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Titolo:
Expression, stability and performance of the three-component alkane mono-oxygenase of Pseudomonas oleovorans in Escherichia coli
Autore:
Staijen, IE; van Beilen, JB; Witholt, B;
Indirizzi:
ETH Honggerberg, Swiss Fed Inst Technol, Inst Biotechnol, CH-8093 Zurich, Switzerland ETH Honggerberg Zurich Switzerland CH-8093 , CH-8093 Zurich, Switzerland
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 7, volume: 267, anno: 2000,
pagine: 1957 - 1965
SICI:
0014-2956(200004)267:7<1957:ESAPOT>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
ENZYMATIC OMEGA-OXIDATION; RUBREDOXIN REDUCTASE; POLYACRYLAMIDE GELS; ALKBAC OPERON; SYSTEM; HYDROXYLASE; PUTIDA; GENES; PROTEINS; OVEREXPRESSION;
Keywords:
alkane hydroxylase; expression; Pseudomonas oleovorans; rubredoxin reductase; rubredoxin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
55
Recensione:
Indirizzi per estratti:
Indirizzo: Witholt, B ETH Honggerberg, Swiss Fed Inst Technol, Inst Biotechnol, CH-8093 Zurich, Switzerland ETH Honggerberg Zurich Switzerland CH-8093 urich, Switzerland
Citazione:
I.E. Staijen et al., "Expression, stability and performance of the three-component alkane mono-oxygenase of Pseudomonas oleovorans in Escherichia coli", EUR J BIOCH, 267(7), 2000, pp. 1957-1965

Abstract

We tested the synthesis and in vivo function of the inducible alkane hydroxylase of Pseudomonas oleovorans GPo1 in several Escherichia coli recombinants. The enzyme components (AlkB, AlkG and AlkT) were synthesized at various rates in different E. coli hosts, which after induction produced between twofold and tenfold more of the Alk components than did P. oleovorans. The enzyme components were less stable in recombinant E. coli hosts than in P. oleovorans. In addition, the specific activity of the alkane mono-oxygenasecomponent AlkB was five or six times lower in E. coli than in P. oleovorans. Evidently, optimal functioning of the hydroxylase system requires factors or a molecular environment that are available in Pseudomonas but not in E. coli. These factors are likely to include correct interactions of AlkB with the membrane and incorporation of iron into the AlkG and AlkB apoproteins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 16:39:03