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Titolo:
KINETICS AND MECHANISM OF ACETATE KINASE FROM BACILLUS-STEAROTHERMOPHILUS
Autore:
ISHIKAWA H; SHIROSHIMA M; WIDJAJA A; NAKAJIMA H; TSURUTANI R;
Indirizzi:
UNIV OSAKA PREFECTURE,DEPT CHEM ENGN,1-1 GAKUEN CHO SAKAI OSAKA 593 JAPAN UNITIKA RES & DEV CTR,DEPT BIOCHEM UJI KYOTO 611 JAPAN
Titolo Testata:
Journal of Chemical Engineering of Japan
fascicolo: 5, volume: 28, anno: 1995,
pagine: 517 - 524
SICI:
0021-9592(1995)28:5<517:KAMOAK>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
REGENERATION; ATP; ENZYME;
Keywords:
BIOCHEMICAL ENGINEERING; ALLOSTERIC ENZYME; RANDOM BI BI; REACTION RATE; ATP REGENERATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
18
Recensione:
Indirizzi per estratti:
Citazione:
H. Ishikawa et al., "KINETICS AND MECHANISM OF ACETATE KINASE FROM BACILLUS-STEAROTHERMOPHILUS", Journal of Chemical Engineering of Japan, 28(5), 1995, pp. 517-524

Abstract

The initial rates of ATP regeneration catalyzed by acetate kinase (ATP: acetate phosphotransferase; EC 2.7.2.1) from Bacillus stearothermophilus were measured under a wide range of MgADP(-), acetyl phosphate, MgATP(2-) and acetate concentrations. The experimental results shelvedthat the enzyme exhibited positive co-operativity for MgATP2(-) and no co-operativity for MgADP(-), acetyl phosphate and acetate. Furthermore, the initial rates of the forward reaction, in which MgATP(2-) and acetate were produced from MgADP(-) and acetyl phosphate, were inhibited by MgATP(2-) and acetate, and those of the reverse reaction were inhibited by MgADP(-) and acetyl phosphate. The initial rate data were correlated well by using the rate equation derived based on the assumption that the reaction obeys the general reaction scheme based on the Random Bi Bi mechanism, and on the previous experimental result that the enzyme behaves like a dimeric enzyme, even though it is a tetramericenzyme.

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Documento generato il 25/09/20 alle ore 16:03:59