Site-directed mutagenesis and biochemical analysis of the endogenous ligands in the ferrous active site of clavaminate synthase. The His-3 variant of the 2-His-1-carboxylate model

Biochemistry

Volumn 39, Issue 29, 2000, Pages 8666-8673

  Khaleeli, Nusrat ^a   Busby, Robert W ^a,b   Townsend, Craig A ^a  

^a JOHNS HOPKINS UNIVERSITY   (United States)

^b Microbia PE Inc   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

2 OXOGLUTARIC ACID; ASPARTIC ACID; CARBAPENEM; CARBOXYLIC ACID DERIVATIVE; CLAVAMINATE SYNTHASE; CLAVULANIC ACID; GLUTAMIC ACID; HISTIDINE; ISOENZYME; LIGAND; OXYGENASE; UNCLASSIFIED DRUG;

ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME MODIFICATION; METAL BINDING; PRIORITY JOURNAL; PROTEIN FAMILY; SITE DIRECTED MUTAGENESIS;

AFFINITY LABELS; AMINO ACID SEQUENCE; BASE SEQUENCE; CATALYTIC DOMAIN; CIRCULAR DICHROISM; DNA PRIMERS; HISTIDINE; IRON; LIGANDS; MIXED FUNCTION OXYGENASES; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; SEQUENCE HOMOLOGY, AMINO ACID; STREPTOMYCES; VARIATION (GENETICS);

EID: 0034713902     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi000534c     Document Type: Article

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