Site-directed mutagenesis of residues in a conserved region of bovine aspartyl (asparaginyl) β-hydroxylase: Evidence that histidine 675 has a role in binding Fe2+

Biochemistry

Volumn 35, Issue 13, 1996, Pages 3957-3962

  McGinnis, Kathleen ^a   Ku, Gregory M ^a   VanDusen, William J ^a   Fu, Jeffrey ^a   Garsky, Victor ^a   Stern, Andrew M ^a   Friedman, Paul A ^a  

^a MERCK RESEARCH LABORATORIES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FERROUS ION; OXYGENASE;

ARTICLE; CATTLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME KINETICS; HYDROXYLATION; NONHUMAN; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CATTLE; CHICKENS; CONSERVED SEQUENCE; HISTIDINE; HUMANS; IRON; KINETICS; MIXED FUNCTION OXYGENASES; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; POINT MUTATION; RECOMBINANT PROTEINS; RESTRICTION MAPPING; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0029943823     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi951520n     Document Type: Article

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