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Titolo:
Cloning and characterization of oah, the gene encoding oxaloacetate hydrolase in Aspergillus niger
Autore:
Pedersen, H; Hjort, C; Nielsen, J;
Indirizzi:
Tech Univ Denmark, Dept Biotechnol, Ctr Proc Biotechnol, DK-2800 Lyngby, Denmark Tech Univ Denmark Lyngby Denmark DK-2800 echnol, DK-2800 Lyngby, Denmark Novo Nordisk AS, DK-2880 Bagsvaerd, Denmark Novo Nordisk AS Bagsvaerd Denmark DK-2880 AS, DK-2880 Bagsvaerd, Denmark
Titolo Testata:
MOLECULAR AND GENERAL GENETICS
fascicolo: 2, volume: 263, anno: 2000,
pagine: 281 - 286
SICI:
0026-8925(200003)263:2<281:CACOOT>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
HOST STRAINS; OXALIC-ACID; SEQUENCES;
Keywords:
oxalate; Aspergillus; oxaloacetate hydrolase; oxalacetase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
22
Recensione:
Indirizzi per estratti:
Indirizzo: Nielsen, J Tech Univ Denmark, Dept Biotechnol, Ctr Proc Biotechnol, Bldg 227, DK-2800Lyngby, Denmark Tech Univ Denmark Bldg 227 Lyngby Denmark DK-2800 gby, Denmark
Citazione:
H. Pedersen et al., "Cloning and characterization of oah, the gene encoding oxaloacetate hydrolase in Aspergillus niger", MOL G GENET, 263(2), 2000, pp. 281-286

Abstract

The enzyme oxaloacetate hydrolase (EC 3.7.1.1). which is involved in oxalate formation, was purified from Aspergillus niger. The native enzyme has a molecular mass of 360-440 kDa, and the denatured enzyme has a molecular mass of 39 kDa, as determined by gel electrophoresis. Enzyme activity is maximal at pH 7.0 and 45 degrees C. The Fraction containing the enzyme activity contained at least five proteins. The N-terminal amino acid sequences of four of these proteins were determined. The amino acid sequences were alignedwith EST sequences from A. niger, and an EST sequence that showed 100% identity to all four sequences was identified. Using this EST sequence the gene encoding oxaloacetate hydrolase (oah) was cloned by inverse PCR. It consists of an ORF of 1227 bp with two introns of 92 and 112 bp, respectively. The gene encodes a protein of 341 amino acids with a molecular mass of 37 kDa. Under the growth conditions tested, the highest oah expression was foundfor growth on acetate as carbon source. The gene was expressed only at pH values higher than 4.0.

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Documento generato il 15/07/20 alle ore 21:38:06