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Literature summary 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

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

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.61 Escherichia coli
-
-
-
3.1.1.61 Escherichia coli JM 109
-
-
-

Reaction

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

Substrates and Products (Substrate)

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

Subunits

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