Open AccessCrystalline 3‐methylaspartase from a facultative anaerobe, Escherichia coli strain YG1002
Author(s) -
Asano Yasuhisa,
Kato Yasuo
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb06837.x
Subject(s) - escherichia coli , deamination , strain (injury) , enzyme , divalent , substrate (aquarium) , chemistry , biochemistry , bacteria , stereochemistry , biology , organic chemistry , ecology , gene , anatomy , genetics
Crystalline 3‐methylaspartase (EC 4.3.1.2) from Escherichia coli strain YG1002 that had been isolated from soil was characterized. The enzyme activity was induced when the organism was grown statically on medium containing ( S )‐glutamic acid. Its molecular mass is about 84 kDa, and it may be composed of two identical subunits of 42 kDa. The enzyme requires both divalent and monovalent cations such as Mg 2+ and K + , respectively. The enzyme catalyzes reversible amination‐deamination between mesaconic acid and (2 S ,3 S )‐methylaspartic acid, which is the best substrate.