Open AccessEffect of various analogues of D‐glutamic acid on the D‐glutamate‐adding enzyme from Escherichis coli
Author(s) -
PratvielSosa Flore,
Acher Francine,
Trigalo François,
Blanot Didier,
Azerad Robert,
Heijenoort Jean
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.tb06642.x
Subject(s) - diastereomer , glutamic acid , enzyme , cyclohexanecarboxylic acid , alanine , chemistry , amino acid , escherichia coli , stereochemistry , biochemistry , gene
Twenty‐four analogues of D‐glutamic acid were tested as substrates or inhibitors of the D‐glutamate‐adding enzyme from Escherichia coli . The best substrates were, in decreasing order of specific activity, D‐ erythro ‐4‐methylglutamic acid, D‐ erythro ‐ methylglutamic acid, DL‐homocysteic acid, (±)‐ trans ‐1‐amino‐3‐carboxy‐cyclopentanecarboxylic acid and (±)‐ trans ‐1‐amino‐3‐carboxy‐cyclohexanecarboxylic acid. Among the different stereoisomers, only the D‐ erythro isomers for methylglutamic acids, and the trans isomers for the cyclic analogs, were substrates. Apart from the D‐ erythro ‐3 and 4‐methylglutamic acids and DL‐homocysteic acid, none of the examined compounds significantly inhibited the addition of radioactive D‐glutamic acid to UDP‐N‐acetylmuramyl‐L‐alanine.