Effect of various analogues of D-glutamic acid on the D-glutamate-adding enzyme from Escherichia coli.
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-3-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.
Pratviel-Sosa
F
F
Enveloppes Bactériennes et Peptides, URA 1131 du CNRS, Université de Paris-Sud, Orsay, France.
Acher
F
F
Trigalo
F
F
Blanot
D
D
Azerad
R
R
van Heijenoort
J
J
D004926:Escherichia coli / Q000201:enzymology*; D005971:Glutamates / Q000737:chemistry*; D018698:Glutamic Acid; D010453:Peptide Synthases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D010457:Peptidoglycan / Q000096:biosynthesis; D013237:Stereoisomerism; D013379:Substrate Specificity
D005971:Glutamates; D010457:Peptidoglycan; D018698:Glutamic Acid; D010453:Peptide Synthases; C053379:UDP-N-acetylmuramoylalanine-D-glutamate ligase