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Titolo:
THE 5 CYSTEINE RESIDUES LOCATED IN THE ACTIVE-SITE REGION OF BOVINE ASPARTYL-(ASPARAGINYL)-BETA-HYDROXYLASE ARE NOT ESSENTIAL FOR CATALYSIS
Autore:
MCGINNIS K; KU GM; FU J; STERN AM; FRIEDMAN PA;
Indirizzi:
CARE OF JEFFREY FU,MERCK & CO INC,WP37T2-3 W POINT PA 19486 MERCK RES LABS W POINT PA 19486
Titolo Testata:
Biochimica et biophysica acta. Protein structure and molecular enzymology
fascicolo: 1-2, volume: 1387, anno: 1998,
pagine: 454 - 456
SICI:
0167-4838(1998)1387:1-2<454:T5CRLI>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
GROWTH-FACTOR PRECURSOR; DIRECTED MUTAGENESIS; HISTIDINE-RESIDUES; DOMAINS; IDENTIFICATION; PURIFICATION; DIOXYGENASES; VERTEBRATE; MODULES;
Keywords:
CYSTEINE; SITE-DIRECTED MUTAGENESIS; ASP (ASN) BETA-HYDROXYLASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
17
Recensione:
Indirizzi per estratti:
Citazione:
K. Mcginnis et al., "THE 5 CYSTEINE RESIDUES LOCATED IN THE ACTIVE-SITE REGION OF BOVINE ASPARTYL-(ASPARAGINYL)-BETA-HYDROXYLASE ARE NOT ESSENTIAL FOR CATALYSIS", Biochimica et biophysica acta. Protein structure and molecular enzymology, 1387(1-2), 1998, pp. 454-456

Abstract

In previous chemical modification studies on bovine aspartyl (asparaginyl) P-hydroxylase, cysteines were implicated as critical catalytic residues. Using site-directed mutagenesis, the five cysteine residues located in a highly conserved region of the enzyme identified as the active site were individually mutated to alanine. Substitutions at cysteine 637, 644, 656, 681, and 696 resulted in active mutant enzymes indicating that these residues are not required for catalysis. (C) 1998 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 01/12/20 alle ore 07:58:55