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Titolo:
Cloning and characterization of a new member of the nudix hydrolases from human and mouse
Autore:
Yang, HJ; Slupska, MM; Wei, YF; Tai, JH; Luther, WM; Xia, YR; Shih, DM; Chiang, JH; Baikalov, C; Fitz-Gibbon, S; Phan, IT; Conrad, A; Miller, JH;
Indirizzi:
Univ Calif Los Angeles, Dept Microbiol & Mol Genet, Los Angeles, CA 90095 USA Univ Calif Los Angeles Los Angeles CA USA 90095 Los Angeles, CA 90095 USA Univ Calif Los Angeles, Inst Mol Biol, Los Angeles, CA 90095 USA Univ Calif Los Angeles Los Angeles CA USA 90095 Los Angeles, CA 90095 USA Univ Calif Los Angeles, Sch Med, Dept Med, Div Cardiol, Los Angeles, CA 90095 USA Univ Calif Los Angeles Los Angeles CA USA 90095 Los Angeles, CA 90095 USA Human Genome Sci, Rockville, MD 20850 USA Human Genome Sci Rockville MD USA 20850 nome Sci, Rockville, MD 20850 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 12, volume: 275, anno: 2000,
pagine: 8844 - 8853
SICI:
0021-9258(20000324)275:12<8844:CACOAN>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
ADP-RIBOSE PYROPHOSPHATASE; NUCLEOSIDE TRIPHOSPHATE PYROPHOSPHOHYDROLASE; ESCHERICHIA-COLI MUTT; RADIATION HYBRID MAP; MOLECULAR-CLONING; CATALYTIC DOMAIN; RAT-LIVER; NUCLEOTIDE PYROPHOSPHATASE; STREPTOCOCCUS-PNEUMONIAE; IDENTIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Miller, JH Univ Calif Los Angeles, Dept Microbiol & Mol Genet, 1602 Mol Sci Bldg,405 Hilgard Ave, Los Angeles, CA 90095 USA Univ Calif Los Angeles 1602 Mol Sci Bldg,405 Hilgard Ave Los Angeles CA USA 90095
Citazione:
H.J. Yang et al., "Cloning and characterization of a new member of the nudix hydrolases from human and mouse", J BIOL CHEM, 275(12), 2000, pp. 8844-8853

Abstract

Proteins containing the Nudix box "GX(5)EX(7)REUXEEXGU" (where U is usually Leu, Val, or lie) are Nudix hydrolases, which catalyze the hydrolysis of a variety of nucleoside diphosphate derivatives. Here we report cloning andcharacterization of a human cDNA encoding a novel nudix hydrolase NUDT5 for the hydrolysis of ADP-sugars. The deduced amino acid sequence of NUDT5 contains 219 amino acids, including a conserved Nudix hox sequence. The recombinant NUDT5 was expressed in Escherichia coli and purified to near homogeneity. At the optimal pH of 7, the purified recombinant NUTDT5 catalyzed hydrolysis of two major substrates, ADP-ribose and ADP-mannose with K-m valuesof 32 and 83 mu M, respectively; the V-max for ADP-mannose was about 1.5 times that with ADP-ribose. The murine NUDT5 homolog was also cloned and characterized. mNudT5 has 81% amino acid identity to NUDT5 with catalytic activities similar to NUDT5 under the optimal pH of 9. Both NUDT5 and mNudT5 transcripts were ubiquitously expressed in tissues analyzed with preferentialabundance in liver. The genomic structures of both NUDT5 and mNudT5 were determined and located on human chromosome 10 and mouse chromosome 2, respectively. The role of NUDT5 in maintaining levels of free ADP-ribose in cellsis discussed.

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Documento generato il 04/12/20 alle ore 04:03:58