Literature summary for 2.1.1.142 extracted from

Nes, W.D.; Sinha, A.; Jayasimha, P.; Zhou, W.; Song, Z.; Dennis, A.L.
Probing the sterol binding site of soybean sterol methyltransferase by site-directed mutagenesis: functional analysis of conserved aromatic amino acids in Region 1 (2006), Arch. Biochem. Biophys., 448, 23-30.

Search for more literature for 2.1.1.142

Application

Application	Comment	Organism
degradation	the amino acids of Region 1 provide a tight substrate orientation imposed by hydrophobic interactions between the sterol side chain and the SMT active site contacts and control the production and processing of the transmethylation pathways governed by the first and second C1-transfer activities	Glycine max

Cloned(Commentary)

Cloned (Comment)	Organism
overexpression of the pET vector in Escherichia coli BL21(DE3)	Glycine max

Protein Variants

Protein Variants	Comment	Organism
F82I	continues to catalyze strongly both the first and second C1-transfer activities and generates product sets similar to the control	Glycine max
F82L	first C1-transfer activity is relatively unaffected, loss of the second C1-transfer activity	Glycine max
F85L	first C1-transfer activity is relatively unaffected, loss of the second C1-transfer activity	Glycine max
F91L	first C1-transfer activity reduced from the control activity, loss of the second C1-transfer activity	Glycine max
F93L	first C1-transfer activity reduced from the control activity, loss of the second C1-transfer activity	Glycine max
W87L	first and second C1-transfer activities are greatly reduced from the control activities	Glycine max
Y83F	first C1-transfer activity is relatively unaffected whereas the second C1-transfer activity generates different amounts of product compared to the control	Glycine max
Y83F	Km and kcat, of wild-type enzyme and mutant enzyme are similar for cycloartenol as substrate	Glycine max
Y83L	first C1-transfer activity greatly reduced from the control activity, loss of the second C1-transfer activity	Glycine max
Y83L	Km and kcat, of wild-type enzyme and mutant enzyme are similar for cycloartenol as substrate	Glycine max

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.045	-	Cycloartenol	-	Glycine max
0.045	-	Cycloartenol	wild-type and mutants Y83F and Y83L	Glycine max
0.05	-	24(28)-methylene lophenol	wild-type	Glycine max
0.05	-	24(28)-methylene lophenol	mutant Y83F	Glycine max

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
160000	-	wild-type and mutants Y83F and Y83L, gel filtration	Glycine max

Organism

Organism	UniProt	Comment	Textmining
Glycine max	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
24(28)-methylene lophenol + S-adenosyl-L-methionine	-	Glycine max	?	-	?
cycloartenol + S-adenosyl-L-methionine	-	Glycine max	24-methylenecycloartanol + S-adenosyl-L-homocysteine	-	?
S-adenosyl-L-methionine + cycloartenol	-	Glycine max	S-adenosyl-L-homocysteine + (24R)-24-methylcycloart-25-en-3beta-ol	-	?

Synonyms

Synonyms	Comment	Organism
SMT	-	Glycine max
sterol methyltransferase	-	Glycine max

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.001	-	24(28)-methylene lophenol	wild-type	Glycine max
0.005	-	24(28)-methylene lophenol	mutant Y83F	Glycine max
0.01	-	Cycloartenol	-	Glycine max
0.01	-	Cycloartenol	wild-type and mutants Y83F and Y83L	Glycine max

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
5.8	8.9	-	Glycine max

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Release 2023.1 (January 2023)