2.6.1.88: methionine transaminase
This is an abbreviated version!
For detailed information about methionine transaminase, go to the full flat file.
Reaction
Synonyms
BcaT, BCAT4, branched-chain amino acid aminotransferase, branched-chain aminotransferase4, KMAT, methionine aminotransferase, TyrAT, tyrosine aminotransferase, YbdL
ECTree
2.6.1.88 methionine transaminaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 2.6.1.88 - methionine transaminase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-oxo-4-methylthiobutanoate + L-glutamate
L-methionine + ?
-
-
-
-
?
2-oxo-4-methylthiobutanoate + L-isoleucine
L-methionine + 2-oxo-methylvalerate
-
-
-
-
?
2-oxo-4-methylthiobutanoate + L-leucine
L-methionine + 2-oxo-isocaproate
-
-
-
-
r
2-oxo-4-methylthiobutanoate + L-phenylalanine
L-methionine + ?
-
-
-
-
?
2-oxo-4-methylthiobutanoate + L-tryptophan
L-methionine + 3-(1H-indol-3-yl)-2-oxopropanoate
2-oxo-4-methylthiobutanoate + L-tyrosine
L-methionine + 4-hydroxyhenylpyruvate
-
-
-
-
r
2-oxo-4-methylthiobutanoate + L-valine
L-methionine + 2-oxo-isovalerate
-
-
-
-
?
4-methyl-2-oxopentanoate + ?
L-methionine + a 2-oxo acid
41% activity at 2 mM compared to 2-oxo-4-methylthiobutanoate
-
-
r
5-methylthio-2-oxopentanoate + ?
L-methionine + a 2-oxo acid
48% activity at 0.1 mM and 53% activity at 2 mM compared to 2-oxo-4-methylthiobutanoate
-
-
r
L-histidine + a 2-oxo acid
?
88% activity compared to L-methionine (at 1 mM)
-
-
?
L-homomethionine + a 2-oxo acid
?
37% activity at 1 mM and 65% activity at 5 mM compared to L-methionine
-
-
r
L-leucine + a 2-oxo acid
2-oxo-4-methylthiobutanoate + an L-amino acid
29% activity at 1 mM and 62% activity at 5 mM compared to 2-oxo-4-methylthiobutanoate
-
-
r
L-leucine + a 2-oxo acid
?
11% activity compared to L-methionine (at 1 mM)
-
-
?
L-methionine + 2-oxo-isocaproate
2-oxo-4-methylthiobutanoate + L-leucine
-
-
-
-
r
L-methionine + 2-oxoglutarate
2-oxo-4-methylthiobutanoate + L-glutamate
-
-
-
-
r
L-methionine + a 2-oxo acid
2-oxo-4-methylthiobutanoate + an L-amino acid
recombinant enzyme shows high efficiency with L-methionine (100% activity at 1 and 5 mM)
-
-
r
L-methionine + a 2-oxo acid
?
the enzyme shows a preference for L-methionine (100% activity at 1 mM L-methionine)
-
-
?
L-phenylalanine + a 2-oxo acid
?
57% activity compared to L-methionine (at 1 mM)
-
-
?
L-tyrosine + a 2-oxo acid
?
9% activity compared to L-methionine (at 1 mM)
-
-
?
2-oxo-4-methylthiobutanoate + an L-amino acid
L-methionine + a 2-oxo acid
recombinant enzyme shows high activity with 2-oxo-4-methylthiobutanoate (100% activity at 0.1 and 2 mM)
-
-
r
2-oxo-4-methylthiobutanoate + an L-amino acid
L-methionine + a 2-oxo acid
-
a wide range of L-amino acids are effective donors, with Asp, Glu, Phe, His, Ile, Leu, Asn, Gln, Trp, and Tyr all producing more than 0.5 nM of L-methionine/min/mg of protein. Glu, Phe, Trp, and Tyr are the preferred amino donors, catalyzing the formation of above 1100 nM L-methionine/min/mg of protein
-
-
?
2-oxo-4-methylthiobutanoate + an L-amino acid
L-methionine + a 2-oxo acid
-
a wide range of L-amino acids are effective donors, with Asp, Glu, Phe, His, Ile, Leu, Asn, Gln, Trp, and Tyr all producing more than 0.5 nM of L-methionine/min/mg of protein. Glu, Phe, Trp, and Tyr are the preferred amino donors, catalyzing the formation of above 1100 nM L-methionine/min/mg of protein
-
-
?
2-oxo-4-methylthiobutanoate + an L-amino acid
L-methionine + a 2-oxo acid
-
isoleucine, leucine, and valine are the most effective substrates while glutamate and phenylalanine are also active as amino donors. Tyrosine and tryptophan have a much lesser ability to transaminate 2-oxo-4-methylthiobutanoate and all other L-amino acids are inactive
-
-
?
2-oxo-4-methylthiobutanoate + L-glutamate
L-methionine + 2-oxoglutarate
-
while L-glutamate is capable of producing the highest maximum initial velocity for L-methionine production from 2-oxo-4-methylthiobutanoate, it is 5-10fold poorer in terms of substrate specificity when compared with L-tyrosine, L-tryptophan, and L-phenylalanine
-
-
?
2-oxo-4-methylthiobutanoate + L-glutamate
L-methionine + 2-oxoglutarate
-
while L-glutamate is capable of producing the highest maximum initial velocity for L-methionine production from 2-oxo-4-methylthiobutanoate, it is 5-10fold poorer in terms of substrate specificity when compared with L-tyrosine, L-tryptophan, and L-phenylalanine
-
-
?
2-oxo-4-methylthiobutanoate + L-phenylalanine
L-methionine + 2-oxo-3-phenylpropanoate
-
-
-
-
?
2-oxo-4-methylthiobutanoate + L-phenylalanine
L-methionine + 2-oxo-3-phenylpropanoate
-
-
-
-
?
2-oxo-4-methylthiobutanoate + L-tryptophan
L-methionine + 3-(1H-indol-3-yl)-2-oxopropanoate
-
-
-
-
?
2-oxo-4-methylthiobutanoate + L-tryptophan
L-methionine + 3-(1H-indol-3-yl)-2-oxopropanoate
-
-
-
-
?
additional information
?
-
the enzyme does not use L-isoleucine (at 1 mM), L-valine (at 1 and 5 mM), 4-methyl-2-oxopentanoate (at 0.1 mM), 6-methylthio-2-oxohexanoate, 3-methyl-2-oxopentanoate, and 3-methyl-2-oxobutyrate as substrates (at 0.1 mM each)
-
-
?
additional information
?
-
the enzyme does not use L-tryptophan, L-valine, L-asparagine, L-glutamate, and L-arginine as substrates
-
-
?
additional information
?
-
-
the enzyme does not use L-tryptophan, L-valine, L-asparagine, L-glutamate, and L-arginine as substrates
-
-
?
additional information
?
-
-
the purified enzyme is unable to effectively utilize systems containing L-glutamate and oxaloacetate, L-glutamate and pyruvate, or L-alanine and 2-oxoglutarate
-
-
?
additional information
?
-
-
the purified enzyme is unable to effectively utilize systems containing L-glutamate and oxaloacetate, L-glutamate and pyruvate, or L-alanine and 2-oxoglutarate
-
-
?
