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Titolo:
Expression and properties of human liver beta-ureidopropionase
Autore:
Sakamoto, T; Sakata, SF; Matsuda, K; Horikawa, Y; Tamaki, N;
Indirizzi:
Kobe Gakuin Univ, Fac Nutr, Nishi Ku, Kobe, Hyogo 6512180, Japan Kobe Gakuin Univ Kobe Hyogo Japan 6512180 Ku, Kobe, Hyogo 6512180, Japan Kobe Gakuin Univ, High Technol Res Ctr, Nishi Ku, Kobe, Hyogo 6512180, Japan Kobe Gakuin Univ Kobe Hyogo Japan 6512180 Ku, Kobe, Hyogo 6512180, Japan
Titolo Testata:
JOURNAL OF NUTRITIONAL SCIENCE AND VITAMINOLOGY
fascicolo: 2, volume: 47, anno: 2001,
pagine: 132 - 138
SICI:
0301-4800(200104)47:2<132:EAPOHL>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
RAT-LIVER; DIHYDROPYRIMIDINE DEHYDROGENASE; ALANINE SYNTHASE; CLONING; PURIFICATION; DEFICIENCY; CATABOLISM; ENZYMES; DIET;
Keywords:
beta-ureidopropionase; dihydropyrimidinase; dihydropyrimidine dehydrogenase; tissue distribution; propionate;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
26
Recensione:
Indirizzi per estratti:
Indirizzo: Sakata, SF Kobe Gakuin Univ, Fac Nutr, Nishi Ku, Kobe, Hyogo 6512180, Japan Kobe Gakuin Univ Kobe Hyogo Japan 6512180 Hyogo 6512180, Japan
Citazione:
T. Sakamoto et al., "Expression and properties of human liver beta-ureidopropionase", J NUTR SC V, 47(2), 2001, pp. 132-138

Abstract

A cDNA encoding beta -ureidopropionase (BUP) was isolated from a human liver cDNA library, expressed in E, coli, and purified from the culture extract, The 2,006 bp cDNA contained a 1,152 bp open reading frame encoding a protein of 384 amino acids with a molecular weight of 43,165 Da. The subunit molecular weight of the enzyme expressed was about 43,000 Da. The enzyme wasinhibited by 1 mM propionate, but not by 10 mM beta -alanine. Chemical analysis of the purified human BUP showed 0.54 zinc atoms per subunit, and thesequence of BUP cDNA contained one putative zinc-binding site motif, The purified enzyme had a pI of 5.65, and exhibited positive cooperativity with N-carbamoyl-beta -alanine as the substrate with a Hill coefficient 2.0, These properties of human BUP, except: the inhibition by beta -alanine, were similar to the rat liver purified enzyme. beta -Alanine inhibits rats BUP activity. The complex regulatory function and the negative cooperative mechanism of BUP by beta -alanine have been observed in rats. This kind of mechanism may not exist: in humans, because beta -alanine did not inhibit human BUP.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 20:06:12