Open AccessCharacterisation of rhodococci using peptide hydrolase substrates based on 7‐amino‐4‐methylcoumarin
Author(s) -
Goodfellow M.,
Thomas E.G.,
James A.L.
Publication year - 1987
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.1574-6968.1987.tb02313.x
Subject(s) - chemistry , peptide , enzyme , biochemistry , hydrolase , combinatorial chemistry , stereochemistry
Enzyme activity profiles of 105 rhodococci and related actinomycetes were obtained using peptide hydrolase substrates based on 7‐amino‐4‐methylcoumarin. All of the test strains produced l ‐alanyl‐, l ‐lysyl‐, l ‐methionyl, l ‐seryl‐, l ‐tyrosyl, S‐Bz‐ l ‐cysteinyl and l ‐alanyl‐ l ‐alanyl‐ l ‐phenyl‐alanyl‐peptidases but the distribution of the remaining enzymes gave results of differential value. Fluorogenic probes prepared from 7‐amino‐4‐methylcoumarin provide a simple and rapid means of detecting specific exo‐ and endopeptidases in small amounts of whole rhodococci.