Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
A 2-DOMAIN STRUCTURE FOR THE 2 SUBUNITS OF NAD(P)H-QUINONE ACCEPTOR OXIDOREDUCTASE
Autore:
CHEN S; DENG PSK; BAILEY JM; SWIDEREK KM;
Indirizzi:
BECKMAN RES INST CITY HOPE,DIV IMMUNOL DUARTE CA 91010
Titolo Testata:
Protein science
fascicolo: 1, volume: 3, anno: 1994,
pagine: 51 - 57
SICI:
0961-8368(1994)3:1<51:A2SFT2>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID-SEQUENCE; RAT-LIVER NAD(P)H; SITE-DIRECTED MUTAGENESIS; COLON-CARCINOMA CELLS; INDUCED DNA DAMAGE; DT-DIAPHORASE; CIBACRON BLUE; NAD(P)H-MENADIONE OXIDOREDUCTASE; REACTION-MECHANISM; REDUCTASE;
Keywords:
ACTIVE SITE; FAD PROSTHETIC GROUP; PROTEOLYSIS; QUINONE REDUCTASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
35
Recensione:
Indirizzi per estratti:
Citazione:
S. Chen et al., "A 2-DOMAIN STRUCTURE FOR THE 2 SUBUNITS OF NAD(P)H-QUINONE ACCEPTOR OXIDOREDUCTASE", Protein science, 3(1), 1994, pp. 51-57

Abstract

NAD(P)H:quinone acceptor oxidoreductase (EC 1.6.99.2) (DT-diaphorase)is a FAD-containing reductase that catalyzes a unique 2-electron reduction of quinones. It consists of 2 identical subunits. In this study,it was found that the carboxyl-terminal portion of the 2 subunits canbe cleaved by various proteases, whereas the amino-terminal portion cannot. It was also found that proteolytic digestion of the enzyme can be blocked by the prosthetic group FAD, substrates NAD(P)H and menadione, and inhibitors dicoumarol and phenindione. Interestingly, chrysin and Cibacron blue, 2 additional inhibitors, cannot protect the enzyme from proteolytic digestion. The results obtained from this study indicate that the subunit of the quinone reductase has a 2-domain structure, i.e., an aminoterminal compact domain and a carboxyl-terminal flexible domain. A structural model of the quinone reductase is generated based on results obtained from amino-terminal and carboxyl-terminal protein sequence analyses and electrospray mass spectral analyses of hydrolytic products of the enzyme generated by trypsin, chymotrypsin, and Staphylococcus aureus protease. Furthermore, based on the data, it is suggested that the binding of substrates involves an interaction between 2 structural domains.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 06:50:36