Open AccessInteraction between Monobactams and Streptomyces R61 dd ‐Carboxypeptidase
Author(s) -
GEORGOPAPADAKOU Nafsika H.,
SMITH Sandra A.,
CIMARUSTI Christopher M.
Publication year - 1982
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1982.tb06622.x
Subject(s) - chemistry , stereochemistry , moiety , carboxypeptidase , streptomyces , carboxypeptidase a , streptomycetaceae , proteolysis , biochemistry , hydrolysis , enzyme , combinatorial chemistry , actinomycetales , biology , bacteria , genetics
The monobactams are a novel family of monocyclic β‐lactam antibiotics characterized by the 2‐oxoazetidine‐1‐sulfonic acid moiety. A series of monobactams bind covalently to the streptomyces R61 DD‐carboxypeptidase in a manner similar to that for bicyclic β‐lactams, especially cephalosporins. The similarity of interaction was established by the following criteria: inhibition of binding by diisopropylfluorophosphate and α‐dicarbonyls; stoichiometry of binding; similarity of partial proteolysis products of radiolabelled enzyme: rates of release of bound β‐lactams; nature of hydrolysis and hydroxylaminolysis products.