Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
CLONING AND EXPRESSION OF DIPEPTIDASE FROM ACINETOBACTER-CALCOACETICUS ATCC-23055
Autore:
ADACHI H; TSUJIMOTO M;
Indirizzi:
SUNTORY LTD,INST BIOMED RES SHIMAMOTO OSAKA 618 JAPAN
Titolo Testata:
Journal of Biochemistry
fascicolo: 3, volume: 118, anno: 1995,
pagine: 555 - 561
SICI:
0021-924X(1995)118:3<555:CAEODF>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN RENAL DIPEPTIDASE; HUMAN MICROSOMAL DIPEPTIDASE; ESCHERICHIA-COLI; NUCLEOTIDE-SEQUENCE; PURIFICATION; CLONES; PCR;
Keywords:
ACINETOBACTER CALCOACETICUS; D-AMINO ACID; ANCESTRAL GENE; CO2+; RENAL DIPEPTIDASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
24
Recensione:
Indirizzi per estratti:
Citazione:
H. Adachi e M. Tsujimoto, "CLONING AND EXPRESSION OF DIPEPTIDASE FROM ACINETOBACTER-CALCOACETICUS ATCC-23055", Journal of Biochemistry, 118(3), 1995, pp. 555-561

Abstract

The gene encoding dipeptidase was cloned from Acinetobacter calcoaceticus ATCC 23055. Determination of the nucleotide sequence revealed that the gene had an open reading dame of 1,050 bp coding a protein of 350 amino acids. The deduced amino acid sequence showed 48.8% similarityto human renal dipeptidase and conserved two amino acid residues identified in human and pig renal dipeptidases as essential ones for the catalytic activity, Purified recombinant enzyme expressed in Escherichia coli did not hydrolyze the unsaturated dipeptide, glycyldehydrophenylalanine. On the other hand, it preferentially hydrolyzed dipeptides having a D-amino acid, when compared with those having an L-amino acid at the C-terminal. Furthermore, it could not hydrolyze tripeptides. These results indicate that the dipeptidase produced by A. calcoaceticusATCC 23055 has a unique substrate specificity and preferentially hydrolyzes dipeptides having a D-amino acid at the C-terminal.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 00:17:47