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Titolo:
GLUTAREDOXIN FUNCTION FOR THE CARBOXYL-TERMINAL DOMAIN OF THE PLANT-TYPE 5'-ADENYLYLSULFATE REDUCTASE
Autore:
BICK JA; ASLUND F; CHEN YC; LEUSTEK T;
Indirizzi:
RUTGERS STATE UNIV,BIOTECH CTR,59 DUDLEY RD NEW BRUNSWICK NJ 08901 RUTGERS STATE UNIV,BIOTECH CTR NEW BRUNSWICK NJ 08901 RUTGERS STATE UNIV,DEPT PLANT SCI NEW BRUNSWICK NJ 08901 HARVARD UNIV,SCH MED,DEPT MICROBIOL & MOL GENET BOSTON MA 02115
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 14, volume: 95, anno: 1998,
pagine: 8404 - 8409
SICI:
0027-8424(1998)95:14<8404:GFFTCD>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
GLUTATHIONE-DEPENDENT SYNTHESIS; ESCHERICHIA-COLI; SULFATE REDUCTION; SPINACH-CHLOROPLASTS; APS-SULFOTRANSFERASE; MIXED DISULFIDE; THIOREDOXIN; PROTEIN; DEOXYRIBONUCLEOTIDES; PURIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
36
Recensione:
Indirizzi per estratti:
Citazione:
J.A. Bick et al., "GLUTAREDOXIN FUNCTION FOR THE CARBOXYL-TERMINAL DOMAIN OF THE PLANT-TYPE 5'-ADENYLYLSULFATE REDUCTASE", Proceedings of the National Academy of Sciences of the United Statesof America, 95(14), 1998, pp. 8404-8409

Abstract

5'-Adenylylsulfate (APS) reductase (EC 1.8.99.-) catalyzes the reduction of activated sulfate to sulfite in plants, The evidence presented here shows that a domain of the enzyme is a glutathione (GSH)-dependent reductase that functions similarly to the redox cofactor glutaredoxin, The APR1 cDNA encoding APS reductase from Arabidopsis thaliana is able to complement the cysteine auxotrophy of an Escherichia coli cysH [3'-phosphoadenosine-5'-phosphosulfate (PAPS) reductase] mutant, only if the E. coli strain produces glutathione. The purified recombinant enzyme (APR1p) can use GSH efficiently as a hydrogen donor in vitro, showing a K-m[GsH] of approximate to 0.6 mM. Gene dissection was used toexpress separately the regions of APR1p from amino acids 73-327 (the R domain), homologous with microbial PAPS reductase, and from amino acids 328-465 (the C domain), homologous with thioredoxin. The R and C domains alone are inactive in APS reduction, but the activity is partially restored by mixing the two domains, The C domain shows a number ofactivities that are typical of E. coil glutaredoxin rather than thioredoxin. Both the C domain and APR1p are highly active in GSH-dependentreduction of hydroxyethyldisulfide, cystine, and dehydroascorbate, showing a K-m[GSH] in these assays of approximate to 1 mM, The R domain does not show these activities. The C domain is active in GSH-dependent reduction of insulin disulfides and ribonucleotide reductase, whereas APR1p and R domain are inactive. The C domain can substitute for glutaredoxin in vivo as demonstrated by complementation of an E. coil mutant, underscoring the functional similarity between the two enzymes,

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Documento generato il 30/11/20 alle ore 05:59:19