THE 5 CYSTEINE RESIDUES LOCATED IN THE ACTIVE-SITE REGION OF BOVINE ASPARTYL-(ASPARAGINYL)-BETA-HYDROXYLASE ARE NOT ESSENTIAL FOR CATALYSIS

Authors
MCGINNIS K KU GM FU J STERN AM FRIEDMAN PA
Citation
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
Citations number
17
Categorie Soggetti
Biology,Biophysics
Journal title
Biochimica et biophysica acta. Protein structure and molecular enzymology → ACNP
ISSN journal
01674838
Volume
1387
Issue
1-2
Year of publication
1998
Pages
454 - 456
Database
ISI
SICI code
0167-4838(1998)1387:1-2<454:T5CRLI>2.0.ZU;2-Z
Abstract
In previous chemical modification studies on bovine aspartyl (asparagi nyl) P-hydroxylase, cysteines were implicated as critical catalytic re sidues. Using site-directed mutagenesis, the five cysteine residues lo cated in a highly conserved region of the enzyme identified as the act ive site were individually mutated to alanine. Substitutions at cystei ne 637, 644, 656, 681, and 696 resulted in active mutant enzymes indic ating that these residues are not required for catalysis. (C) 1998 Els evier Science B.V. All rights reserved.