% residual activity at 5 mM
Mn2+
-
inhibition in presence of Mg2+
Na+
80.16% residual activity at 5 mM
Na+
-
in presence of Mg2+
nitric oxide
-
two MAT III isoforms, one with low tripolyphosphatase activity that is insensitive to NO and another with high tripolyphosphatase activity that is inhibited by NO
nitric oxide
-
inactivates hepatic MAT
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
reduces MAT I/III activity
p-chloromercuribenzoate
-
alpha and beta isoenzymes completely inhibited, gamma isoenzyme slightly inhibited
phosphate
-
-
phosphate
-
competitive toward both ATP and methionine
phosphate
-
individually a weak inhibitor, in combination with diphosphate there is a synergistic inhibitory effect
phosphate
-
10 mM, 19% inhibition, S-adenosylmethionine synthetase B; 10 mM, 45% inhibition, S-adenosylmethionine synthetase A
S-adenosyl-L-homocysteine
-
-
S-adenosyl-L-homocysteine
-
not inhibitory
S-adenosyl-L-homocysteine
-
-
S-adenosyl-L-methionine
-
product inhibition. Compared with the wild-type MAT, as little as 200 mM sodium p-toluenesulfonate is required to completely overcome the product inhibition of I303V mutant enzyme on a 30 mM scale incubation
S-adenosyl-L-methionine
product inhibition
S-adenosyl-L-methionine
-
feedback inhibition of isozyme MAT II
S-adenosylmethionine
-
-
S-adenosylmethionine
-
non competitive with ATP at low methionine concentration
S-adenosylmethionine
-
lowers expression of MAT2A and MAT2beta
S-adenosylmethionine
non competitive inhibition
S-adenosylmethionine
-
more than 50% inhibition at 1 mM
S-adenosylmethionine
-
noncompetitive inhibitor with respect to ATP and methionine
S-adenosylmethionine
5 mM downregulates MAT2A expression
S-adenosylmethionine
-
inhibition of rat kidney enzyme and rat liver MAT-II, weak inhibition of rat liver MAT-I
S-adenosylmethionine
-
above 0.3 mM inhibits both high-MW and low-MW isoenzymes
S-adenosylmethionine
-
inhibits the A form but not the B form; non-competitive, S-adenosylmethionine synthetase A; slight inhibition of S-adenosylmethionine synthetase B
S-nitrosoglutathione
the enzyme is inhibited upon S-nitrosylation. S-Nitrosylation of the enzyme is not only mediated via a single cysteine but via several cysteine residues, including Cys52, Cys113 and Cys187
S-nitrosoglutathione
-
inhibits S-adenosylmethionine sinthetase activity
S-nitrosoglutathione
-
inactivates MATI/III by 70%
Tetrapolyphosphate
-
10 mM, 40% inhibition, S-adenosylmethionine synthetase B; 10 mM, 50% inhibition, S-adenosylmethionine synthetase A
tripolyphosphate
-
-
tripolyphosphate
strong inhibitor; strong inhibitor; strong inhibitor
tripolyphosphate
-
competitive with ATP
tripolyphosphate
-
competitive with ATP and non competitive with L-methionine
tripolyphosphate
-
competitive with ATP; non competitive with L-methionine
tripolyphosphate
-
activation or inhibition, depending on isoenzyme, S-adenosylmethionine and tripolyphosphate concentration
tripolyphosphate
-
1.0 mM, 57% inhibition, S-adenosylmethionine synthetase A; 1.0 mM, 62% inhibition, S-adenosylmethionine synthetase B
UTP
-
-
Zn2+
-
about 10% residual activity at 10 mM
Zn2+
22.17% residual activity at 5 mM
additional information
addition of reducing agents has no effect; addition of reducing agents has no effect; addition of reducing agents has no effect
-
additional information
addition of reducing agents has no effect; addition of reducing agents has no effect; addition of reducing agents has no effect
-
additional information
addition of reducing agents has no effect; addition of reducing agents has no effect; addition of reducing agents has no effect
-
additional information
-
addition of reducing agents has no effect; addition of reducing agents has no effect; addition of reducing agents has no effect
-
additional information
-
overview of the regulatory properties, effect of L-methionine analogues and influence of L-methionine concentration on activating and inhibiting effects, effect of tripolyphosphate and p-hydroxymercuribenzoate
-
additional information
-
reactive oxygen and nitrogen species induce the inactivation of MAT I/III
-
additional information
-
no inhibition with cycloleucine, L-homocysteine, L-norleucine, L-cis-2-amino-4-methoxy-3-butenoic acid, S-adenosylhomocysteine, 5'-methylthioadenosine, sinefungin
-
additional information
not inhibitory: (R)-methioninol, 1,3,7-trimethyluric acid, 6-methylpurine
-
additional information
-
not inhibitory: (R)-methioninol, 1,3,7-trimethyluric acid, 6-methylpurine
-
additional information
-
MAT is inactivated after 6 h of incubation in hypoxia (3% O2) in rat hepatocytes, prevented by NG-monomethyl-L-arginine methyl ester. Hepatic MAT s a sensible target for free radicals in vivo
-
additional information
-
S-adenosyl(5')-3-methylthiopropylamine does not inhibit
-
additional information
no effect on activity at 0.1 mM Ni2+
-
additional information
-
no effect on activity at 0.1 mM Ni2+
-
additional information
-
overexpression of yeast AdoMet synthase plus cap guanine-N7 methyltransferase affords greater resistance to sinefungin than either enzyme alone
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0056 - 0.74
L-ethionine
0.0023 - 3.3
L-methionine
2.6
L-methionine methyl esther
-
-
0.3
MgATP2-
-
ATP in form of MgATP2-
0.39 - 2.4
S-(-)-methioninol
0.0013 - 0.026
tripolyphosphate
additional information
additional information
-
0.002
ATP
-
beta form from liver
0.005
ATP
-
alpha form from liver
0.01
ATP
pH 8, 37°C, mutant enzyme I303V/I65V/L186V
0.01
ATP
pH 8, 37°C, mutant enzyme I303V/I65V/L186V/N104K
0.0145
ATP
pH 8.0, 65°C, cosubstrate: L-methionine
0.026
ATP
G6 mutant, S-adenosylmethionine synthesis
0.045
ATP
RLL and G8 mutants, S-adenosylmethionine synthesis
0.05
ATP
pH 8, 37°C, mutant enzyme I303V/I65V
0.0592
ATP
pH 8.0, 65°C, cosubstrate: L-ethionine
0.065
ATP
-
S-adenosylmethionine synthetase A
0.0686
ATP
pH 8.0, 37°C, cosubstrate: L-methionine
0.069
ATP
G7 mutants, S-adenosylmethionine synthesis
0.073
ATP
wild-type S-adenosylmethionine synthesis
0.083
ATP
wild-type, pH 8.0
0.087
ATP
G5 mutant S-adenosylmethionine synthesis
0.0969
ATP
pH 8.0, 37°C, cosubstrate: L-ethionine
0.1
ATP
mutant W387F/Y170W, 55°C
0.1
ATP
mutant W387F/Y226W, 55°C
0.1
ATP
pH 8, 37°C, mutant enzyme I303V
0.11
ATP
mutant W387F, 55°C
0.11
ATP
mutant W387F/Y371W, 55°C
0.11
ATP
mutant W387F/Y72W, 55°C
0.13
ATP
mutant D107C, pH 8.0
0.13
ATP
mutant G105C, pH 8.0
0.13
ATP
mutant W387F/Y120W, 55°C
0.156
ATP
-
S-adenosylmethionine synthetase B
0.17
ATP
pH 8, 37°C, wild-type enzyme
0.176
ATP
pH 8.4, 37°C, mutant enzyme
0.18
ATP
mutant G105R1, pH 8.0
0.18
ATP
mutant W387F/Y49W, 55°C
0.19
ATP
mutant W387F/Y255W, 55°C
0.2
ATP
mutant W387F/Y233W, 55°C
0.2
ATP
mutant W387F/Y267W, 55°C
0.206
ATP
pH 8.4, 37°C, mutant enzyme
0.21
ATP
mutant W387F/Y85W, 55°C
0.22
ATP
-
saturated with KCl
0.22
ATP
mutant W387F/Y323W, 55°C
0.22
ATP
mutant W387F/Y344W, 55°C
0.24
ATP
mutant W387F/Y273W, 55°C
0.34
ATP
-
37°C, pH 8.0, mutant enzyme I303V
0.43
ATP
-
37°C, pH 8.0, wild-type enzyme
0.493
ATP
mutant C35S, presence of dithiothreitol
0.53
ATP
wild-type, presence of glutathione
0.588
ATP
wild-type, presence of dithiothreitol
0.631
ATP
at pH 8.0 and 35°C
0.68
ATP
pH 8.4, 37°C, mutant enzyme
0.778
ATP
mutant C35S, presence of glutathione
0.92
ATP
in 100 mM Tris-Cl pH 8.0, 20 mM MgCl2, at 37°C
1.72
ATP
-
at pH 8.5 and 45°C
2.07
ATP
at pH 8.5 and 35°C
2.54
ATP
mutant C61S, presence of glutathione
2.84
ATP
-
at pH 8.5 and 40°C
3.25
ATP
mutant C61S, presence of dithiothreitol
4.19
ATP
at pH 8.0 and 70°C
6.54
ATP
-
at pH 8.0 and 37°C
0.0056
L-ethionine
pH 8.0, 37°C
0.007
L-ethionine
pH 8.0, 65°C
0.0023
L-methionine
pH 8.0, 37°C
0.0028
L-methionine
pH 8.0, 65°C
0.0061
L-methionine
-
pH 7.0, 37°C
0.0075
L-methionine
-
erythrocyte extract, alpha and beta subunit
0.01
L-methionine
-
isoenzyme A
0.01
L-methionine
-
S-adenosylmethionine synthetase A
0.0125
L-methionine
-
erythrocyte extract, alpha subunit
0.015
L-methionine
-
endogenous MAT II
0.016
L-methionine
-
alpha2-transfected MAT II, two kinetic forms
0.017
L-methionine
-
alpha form from liver
0.02
L-methionine
-
isoenzyme B
0.02
L-methionine
-
recombinant MAT II co-expressing alpha2 and beta subunits
0.022
L-methionine
-
crude extract
0.022
L-methionine
one kinetic form of alpha-two subunit in the presence of beta subunit
0.022 - 0.024
L-methionine
-
ro subunit
0.024
L-methionine
-
wild-type
0.024
L-methionine
-
S-adenosylmethionine synthetase B
0.03
L-methionine
mutant D249N, pH 8.0
0.03 - 0.038
L-methionine
-
one kinetic form of alpha subunit in the presence of beta subunit
0.031
L-methionine
pH 8.0, 80°C
0.034
L-methionine
pH 8.4, 37°C
0.036
L-methionine
mutant D166N, pH 8.0
0.038
L-methionine
mutant D19N, presence of 0.05 mM S-adenosyl methionine, pH 8.0
0.04
L-methionine
wild-type, pH 8.0
0.041
L-methionine
-
MAT-I isoenzyme
0.041
L-methionine
mutant K280A, pH 8.0
0.043
L-methionine
pH 8.4, 37°C, mutant enzyme
0.045
L-methionine
mutant D121N, presence of 0.05 mM S-adenosyl methionine, pH 8.0
0.046
L-methionine
pH 8.4, 37°C, mutant enzyme
0.047
L-methionine
pH 8.0, 37°C, mutant enzyme Q113D
0.05
L-methionine
mutant D249N, presence of 0.05 mM S-adenosyl methionine, pH 8.0
0.051
L-methionine
pH 8.4, 37°C, mutant enzyme
0.06
L-methionine
-
uninduced E. coli NM522 strain extract alpha subunit at low L-methionine concentrations
0.06 - 0.1
L-methionine
alpha-two subunit
0.065 - 0.08
L-methionine
-
alpha subunit at low L-methionine concentrations
0.074
L-methionine
mutant K280A, presence of 0.05 mM S-adenosyl methionine, pH 8.0
0.075
L-methionine
-
alpha2-transfected MAT II, two kinetic forms
0.076
L-methionine
one kinetic form of alpha-two subunit in the presence of beta subunit
0.078
L-methionine
pH 8.0, 37°C, mutant enzyme K289L
0.08
L-methionine
-
S283T mutant
0.08
L-methionine
-
induced E. coli NM522 strain extract alpha subunit at low L-methionine concentrations and uninduced E. coli NM522 strain extract alpha subunit at high L-methionine concentrations
0.08
L-methionine
pH 8, 37°C, wild-type enzyme
0.08 - 0.09
L-methionine
-
alpha subunit at high L-methionine concentrations. Also one kinetic form of alpha subunit in the presence of beta subunit
0.088
L-methionine
-
Q113A mutant, S-adenosylmethionine synthesis
0.092
L-methionine
wild-type, S-adenosylmethionine synthesis
0.096
L-methionine
-
pH 8.2, 37°C
0.11
L-methionine
pH 8.0, 37°C
0.11
L-methionine
wild-type, pH 8.0
0.12
L-methionine
-
pH 8.0, 37°C
0.12
L-methionine
-
37°C, pH 8.0, mutant enzyme I303V
0.13
L-methionine
mutant W387F/Y323W, 55°C
0.13
L-methionine
mutant W387F/Y72W, 55°C
0.137
L-methionine
mutant D282N, presence of 0.05 mM S-adenosyl methionine, pH 8.0
0.137
L-methionine
mutant H17N, presence of 0.05 mM S-adenosyl methionine, pH 8.0
0.14
L-methionine
pH 8.0, 37°C, wild-type enzyme
0.14
L-methionine
pH 8.0, 58°C
0.141
L-methionine
mutant D282N, pH 8.0
0.147
L-methionine
mutant D166N, presence of 0.05 mM S-adenosyl methionine, pH 8.0
0.17
L-methionine
mutant K256A, pH 8.0
0.17
L-methionine
mutant K256A, presence of 0.05 mM S-adenosyl methionine, pH 8.0
0.17
L-methionine
pH 8, 37°C, mutant enzyme I303V/I65V/L186V/N104K
0.176
L-methionine
mutant H17A, presence of 0.05 mM S-adenosyl methionine, pH 8.0
0.18
L-methionine
mutant D107R1, pH 8.0
0.18
L-methionine
-
37°C, pH 8.0, wild-type enzyme
0.19
L-methionine
mutant D107R1, pH 8.0
0.2
L-methionine
-
induced E. coli NM522 strain extract alpha subunit at high L-methionine concentrations
0.215
L-methionine
-
MAT-III isoenzyme
0.22
L-methionine
-
wild-type
0.23
L-methionine
RLL mutant, S-adenosylmethionine synthesis
0.25
L-methionine
mutant W387F/Y371W, 55°C
0.26
L-methionine
in 100 mM Tris-Cl pH 8.0, 20 mM MgCl2, at 37°C
0.287
L-methionine
wild-type, presence of 0.05 mM S-adenosyl methionine, pH 8.0
0.288
L-methionine
37°C, pH 8.2
0.29
L-methionine
mutant D107C, pH 8.0
0.3
L-methionine
G6 mutant, S-adenosylmethionine synthesis
0.3
L-methionine
-
saturated with KCl
0.3
L-methionine
mutant W387F/Y226W, 55°C
0.3
L-methionine
mutant W387F/Y273W, 55°C
0.3
L-methionine
pH 8, 37°C, mutant enzyme I303V/I65V/L186V
0.31
L-methionine
-
at pH 8.0 and 37°C
0.31
L-methionine
mutant W387F, 55°C
0.31
L-methionine
wild-type, 55°C
0.33
L-methionine
mutant W387F/Y344W, 55°C
0.42
L-methionine
pH 8, 37°C, mutant enzyme I303V
0.43
L-methionine
pH 8, 37°C, mutant enzyme I303V/I65V
0.45
L-methionine
mutant G105C, pH 8.0
0.45
L-methionine
mutant W387F/Y267W, 55°C
0.47
L-methionine
mutant W387F/Y233W, 55°C
0.49
L-methionine
G7 mutant, S-adenosylmethionine synthesis
0.5
L-methionine
mutant W387F/Y255W, 55°C
0.51
L-methionine
at pH 8.5 and 35°C
0.527
L-methionine
at pH 8.0 and 35°C
0.54
L-methionine
mutant W387F/Y120W, 55°C
0.57
L-methionine
mutant W387F/Y85W, 55°C
0.62
L-methionine
G8 mutant, S-adenosylmethionine synthesis
0.66
L-methionine
mutant W387F/Y49W, 55°C
0.75
L-methionine
mutant G105R1, pH 8.0
0.77
L-methionine
G5 mutant, S-adenosylmethionine synthesis
0.85
L-methionine
-
at pH 8.5 and 45°C
1
L-methionine
mutant W387F/Y170W, 55°C
1.2
L-methionine
at pH 8.0 and 70°C
1.47
L-methionine
-
at pH 8.5 and 40°C
0.0083
methionine
-
MAT-II isoenzyme
0.222
methionine
mutant C35S, presence of dithiothreitol
0.246
methionine
wild-type, presence of dithiothreitol
0.449
methionine
mutant C35S, presence of glutathione
0.5
methionine
-
beta form from liver
0.756
methionine
mutant C61S, presence of dithiothreitol
0.794
methionine
mutant C61S, presence of glutathione
1.12
methionine
wild-type, presence of glutathione
0.006
Mg2+
-
alpha form from liver
0.007
Mg2+
-
beta form from liver
0.39
S-(-)-methioninol
pH 8.0, 37°C, mutant enzyme Q113D
1
S-(-)-methioninol
pH 8.0, 37°C, mutant enzyme K289L
2.4
S-(-)-methioninol
pH 8.0, 37°C, wild-type enzyme
0.0013
tripolyphosphate
wild type, tripolyphosphatase activity, in the presence of 0.1 mM of S-adenosylmethionine
0.0015
tripolyphosphate
G7 mutant, tripolyphosphatase activity, in absence of S-adenosylmethionine
0.0016
tripolyphosphate
G8 mutant, tripolyphosphatase activity, in absence of S-adenosylmethionine
0.003
tripolyphosphate
wild type, tripolyphosphatase activity, in absence of S-adenosylmethionine
0.0032
tripolyphosphate
G6 mutant, tripolyphosphatase activity, in absence of S-adenosylmethionine
0.0053
tripolyphosphate
G5 mutant, tripolyphosphatase activity, in absence of S-adenosylmethionine
0.008
tripolyphosphate
G8 mutant, tripolyphosphatase activity, in the presence of 0.1 mM of S-adenosylmethionine
0.011
tripolyphosphate
G6 mutant, tripolyphosphatase activity, in the presence of 0.1 mM of S-adenosylmethionine
0.014
tripolyphosphate
RLL mutant, tripolyphosphatase activity, in absence of S-adenosylmethionine
0.015
tripolyphosphate
G7 mutant, tripolyphosphatase activity, in the presence of 0.1 mM of S-adenosylmethionine
0.024
tripolyphosphate
G5 mutant, tripolyphosphatase activity, in the presence of 0.1 mM of S-adenosylmethionine
0.026
tripolyphosphate
RLL mutant, tripolyphosphatase activity, in the presence of 0.1 mM of S-adenosylmethionine
additional information
additional information
-
high performance liquid chromatography assay method using catechol-O-methyltransferase-coupled fluorometric detection, negative cooperativity of enzyme with Hill coefficinet of 0.5
-
additional information
additional information
-
different isoforms of MAT differ in kinetic and regulatory properties, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
structures of catalytic cycle intermediates of the Pyrococcus furiosus methionine adenosyltransferase demonstrate negative cooperativity in the archaeal orthologues. The distinct molecular mechanism for S-adenosylmethionine synthesis in Archaea is likely consequence of the evolutionary pressure to achieve protein stability under extreme conditions
evolution
-
structures of catalytic cycle intermediates of the Pyrococcus furiosus methionine adenosyltransferase demonstrate negative cooperativity in the archaeal orthologues. The distinct molecular mechanism for S-adenosylmethionine synthesis in Archaea is likely consequence of the evolutionary pressure to achieve protein stability under extreme conditions
-
malfunction
-
addition of the methionine adenosyltransferase (MAT2A) inhibitor FIDAS to the culture media of bovine preimplantation embryos reduces their blastocyst development
malfunction
depletion of S-adenosylmethionine has downstream effects on polyamine metabolism and methylation reactions, and is an effective way to combat pathogenic microorganisms such as malaria parasites
malfunction
knocking down MAT1A or overexpressing MafG or c-Maf enhances cholangiocarcinoma growth and invasion in vivo
malfunction
knocking down MAT1A or overexpressing MafG or c-Maf enhances cholangiocarcinoma growth and invasion in vivo
malfunction
mat3 mutants have impaired pollen tube growth and reduced seed set. Metabolomics analyses confirms that mat3 pollen and pollen tubes overaccumulate Met and that mat3 pollen has several metabolite profiles, such as those of polyamine biosynthesis, which are different from those of the wild type. Disruption of Met metabolism in mat3 pollen affects transfer RNA and histone methylation levels
malfunction
mat4 mostly decreases CHG and CHH DNA methylation and histone H3K9me2 and reactivates certain silenced transposons. The exogenous addition of S-adenosyl-L-methionine partially rescues the epigenetic defects of mat4. MAT4 knockout mutations generated by CRISPR/Cas9 are lethal, indicating that MAT4 is an essential gene in Arabidopsis
malfunction
sam1 mutants lose viability during nitrogen starvation-induced G0 phase quiescence. After release from the G0 state, sam1 mutants could neither increase in cell size nor re-initiate DNA replication in the rich medium
malfunction
-
sam1 mutants lose viability during nitrogen starvation-induced G0 phase quiescence. After release from the G0 state, sam1 mutants could neither increase in cell size nor re-initiate DNA replication in the rich medium
-
metabolism
the enzyme plays a key role in the biogenesis of S-adenosyl-L-methionine
metabolism
as a methyl group donor for biochemical reactions, the product S-adenosylmethionine plays a central metabolic role in most organisms
metabolism
methionine adenosyltransferase IIalpha (MAT IIalpha) is a key enzyme in methionine metabolism and is associated with uncontrolled cell proliferation in cancer
metabolism
S-adenosyl-L-methionine (AdoMet) is the primary methyl donor in most biological methylation reactions, is produced from ATP and methionine in a multistep reaction catalyzed by AdoMet synthetase. The diversity of group transfer reactions that involve AdoMet places this compound at a key crossroads in amino-acid, nucleic acid and lipid metabolism
metabolism
the enzyme catalyse the biosynthesis of S-adenosylmethionine, the primary methyl group donor in biochemical reactions
metabolism
the enzyme catalyzes the synthesis of S-adenosyl-Met in the one-carbon metabolism cycle. MAT4 plays a predominant role in SAM production, plant growth, and development
metabolism
-
the enzyme is involved in folate-mediated one-carbon metabolism which is essential for preimplantation embryos in terms of both short-term periconceptional development and long-term phenotypic programming beyond the periconceptional period. Particular importance of the enzyme (MAT2A) in successful blastocyst development. Critical involvement of the enzyme (MAT2A) in the periconceptional period in life-long programming of health and disease as well as successful preimplantation development
metabolism
the enzyme is involved in S-adenosylmethionine synthesis in liver. MATalpha1 interacts mainly with Mnt in normal liver but this switches to c-Maf, MafG and c-Myc in cholestatic livers and cholangiocarcinoma. Knocking down MAT1A or overexpressing MafG or c-Maf enhances cholangiocarcinoma growth and invasion in vivo
metabolism
the enzyme is involved in S-adenosylmethionine synthesis in liver. MATalpha1 interacts mainly with Mnt in normal liver but this switches to c-Maf, MafG and c-Myc in cholestatic livers and cholangiocarcinoma. Knocking down MAT1A or overexpressing MafG or c-Maf enhances cholangiocarcinoma growth and invasion in vivo
metabolism
the product S-adenosyl-L-methionine plays important roles in trans-methylation, transsulfuration, and polyamine synthesis in all living cells
metabolism
the product S-adenosylmethionine serves as the methyl donor in most methyl transfer reactions, including methylation of proteins, nucleic acids, and lipids. The enzyme is required for cell growth and proliferation, and maintenance of and exit from quiescence
metabolism
-
the product S-adenosyl-L-methionine plays important roles in trans-methylation, transsulfuration, and polyamine synthesis in all living cells
-
metabolism
-
the product S-adenosylmethionine serves as the methyl donor in most methyl transfer reactions, including methylation of proteins, nucleic acids, and lipids. The enzyme is required for cell growth and proliferation, and maintenance of and exit from quiescence
-
metabolism
-
the enzyme catalyse the biosynthesis of S-adenosylmethionine, the primary methyl group donor in biochemical reactions
-
metabolism
-
S-adenosyl-L-methionine (AdoMet) is the primary methyl donor in most biological methylation reactions, is produced from ATP and methionine in a multistep reaction catalyzed by AdoMet synthetase. The diversity of group transfer reactions that involve AdoMet places this compound at a key crossroads in amino-acid, nucleic acid and lipid metabolism
-
physiological function
doxorubicin production by the metK1-sp-deleted mutant is reduced
physiological function
-
MAT2A or MAT2beta silencing results in decreased collagen and alpha-smooth muscle actin expression and cell growth and increased apoptosis. MAT2A knockdown decreases intracellular S-adenosylmethionine levels in LX-2 cells. Activation of extracellular signal-regulated kinase and phosphatidylinositol-3-kinase signaling in LX-2 cells requires the expression of MAT2 but not that of MAT2A
physiological function
-
MAT2A silencing in primary heaptic stellate cells results in decreased collagen and alpha-smooth muscle actin expression and cell growth and increased apoptosis
physiological function
the enzyme is involved in biosynthesis of S-adenosyl-L-methionine
physiological function
enzyme overexpression is positively correlated with polyamine and hydrogen peroxide accumulation leading to improve alkali stress tolerance
physiological function
enzyme overexpression promotes polyamine synthesis and oxidation, which in turn improves H2O2-induced antioxidant protection, as a result enhances tolerance to freezing and chilling stress in transgenic plants
physiological function
transgenic tomato plants overexpressing SAMS1 exhibit a significant increase in tolerance to alkali stress and maintained nutrient balance, higher photosynthetic capacity and lower oxidative stress compared with wild type lines
physiological function
methionine adenosyltransferase IIalpha (MAT IIalpha) is a key enzyme in methionine metabolism and is associated with uncontrolled cell proliferation in cancer
physiological function
S-adenosylmethionine synthetase 3 is important for pollen tube growth
physiological function
-
the enzyme is involved in the mechanism of cold tolerance by controlling plant cell wall thickness
physiological function
-
the enzyme is involved in biosynthesis of S-adenosyl-L-methionine
-
physiological function
-
the enzyme is involved in the mechanism of cold tolerance by controlling plant cell wall thickness
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
I105A/I317A
-
the conversion of the natural substrate methionine is reduced in this mutant
I105V/I317A
-
the conversion of the natural substrate methionine is reduced in this mutant
I105A/I317A
-
the conversion of the natural substrate methionine is reduced in this mutant
-
I105V/I317A
-
the conversion of the natural substrate methionine is reduced in this mutant
-
H145Y
spontaneous mutant, excretes a large amount of a red compound identified as coproporphyrin III. The mutant is able to grow under phototrophic conditions but has low levels of intracellular cysteine and glutathione and overexpresses the cysteine synthase CysK. The wild-type phenotype is restored when the gene metK encoding SAM synthetase is supplied in trans. The mutation is responsible for a 70% decrease in intracellular SAM content which probably affects the activities of numerous SAM-dependent enzymes such as coproporphyrinogen oxidase, uroporphyrinogen III methyltransferase, and molybdenum cofactor biosynthesis protein A
D107C
enzyme activity similar to wild-type, attachment of methanethiosulfonate spin label to form D107R1, increase in Km-value, decrease in kcat value
G105C
enzyme activity similar to wild-type, attachment of methanethiosulfonate spin label to form G105R1, increase in Km-value
I303V
-
the Km-values for both substrates are slightly less than those of the wild-type enzyme. The variant is successfully produced at a high level (about 800 mg/l) with approximately four-fold higher specific activity than the wild-type enzyme. The recombinant mutant enzyme is covalently immobilized onto the amino resin and epoxy resin in order to obtain a robust biocatalyst to be used in industrial bioreactors. The immobilized preparation using amino resin exhibits the highest activity coupling yield (about 84%), compared with approximately 3% for epoxy resin. The immobilized mutant enzyme is more stable than the soluble enzyme under the reactive conditions, with a half-life of 229.5 h at 37 °C. The Km(ATP) value (0.18 mM) of the immobilized mutant enzyme is about two-fold lower than that of the soluble enzyme. The immobilized enzyme shows high operational stability during 10 consecutive 8 h batches, with the substrate adenosine triphosphate conversion rate above 95% on the 50 mM scale. Compared with the wild-type enzyme, as little as 200 mM sodium p-toluenesulfonate is required to completely overcome the product inhibition by S-adenosyl-L-methionine of I303V mutant enzyme on a 30 mM scale incubation
I303V/I65V/L186V
product inhibition of the enzyme is reduced via semi-rational modification. The mutant enzyme shows a 42fold increase in Ki(ATP) and a 2.08fold increase in specific activity when compared to wild-type enzyme. Its Ki(ATP) is 0.42 mM and specific acitivity is 3.78 U/mg. Increased Ki(ATP) means reduced product inhibition which enhances accumulation of S-adenosyl-L-methionine. The S-adenosyl-L-methionine produced by the variant could reach to 3.27 mM while S-adenosyl-L-methionine produced by wild-type enzyme is 1.62 mM in the presence of 10 mM substrates
I303V/I65V/L186V/N104K
product inhibition of the enzyme is reduced via semi-rational modification. The mutant enzyme shows a 3.3fold increase in specific activity when compared to wild-type enzyme. Specific acitivity of the mutant enzyme is 6.02 U/mg. Increased Ki(ATP) means reduced product inhibition which enhances accumulation of S-adenosyl-L-methionine. The S-adenosyl-L-methionine produced by the variant could reach to 2.68 mM while S-adenosyl-L-methionine produced by wild-type enzyme is 1.62 mM in the presence of 10 mM substrates
I303V
-
the Km-values for both substrates are slightly less than those of the wild-type enzyme. The variant is successfully produced at a high level (about 800 mg/l) with approximately four-fold higher specific activity than the wild-type enzyme. The recombinant mutant enzyme is covalently immobilized onto the amino resin and epoxy resin in order to obtain a robust biocatalyst to be used in industrial bioreactors. The immobilized preparation using amino resin exhibits the highest activity coupling yield (about 84%), compared with approximately 3% for epoxy resin. The immobilized mutant enzyme is more stable than the soluble enzyme under the reactive conditions, with a half-life of 229.5 h at 37 °C. The Km(ATP) value (0.18 mM) of the immobilized mutant enzyme is about two-fold lower than that of the soluble enzyme. The immobilized enzyme shows high operational stability during 10 consecutive 8 h batches, with the substrate adenosine triphosphate conversion rate above 95% on the 50 mM scale. Compared with the wild-type enzyme, as little as 200 mM sodium p-toluenesulfonate is required to completely overcome the product inhibition by S-adenosyl-L-methionine of I303V mutant enzyme on a 30 mM scale incubation
-
I303V/I65V/L186V
-
product inhibition of the enzyme is reduced via semi-rational modification. The mutant enzyme shows a 42fold increase in Ki(ATP) and a 2.08fold increase in specific activity when compared to wild-type enzyme. Its Ki(ATP) is 0.42 mM and specific acitivity is 3.78 U/mg. Increased Ki(ATP) means reduced product inhibition which enhances accumulation of S-adenosyl-L-methionine. The S-adenosyl-L-methionine produced by the variant could reach to 3.27 mM while S-adenosyl-L-methionine produced by wild-type enzyme is 1.62 mM in the presence of 10 mM substrates
-
I303V/I65V/L186V/N104K
-
product inhibition of the enzyme is reduced via semi-rational modification. The mutant enzyme shows a 3.3fold increase in specific activity when compared to wild-type enzyme. Specific acitivity of the mutant enzyme is 6.02 U/mg. Increased Ki(ATP) means reduced product inhibition which enhances accumulation of S-adenosyl-L-methionine. The S-adenosyl-L-methionine produced by the variant could reach to 2.68 mM while S-adenosyl-L-methionine produced by wild-type enzyme is 1.62 mM in the presence of 10 mM substrates
-
A55D
the mutation reduces the enzyme activity by more than 50%
D258G
the mutation reduces the enzyme activity by more than 50%
E70S
the mutant enzyme lacks appreciable activity in the presence of non-native methionine surrogates (3.2% S-(-)-methioninol, 240 min versus 25% L-Met, 20 min)
I322M
the mutation reduces the enzyme activity by more than 50%
K289F
the mutant enzyme lacks selectivity (33% (3S)-3-amino-5-(methylthio)pentan-2-ol versus 30% L-Met, 240 min)
K289L
160fold inversion of the enzyme (hMAT2A) selectivity index for a non-native methionine analogue over the native substrate L-methionine. Structure elucidation of K289L reveales the mutant to be folded normally with minor observed repacking within the modified substrate pocket. It is an example of exchanging L-Met terminal carboxylate/amine recognition elements within the hMAT2A active-site to enable non-native bioorthgonal substrate utilization
K289S
mutant displays selectivity toward (3S)-3-amino-5-(methylthio)pentan-2-ol (38%, 240 min) over L-Met (14%, 240 min)
K289T
mutant displays selectivity toward (3S)-3-amino-5-(methylthio)pentan-2-ol (14%, 240 min) over L-Met (2.5%, 240 min)
Q113D
mutant displays selectivity toward (3S)-3-amino-5-(methylthio)pentan-2-ol (39%, 240 min) over L-Met (13%, 240 min)
R264H
the mutation almost completely abolishes enzyme activity
D121N
no basal enzymic activity, little activity in presence of S-adenosyl methionine
D166N
reduced enzymic activity, little activation by S-adenosyl methionine
D19N
no basal enzymic activity, little activity in presence of S-adenosyl methionine
D249N
reduced enzymic activity, little activation by S-adenosyl methionine
D277N
no enzymic activity
D282N
reduced enzymic activity, little activation by S-adenosyl methionine
F241A
no enzymic activity, but hydrolysis of triphosphate
H17A
no basal enzymic activity, little activity in presence of S-adenosyl methionine
H17N
no basal enzymic activity, little activity in presence of S-adenosyl methionine
K168A
no enzymic activity
K256A
no activation by S-adenosyl methionine
K276A
no enzymic activity
K280A
enhanced enzymic activity, little activation by S-adenosyl methionine
R255L
no enzymic activity
W387F
-
the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme exhibits two inactivation transitions in guanidinium chloride
-
W387F/Y120W
-
the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Lower resistance to guanidinium chloride than the wild type enzyme
-
W387F/Y49W
-
the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme shows a single inactivation transition
-
W387F/Y72W
-
the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme and mutant enzyme W387F/Y72W in guanidinium chloride is a three-state process. Lower resistance to guanidinium chloride than the wild type enzyme
-
W387F/Y85W
-
the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme exhibits two inactivation transitions in guanidinium chloride
-
C113S
compared with the wild type enzyme the mutant enzyme is only weakly activated by PfTrx1. The mutation significantly decreases the affinity to the substrate L-methionine. The mutant enzyme shows higher affinity towards ATP when compared with the wild type
C187S
with regard to specific activity the mutant enzyme does not show major differences compared with the wild type enzyme. The mutant enzyme shows higher affinity towards ATP when compared with the wild type
C52S
compared with the wild type enzyme the mutant enzyme is only weakly activated by PfTrx1. With regard to specific activity the mutant enzyme does not show major differences compared with the wild type enzyme. The mutation significantly decreases the affinity to the substrate L-methionine and ATP
C35S
reduction in Vmax value
C61S
reduction in Vmax value
F251D
-
inactive, but displays correct nuclear localization and matrix binding
W387F
kinetic data
W387F
the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme exhibits two inactivation transitions in guanidinium chloride
W387F/Y120W
kinetic data
W387F/Y120W
the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Lower resistance to guanidinium chloride than the wild type enzyme
W387F/Y170W
kinetic data
W387F/Y170W
the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Lower resistance to guanidinium chloride than the wild type enzyme
W387F/Y226W
kinetic data
W387F/Y226W
the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Lower resistance to guanidinium chloride than the wild type enzyme
W387F/Y233W
4.9fold increase in kcat value. Mutant shows three transitions in urea titration curve, contrary to two transitions of wild-type
W387F/Y233W
the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Lower resistance to guanidinium chloride than the wild type enzyme
W387F/Y255W
fluorescence intensity reduced to 18% of wild-type
W387F/Y255W
the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Lower resistance to guanidinium chloride than the wild type enzyme
W387F/Y267W
kinetic data
W387F/Y267W
the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Lower resistance to guanidinium chloride than the wild type enzyme
W387F/Y273W
kinetic data
W387F/Y273W
the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme exhibits two inactivation transitions in guanidinium chloride. Lower resistance to guanidinium chloride than the wild type enzyme
W387F/Y323W
kinetic data
W387F/Y323W
the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme shows a delayed first transition
W387F/Y344W
kinetic data
W387F/Y344W
the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme shows a single inactivation transition
W387F/Y371W
shows one transition in urea titration curve, contrary to two transitions of wild-type
W387F/Y371W
the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme shows a delayed first transition
W387F/Y49W
decrease in kcat value by 32%
W387F/Y49W
the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme shows a single inactivation transition
W387F/Y72W
kinetic data
W387F/Y72W
the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme and mutant enzyme W387F/Y72W in guanidinium chloride is a three-state process. Lower resistance to guanidinium chloride than the wild type enzyme
W387F/Y85W
kinetic data
W387F/Y85W
the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme exhibits two inactivation transitions in guanidinium chloride
additional information
-
a single mutant metK10 with one nucleotide substitution in the metK gene resulting in a 15fold decrease in SAM synthetase activity and a 4fold decrease in SAM concentration in vivo, the metK10 mutation specifically affects S-box gene expression, and the increase in expression under repressing conditions is dependent on the presence of a functional transcriptional antiterminator element, phenotype, overview
additional information
-
mutational analysis and structural mapping of the the S(MK) box, conserved RNA motif in the 5'-untranslated region of the metK gene, overview
additional information
mutants D107R1, D105R1, derived from mutants D107C, D105C, by addition of methanethiosulfonate spin label
additional information
-
construction of a metK deletion mutant strain MOB1490 from wild-type strain BW25113, complementation by wild-type gene metK, as well as by genes metK from Rickettsia prowazekii and Rickettsia typhi, overview
additional information
recombination of MAT genes from Escherichia coli, Saccharomyces cerevisiae, and Streptomyces spectabilis by DNA shuffling and transformation into Pichia pastoris. In the two best recombinant strains, the MAT activities are respectively 201% and 65% higher than the recombinant strains containing the starting MAT genes, and the SAM concentration increases by 103% and 65%, respectively. A 6.14 g/l of SAM production is reached in a 500 l bioreactor with the best recombinant strain
additional information
-
recombination of MAT genes from Escherichia coli, Saccharomyces cerevisiae, and Streptomyces spectabilis by DNA shuffling and transformation into Pichia pastoris. In the two best recombinant strains, the MAT activities are respectively 201% and 65% higher than the recombinant strains containing the starting MAT genes, and the SAM concentration increases by 103% and 65%, respectively. A 6.14 g/l of SAM production is reached in a 500 l bioreactor with the best recombinant strain
additional information
-
expression of dihydrodipicolinate synthase or co-expression of cystathionine gamma-synthase and dihydrodipicolinate synthase from Arabidopsis thaliana in tobacco leaves and seeds results in enhanced methionine levels, overview
additional information
-
MAT1A knockout mice, spontaneous steatohepatitis develops by 8 months, hepatocellular carcinoma develops by 18 months
additional information
-
mutations that affect the function of the metK gene products are a stop codon in the Madrid E strain and a 6-bp deletion in the Breinl strain, these typhus group genes, like the more degenerate spotted fever group orthologs, are in the process of gene degradation, overview
additional information
recombination of MAT genes from Escherichia coli, Saccharomyces cerevisiae, and Streptomyces spectabilis by DNA shuffling and transformation into Pichia pastoris. In the two best recombinant strains, the MAT activities are respectively 201% and 65% higher than the recombinant strains containing the starting MAT genes, and the SAM concentration increases by 103% and 65%, respectively. A 6.14 g/l of SAM production is reached in a 500 l bioreactor with the best recombinant strain
additional information
-
improved production of erythromycin A by expression of MAT in Saccharopolyspora erythraea E1
additional information
-
recombination of MAT genes from Escherichia coli, Saccharomyces cerevisiae, and Streptomyces spectabilis by DNA shuffling and transformation into Pichia pastoris. In the two best recombinant strains, the MAT activities are respectively 201% and 65% higher than the recombinant strains containing the starting MAT genes, and the SAM concentration increases by 103% and 65%, respectively. The K18R mutation of Streptomyces spectabilis probably result in the increased activity of the best MAT. A 6.14 g/l of SAM production is reached in a 500 l bioreactor with the best recombinant strain
additional information
-
overexpression in Nicotiana tabacum using Agrobacterium tumefaciens-mediated transformation results in active SAMS2 and accumulation of soluble polyamines
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.