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Titolo:
Comparative biochemistry of bacterial N-acyl-D-amino acid amidohydrolase
Autore:
Wakayama, M; Moriguchi, M;
Indirizzi:
Oita Univ, Fac Engn, Dept Appl Chem, Oita 8701192, Japan Oita Univ Oita Japan 8701192 c Engn, Dept Appl Chem, Oita 8701192, Japan
Titolo Testata:
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
fascicolo: 1-6, volume: 12, anno: 2001,
pagine: 15 - 25
SICI:
1381-1177(20010228)12:1-6<15:CBOBNA>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
SUBSP XYLOSOXYDANS A-6; D-GLUTAMATE AMIDOHYDROLASE; D-ASPARTATE OXIDASE; BETA-LACTAM COMPOUND; PSEUDOMONAS SP 1158; SP STRAIN 5F-1; D-AMINOACYLASE; ALCALIGENES-DENITRIFICANS; ESCHERICHIA-COLI; THERMOSTABLE AMINOACYLASE;
Keywords:
N-acyl-D-amino acid; amidohydrolase; Alcaligenes; enzyme characterization; primary structure;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
78
Recensione:
Indirizzi per estratti:
Indirizzo: Moriguchi, M Oita Univ, Fac Engn, Dept Appl Chem, Oita 8701192, Japan OitaUniv Oita Japan 8701192 Appl Chem, Oita 8701192, Japan
Citazione:
M. Wakayama e M. Moriguchi, "Comparative biochemistry of bacterial N-acyl-D-amino acid amidohydrolase", J MOL CAT B, 12(1-6), 2001, pp. 15-25

Abstract

N-acyl-D-amino acid amidohydrolases can be classified into three types based on substrate specificity. D-aminoacylase has been reported to occur in avery few bacteria such as Pseudomonas. Streptomyces. and Alcaligenes. N-acyl-D-aspartate ami dohydrolase (D-AAase) has been reported in only Alcaligenes xylosoxydans subsp. xylosoxydans A-6 (Alcaligenes A-6) while N-acyl-D-glutamate amidohydrolase (D-AGase) has been isolated in two stains of Pseudomonas sp. 5f-1 and Alcaligenes A-6. The physiological roles of these enzymes in these microbes are not clear. They are individually characteristic in their substrate specificities. inducer profiles, inhibitors, isoelectric points. metal dependency, and some physicochemical properties. The primary structures of all the three types of N-acyl-D-amino acid amidohydrolases fromAlcaligenes A-6 were determined from their nucleotide sequences. Comparison of their primary structures revealed high homology (46-56%) between the different enzymes. The three enzymes showed 26-27% sequence homology with L-aminoacylases from Bacillus stearothermophilus, porcine, and human. Chemical modification and site-directed mutagenesis identified the histidyl residues essential for catalysis. The Alcaligenes N-acyl-D-amino acid amidohydrolases share significant sequence similarities with some members of the urease-related amidohydrolase superfamily proposed by Helm and Sander [L. Helm, C. Sander. Proteins: Structure, Function and Genetics 28 (1997) 72]. (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 17:07:52