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Titolo:
ISOLATION AND CHARACTERIZATION OF THE THERMORESISTANT GLUCONOKINASE FROM ESCHERICHIA-COLI
Autore:
VIVAS EI; LIENDO A; DAWIDOWICZ K; ISTURIZ T;
Indirizzi:
CENT UNIV VENEZUELA,FAC CIENCIAS,ESCUELA BIOL,CTR BIOL CELULAR,APARTADO POSTAL 47557 CARACAS 1041A VENEZUELA CENT UNIV VENEZUELA,FAC CIENCIAS,ESCUELA BIOL,CTR BIOL CELULAR CARACAS 1041A VENEZUELA CENT UNIV VENEZUELA,FAC CIENCIAS,ESCUELA BIOL,DEPT BIOL CELULAR CARACAS 1041A VENEZUELA
Titolo Testata:
Journal of basic microbiology
fascicolo: 2, volume: 34, anno: 1994,
pagine: 117 - 122
SICI:
0233-111X(1994)34:2<117:IACOTT>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
ZYMOMONAS-MOBILIS; SORBITOL PRODUCTION; GLUCONATE; CATABOLISM;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
22
Recensione:
Indirizzi per estratti:
Citazione:
E.I. Vivas et al., "ISOLATION AND CHARACTERIZATION OF THE THERMORESISTANT GLUCONOKINASE FROM ESCHERICHIA-COLI", Journal of basic microbiology, 34(2), 1994, pp. 117-122

Abstract

It is known that two gluconokinases are inducibly expressed during the utilization of gluconate by E. coli. One is thermoresistant (activity stable for 3 h at 30 degrees C) and the other thermosensitive (losses 75% or more of its activity under the above conditions). The thermoresistant gluconokinase (EC 2.7.1.12) was isolated, purified and characterized for the first time from the E. coli mutant Ca26, a K12 derivative which lacks the thermosensitive activity. The enzyme was purified 43 fold with a recovery of 11%. The M(r) of the enzyme was 100 kDa with three equal subunits of approximately 29.5 kDa. The enzyme exhibitedMICHAELIS-MENTEN kinetics and the K-m values for gluconate and ATP were 0.02 mM and 0.045 mM respectively.

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Documento generato il 25/09/20 alle ore 08:51:08