Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 Å resolution
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منابع مشابه
Active-site-directed inactivators of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of Streptomyces albus G.
Several types of active-site-directed inactivators (inhibitors) of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase were tested. (i) Among the heavy-atom-containing compounds examined, K2Pt(C2O4)2 inactivates the enzyme with a second-order rate constant of about 6 X 10(-2)M-1 X S-1 and has only one binding site located close to the Zn2+ cofactor within the enzyme active site. (i...
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Under certain conditions, the values of the parameters that govern the interactions between the active-siteserine D-alanyl-D-alanine-cleaving peptidases and both carbonyl-donor substrates and ,J-lactam suicide substrates can be determined on the basis of the amounts of (serine ester-linked) acyl-protein formed during the reactions. Expressing the 'affinity' of a ,J-lactam compound for a DD-pept...
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Antibiotic A3 5512B1.2) is a member of the glycopeptide family of antibiotics; complete structures have been reported for two members of this group, vancomycin3' and ristocetin A4' a) . Both vancomycin and ristocetin have been shown to form complexes with mucopeptides containing the terminal dipeptide D-alanyl-D-alaninee) ; this interaction within the bacterial cell inhibits crosslinking of the...
متن کاملD=Alanine Carboxypeptidase from Bacillus subtilis Membranes
The D-alanine carboxypeptidase was solubilized from the membranes of Bacillus subtilis with the nonionic detergent, Triton X-100, and pursed to homogeneity. The purified protein bound irreversibly radioactivity from [Wlpenicillin G. It contained a single polypeptide chain of molecular weight 50,000 and existed in solution as a protein-detergent aggregate of molecular weight about 350,000. The a...
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ژورنال
عنوان ژورنال: Nature
سال: 1982
ISSN: 0028-0836,1476-4687
DOI: 10.1038/299469a0