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Titolo:
Homomultimeric protease in the hyperthermophilic bacterium Thermotoga maritima has structural and amino acid sequence homology to bacteriocins in mesophilic bacteria
Autore:
Hicks, PM; Rinker, KD; Baker, JR; Kelly, RM;
Indirizzi:
N Carolina State Univ, Dept Chem Engn, Raleigh, NC 27695 USA N Carolina State Univ Raleigh NC USA 27695 em Engn, Raleigh, NC 27695 USA
Titolo Testata:
FEBS LETTERS
fascicolo: 3, volume: 440, anno: 1998,
pagine: 393 - 398
SICI:
0014-5793(199812)440:3<393:HPITHB>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
ARCHAEON PYROCOCCUS-FURIOSUS; COMPLETE GENOME SEQUENCE; SP-NOV REPRESENTS; ESCHERICHIA-COLI; BREVIBACTERIUM LINENS; MULTICATALYTIC PROTEINASE; METHANOGENIC ARCHAEON; ACTIVATION; PURIFICATION; M18;
Keywords:
proteolysis; bacteriocin; Thermotoga;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Kelly, RM N Carolina State Univ, Dept Chem Engn, Raleigh, NC 27695 USA N Carolina State Univ Raleigh NC USA 27695 aleigh, NC 27695 USA
Citazione:
P.M. Hicks et al., "Homomultimeric protease in the hyperthermophilic bacterium Thermotoga maritima has structural and amino acid sequence homology to bacteriocins in mesophilic bacteria", FEBS LETTER, 440(3), 1998, pp. 393-398

Abstract

A novel homomultimeric protease (>669 kDa), based on 31 kDa subunits, was purified from cell extracts of the hyperthermophilic bacterium Thermotoga maritima, This protease exhibits activity toward chymotrypsin and trypsin substrates, optimally at 90 degrees C and pH 7.1, and has a half-life of 36 min at 95 degrees C, Transmission electron microscopy established that the protease consists of a large globular assembly which appears circular from the front view. The function of this protease in T. maritima remains unclear, although putative homologs include a 29 kDa antigen from Mycobacterium tuberculosis and a 31 kDa monomer of a high molecular weight bacteriocin produced by Brevibacterium linens [Valdes-Stauber, N. and Scherer, S. (1996) Appl, Environ, Microbiol, 62, 1283-1286], The relationship of these mesophilic proteins to the T, maritima protease suggests that their antibacterial activity may involve elements of proteolysis, and raises the prospect for antimicrobial ecological strategies in hyperthermophilic niches. (C) 1998 Federation of European Biochemical Societies.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 07:18:10