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Literature summary for 3.1.1.61 extracted from

  • Krueger, J.K.; Stock, J.; Schutt, C.E.
    Evidence that the methylesterase of bacterial chemotaxis may be a serine hydrolase (1992), Biochim. Biophys. Acta, 1119, 322-326.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C207A mutant retains at least 50% of the wild-type enzyme activity Escherichia coli
C207A/C309A the double mutant retains at 70% of the wild-type enzyme activity Escherichia coli
C309A mutant retains at least 50% of the wild-type enzyme activity Escherichia coli
S164C mutant has less than 2% of the wild-type activity Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli enzyme catalyses the hydrolysis of glutamyl-methyl esters in bacterial chemoreceptor proteins ?
-
?
additional information Escherichia coli JM 109 enzyme catalyses the hydrolysis of glutamyl-methyl esters in bacterial chemoreceptor proteins ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli JM 109
-
-
-

Reaction

Reaction Comment Organism Reaction ID
protein L-glutamate O5-methyl ester + H2O = protein L-glutamate + methanol mechanism Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme catalyses the hydrolysis of glutamyl-methyl esters in bacterial chemoreceptor proteins Escherichia coli ?
-
?
additional information enzyme catalyses the hydrolysis of glutamyl-methyl esters in bacterial chemoreceptor proteins Escherichia coli JM 109 ?
-
?

Subunits

Subunits Comment Organism
More enzyme may be a serine hydrolase Escherichia coli