The five cysteine residues located in the active site region of bovine aspartyl (asparaginyl) β-hydroxylase are not essential for catalysis

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1387, Issue 1-2, 1998, Pages 454-456

  McGinnis, Kathleen ^a   Ku, Gregory M ^a   Fu, Jeffrey ^a   Stern, Andrew M ^a   Friedman, Paul A ^a  

^a MERCK RESEARCH LABORATORIES   (United States)

Author keywords

Asp (Asn) hydroxylase; Cysteine; Site directed mutagenesis

Indexed keywords

ALANINE; ASPARTIC ACID; CYSTEINE; OXYGENASE;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CATTLE; ENZYME ACTIVE SITE; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

ALANINE; ANIMALS; BINDING SITES; CATALYSIS; CATTLE; CYSTEINE; MIXED FUNCTION OXYGENASES; MUTAGENESIS, SITE-DIRECTED; RECOMBINANT PROTEINS;

BOVINAE;

EID: 0032497332     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(98)00130-7     Document Type: Article

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