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Titolo:
Sequence analysis of the aminoacylase-1 family. A new proposed signature for metalloexopeptidases
Autore:
Biagini, A; Puigserver, A;
Indirizzi:
Univ Aix Marseille 3, UMR, Inst Mediterraneen Rech & Nutr, Fac Sci & Tech St Jerome, F-13397 Marseille 20, France Univ Aix Marseille 3 Marseille France 20 e, F-13397 Marseille 20, France
Titolo Testata:
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY
fascicolo: 3, volume: 128, anno: 2001,
pagine: 469 - 481
SICI:
1096-4959(200103)128:3<469:SAOTAF>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
STREPTOMYCES-GRISEUS AMINOPEPTIDASE; AMINO-ACID AMIDOHYDROLASE; MOLECULAR-CLONING; ESCHERICHIA-COLI; BACILLUS-STEAROTHERMOPHILUS; ACETYLORNITHINE DEACETYLASE; GLYCOSYL HYDROLASES; KIDNEY AMINOACYLASE; NUCLEOTIDE-SEQUENCE; PSEUDOMONAS STRAIN;
Keywords:
metalloexopeptidase; acylase; deacetylase; dipeptidase; aminopeptidase; carboxypeptidase; protein C; amidohydrolase; desuccinylase; sequence alignments;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
58
Recensione:
Indirizzi per estratti:
Indirizzo: Biagini, A Univ Aix Marseille 3, UMR, Inst Mediterraneen Rech & Nutr, Fac Sci & Tech St Jerome, F-13397 Marseille 20, France Univ Aix Marseille 3 Marseille France 20 Marseille 20, France
Citazione:
A. Biagini e A. Puigserver, "Sequence analysis of the aminoacylase-1 family. A new proposed signature for metalloexopeptidases", COMP BIOC B, 128(3), 2001, pp. 469-481

Abstract

The amino acid sequence analysis of the human and porcine aminoacylases-1,the carboxypeptidase S precursor from Saccharomyces cerevisiae, the succinyl-diaminopimelate desuccinylase from Escherichia coli, Haemophilus influenzae and Corynebacterium glutamicum, the acetylornithine deacetylase from Escherichia coli and Dictyostelium discoideum and the carboxypeptidase G(2) precursor from Pseudomonas strain, using the Basic Local Alignment Search Tool (BLAST) and the Position-Specific Iterated BLAST (PSI-BLAST), allowed usto suggest that all these enzymes, which share common functional and biochemical features, belong to the same structural family. The three amino acidblocks which were found to be highly conserved, using the CLUSTAL W program, could be assigned to the catalytic active site, based on the general three-dimensional structure of the carboxypeptidase G(2) from the Pseudomonas str ain precursor. Six additional proteins with the same signature have been retrieved after performing two successive PSI-BLAST iterations using the sequence of the conserved motif, namely Lactobacillus delbrueckii aminoacyl-histidine dipeptidase, Streptomyces griseus aminopeptidase, Saccharomyces cerevisiae aminopeptidase Y precursor, two Bacillus stearothermophilus N-carbamyl-L-amino acid amidohydrolases and Pseudomonas sp. hydantoin utilization protein C. The three conserved amino acid motifs corresponded to the following blocks: (i) [S, G, A]-H-x-D-x-V; (ii) G-x-x-D; and (iii) x-E-E. Thisnew sequence signature is clearly different from that commonly reported inthe literature for proteins belonging to the ArgE/DapE/CPG2/YscS family. (C) 2001 Elsevier Science Inc. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/10/20 alle ore 00:32:49