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Titolo:
PURIFICATION AND CHARACTERIZATION OF METALLO-BETA-LACTAMASE FROM SERRATIA-MARCESCENS
Autore:
MARUMO K; TAKEDA A; NAKAMURA Y; NAKAYA K;
Indirizzi:
SHOWA UNIV,FUJIGAOKA HOSP,DEPT CLIN PATHOL,AOBA KU,1-30 FUJIGAOKA YOKOHAMA KANAGAWA 227 JAPAN SHOWA UNIV,DEPT PHARMACEUT SCI,SHINAGAWA KU TOKYO 142 JAPAN
Titolo Testata:
Microbiology and immunology
fascicolo: 1, volume: 39, anno: 1995,
pagine: 27 - 33
SICI:
0385-5600(1995)39:1<27:PACOMF>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
PSEUDOMONAS-MALTOPHILIA; BIOCHEMICAL-PROPERTIES; BACTEROIDES-FRAGILIS; CARBAPENEMS; RESISTANCE; PROTEIN;
Keywords:
SERRATIA MARCESCENS; PURIFICATION; METALLO-BETA-LACTAMASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
17
Recensione:
Indirizzi per estratti:
Citazione:
K. Marumo et al., "PURIFICATION AND CHARACTERIZATION OF METALLO-BETA-LACTAMASE FROM SERRATIA-MARCESCENS", Microbiology and immunology, 39(1), 1995, pp. 27-33

Abstract

Carbapenem-hydrolyzing beta-lactamase from Serratia marcescens FHSM4055 was purified 926-fold by means of carboxylmethyl Sephadex C-50, Sephacryl S-200, and Mono S column chromatography, The molecular weight was 30,000 by SDS-PAGE and the isoelectric point was 8.7. The enzyme activity was inhibited by EDTA, and restored by adding zinc (II) or manganese (II). It was inhibited by p-chloromercuribenzoate and iodine as well as the heavy metals, Hg (II), Fe (II), Fe (III), and Cu (II). These results indicate that the enzyme is a metallo-beta-lactamase and that the SH-group of only one cysteine residue probably binds to the metal ion, thus contributing to the stability of the enzyme active center. The specific constant (kcat/Km) showed that the enzyme hydrolyzed various beta-lactam antibiotics such as carbapenems, cephalosporins, moxalactam, cephamycins, and penicillins other than monobactams. Ampicillin and piperacillin with respective amino- and imino-groups, ceftazidime with a carboxypropyloxyimino-group, and cefclidin with a carbamoylquinuclidine-group were poor substrates among the beta-lactam antibiotics other than the monobactams tested, The plots of the turnover number(kcat) against pH for the hydrolysis of cephaloridine gave an asymmetrical curve with the 'tail' on the acid side (pK(1) 5.9; pK(2), 9.0; pK(3), 10.8), whereas those of kcat/Km gave a bell-shaped curve (pK(1),5.8; pK(2), 9.8). Both results suggest that two tonic forms of an intermediate yield the same product at different rates and that the enzyme is stable under alkaline conditions. Since the N-terminal amino acidsequence of 27 residues determined was consistent with that of the metalloenzyme (Antimicrob. Agents Chemother., 1994, 38: 71-78), the above enzymatic characteristics seem to coincide.

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Documento generato il 29/03/20 alle ore 09:20:58