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Titolo:
MOLECULAR CHARACTERIZATION OF GLYCOSOMAL NAD(-DEPENDENT GLYCEROL 3-PHOSPHATE DEHYDROGENASE FROM TRYPANOSOMA-BRUCEI-RHODESIENSE())
Autore:
STEBECK CE; FREVERT U; MOMMSEN TP; VASSELLA E; RODITI I; PEARSON TW;
Indirizzi:
UNIV VICTORIA,DEPT BIOCHEM & MICROBIOL,POB 3055 VICTORIA BC V8W 3P6 CANADA UNIV VICTORIA,DEPT BIOCHEM & MICROBIOL VICTORIA BC V8W 3P6 CANADA NYU,MED CTR,DEPT PATHOL,MICHAEL HEIDELBERGER DIV IMMUNOL NEW YORK NY 10016 UNIV BERN,INST ALLGEMEINE MIKROBIOL BERN SWITZERLAND
Titolo Testata:
Molecular and biochemical parasitology
fascicolo: 1-2, volume: 76, anno: 1996,
pagine: 145 - 158
SICI:
0166-6851(1996)76:1-2<145:MCOGNG>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
GLYCEROL-3-PHOSPHATE DEHYDROGENASE; MONOCLONAL-ANTIBODIES; GLYCOLYTIC-ENZYMES; SEQUENCE; PRIMER; KINASE; GENES; AMPLIFICATION; PURIFICATION; CATABOLISM;
Keywords:
TRYPANOSOME; GLYCEROL 3-PHOSPHATE DEHYDROGENASE; RATIONAL DRUG DESIGN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
44
Recensione:
Indirizzi per estratti:
Citazione:
C.E. Stebeck et al., "MOLECULAR CHARACTERIZATION OF GLYCOSOMAL NAD(-DEPENDENT GLYCEROL 3-PHOSPHATE DEHYDROGENASE FROM TRYPANOSOMA-BRUCEI-RHODESIENSE())", Molecular and biochemical parasitology, 76(1-2), 1996, pp. 145-158

Abstract

The primary structure of a 38-kDa protein isolated from membrane preparations of African trypanosomes was determined by protein and DNA sequencing. Searching of the protein database with the trypanosome translated amino acid sequence identified glycerol 3-phosphate dehydrogenase(EC 1.1.1.8) from various prokaryotic and eukaryotic organisms as theoptimal scoring protein. Surprisingly, the eukaryotic trypanosome enzyme showed the highest degree of sequence identity with the corresponding enzyme from the prokaryote Escherichia coli. The trypanosome molecule was expressed in Escherichia coli and found to be enzymatically active, thus confirming the identity of the molecule as an NAD(+)-dependent glycerol 3-phosphate dehydrogenase. A monoclonal antibody specificfor the 38-kDa protein was used to localize the enzyme to glycosomes. Immunoblotting showed that the monoclonal antibody bound to a 38-kDa protein in African trypanosomes but not in T. cruzi, Leishmania or Crithidia. The enzyme has a pI of 9.1, a net charge of + 17 and contains the peroxisome-like targeting tripeptide SKIM at its C-terminus, all characteristic of glycosomal enzymes. Amino acids predicted to be involved in the NAD(+)-dependent glycerol 3-phosphate dehydrogenase active site have diverged from those of the mammalian enzyme. Kinetic analyses of the trypanosome GPD and CPD from rabbit muscle showed that the K-m values of the two enzymes are different. The data suggest that the trypanosome protein may be a candidate target for rational drug design.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/12/20 alle ore 18:07:34