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Titolo:
BACTERIAL AMINOPEPTIDASES - PROPERTIES AND FUNCTIONS
Autore:
GONZALES T; ROBERTBAUDOUY J;
Indirizzi:
INST NATL SCI APPL,LAB GENET MOL MICROORGANISMES & INTERACT CELLULAI,CNRS,UMR 5577 F-69621 VILLEURBANNE FRANCE INST NATL SCI APPL,LAB GENET MOL MICROORGANISMES & INTERACT CELLULAI,CNRS,UMR 5577 F-69621 VILLEURBANNE FRANCE
Titolo Testata:
FEMS microbiology reviews
fascicolo: 4, volume: 18, anno: 1996,
pagine: 319 - 344
SICI:
0168-6445(1996)18:4<319:BA-PAF>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROLYL-DIPEPTIDYL-AMINOPEPTIDASE; LACTIS SUBSP CREMORIS; PYRROLIDONE CARBOXYL PEPTIDASE; AEROMONAS-PROTEOLYTICA AMINOPEPTIDASE; STREPTOMYCES-GRISEUS AMINOPEPTIDASE; INTRACELLULAR PROTEIN DEGRADATION; LACTOBACILLUS-HELVETICUS CNRZ-32; NUCLEOTIDE-SEQUENCE ANALYSIS; PROLINE IMINOPEPTIDASE GENE; ESCHERICHIA-COLI;
Keywords:
AMINOPEPTIDASE; CLASSIFICATION; CATALYTIC MECHANISM; LOCATION; FUNCTION;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
248
Recensione:
Indirizzi per estratti:
Citazione:
T. Gonzales e J. Robertbaudouy, "BACTERIAL AMINOPEPTIDASES - PROPERTIES AND FUNCTIONS", FEMS microbiology reviews, 18(4), 1996, pp. 319-344

Abstract

Aminopeptidases are exopeptidases that selectively release N-terminalamino acid residues from polypeptides and proteins. Bacteria display several aminopeptidasic activities which may be localised in the cytoplasm, on membranes, associated with the cell envelope or secreted intothe extracellular media. Studies on the bacterial aminopeptide systemhave been carried out over the past three decades and are significantin fundamental and biotechnological domains. At present, about one hundred bacterial aminopeptidases have been purified and biochemically studied. About forty genes encoding aminopeptidases have also been cloned and characterised. Recently, the three-dimensional structure of twoaminopeptidases, the methionine aminopeptidase from Escherichia coli and the leucine aminopeptidase from Aeromonas proteolytica, have been elucidated by crystallographic studies. Most of the quoted studies demonstrate that bacterial aminopeptidases generally show Michaelis-Menten kinetics and can be placed into either of two categories based on their substrate specificity: broad or narrow. These enzymes can also be classified by another criterium based on their catalytic mechanism: metallo-, cysteine- and serine-aminopeptidases, the former type being predominant in bacteria. Aminopeptidases play a role in several important physiological processes. It is noteworthy that some of them take part in the catabolism of exogenously supplied peptides and are necessaryfor the final steps of protein turnover. In addition, they are involved in some specific functions, such as the cleavage of N-terminal methionine from newly synthesised peptide chains (methionine aminopeptidases), the stabilisation of multicopy ColE1 based plasmids (aminopeptidase A) and the pyroglutamyl aminopeptidase (Pcp) present in many bacteria and responsible for the cleavage of the N-terminal pyroglutamate.

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Documento generato il 20/09/20 alle ore 03:46:03