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Titolo:
New thioredoxins and glutaredoxins as electron donors of 3 '-phosphoadenylylsulfate reductase
Autore:
Lillig, CH; Prior, A; Schwenn, JD; Aslund, F; Ritz, D; Vlamis-Gardikas, A; Holmgren, A;
Indirizzi:
Ruhr Univ Bochum, Fac Biol, D-44780 Bochum, Germany Ruhr Univ Bochum Bochum Germany D-44780 ac Biol, D-44780 Bochum, Germany Harvard Med Sch, Dept Microbiol & Mol Genet, Boston, MA USA Harvard Med Sch Boston MA USA Dept Microbiol & Mol Genet, Boston, MA USA Karolinskaolm,t, Med Nobel Inst Biochem, Dept Med Biochem & Biophys, Stockh Karolinska Inst Stockholm Sweden em, Dept Med Biochem & Biophys, Stockh
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 12, volume: 274, anno: 1999,
pagine: 7695 - 7698
SICI:
0021-9258(19990319)274:12<7695:NTAGAE>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
GLUTATHIONE-DEPENDENT SYNTHESIS; ESCHERICHIA-COLI; RIBONUCLEOTIDE REDUCTASE; SULFATE REDUCTION; MIXED DISULFIDE; PAPS-REDUCTASE; PROTEINS; DEOXYRIBONUCLEOTIDES; MECHANISM; MUTANT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Schwenn, JD Ruhr Univ Bochum, Fac Biol, POB 10 21 48, D-44780 Bochum, Germany Ruhr Univ Bochum POB 10 21 48 Bochum Germany D-44780 Germany
Citazione:
C.H. Lillig et al., "New thioredoxins and glutaredoxins as electron donors of 3 '-phosphoadenylylsulfate reductase", J BIOL CHEM, 274(12), 1999, pp. 7695-7698

Abstract

Reduction of inorganic sulfate to sulfite in prototrophic bacteria occurs with 3'-phosphoadenylylsulfate (PAPS) as substrate for PAPS reductase and is the first step leading to reduced sulfur for cellular biosynthetic reactions. The relative efficiency as reductants of homogeneous highly active PAPS reductase of the newly identified second thioredoxin (Trx2) and glutaredoxins (Grx1, Grx2, Grx3, and a mutant Grx1C14S) was compared with the well known thioredoxin (Trx1) from Escherichia coil, Trx1, Trx2, and Grx1 supported virtually identical rates of sulfite formation with a V-max, ranging from 6.6 units mg(-1) (Trx1) to 5.1 units mg(-1) (Grx1), whereas Grx1C14S was only marginally active, and Grx2 and Grx3 had no activity. The structural difference between active reductants had no effect upon K-m (PAPS) (22.5 mu m) Grx1 effectively replaced Trx1 with essentially identical K-m-values: K-m (trx1) (13.7 mu M), K-m (grx1) (14.9 mu M), whereas the K-m (trx2) was considerably higher (34.2 mu M). The results agree with previous in vivo datasuggesting that Trx1 or Grx1 is essential for sulfate reduction but not for ribonucleotide reduction in E, coli.

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Documento generato il 30/11/20 alle ore 07:04:57