Conserved and Nonconserved Residues in the Substrate Binding Site of 7,8-Diaminopelargonic Acid Synthase from Escherichia coli Are Essential for Catalysis

Biochemistry

Volumn 43, Issue 5, 2004, Pages 1213-1222

  Sandmark, Jenny ^a   Eliot, Andrew C ^b   Famm, Kristoffer ^b   Schneider, Gunter ^a   Kirsch, Jack F ^b  

^a KAROLINSKA INSTITUTE   (Sweden)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CATALYST ACTIVITY; CRYSTALLOGRAPHY; ENZYME KINETICS; ESCHERICHIA COLI; MUTAGENESIS;

KINETIC DEFICIENCIES;

AMINO ACIDS;

7,8 DIAMINOPELARGONIC ACID SYNTHASE; 8 AMINO 7 OXONONANOIC ACID; AMINO ACID; ARGININE; BIOTIN; NONANOIC ACID; S ADENOSYLMETHIONINE; SYNTHETASE; TYROSINE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CATALYSIS; CRYSTALLOGRAPHY; DECARBOXYLATION; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; ESCHERICHIA COLI; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN SYNTHESIS;

ALANINE; AMINATION; AMINO ACIDS, DIAMINO; ARGININE; BINDING SITES; CATALYSIS; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI PROTEINS; GLUTAMINE; KINETICS; LYSINE; MUTAGENESIS, SITE-DIRECTED; S-ADENOSYLMETHIONINE; SUBSTRATE SPECIFICITY; TRANSAMINASES; TYROSINE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0842283070     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0358059     Document Type: Article

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