Insights into enzyme evolution revealed by the structure of methylaspartate ammonia lyase

Structure

Volumn 10, Issue 1, 2002, Pages 105-113

  Levy, C W ^a   Buckley, P A ^a   Sedelnikova, S ^a   Kato, Y ^b   Asano, Y ^b   Rice, D W ^a   Baker, P J ^a  

^a UNIVERSITY OF SHEFFIELD   (United Kingdom)

^b TOYAMA PREFECTURAL UNIVERSITY   (Japan)

Author keywords

Enolase superfamily; Evolution; MAD phasing; Methylaspartate ammonia lyase; Selenomethionine; X ray crystallography

Indexed keywords

AMMONIA LYASE; ASPARTIC ACID DERIVATIVE; ENOLASE; MAGNESIUM; METHYLASPARTATE AMMONIA LYASE; PHENYLALANINE AMMONIA LYASE; UNCLASSIFIED DRUG;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CITROBACTER; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBUNIT; MOLECULAR EVOLUTION; NONHUMAN; PRIORITY JOURNAL; PROTON TRANSPORT; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; AMMONIA-LYASES; BINDING SITES; CITROBACTER; CRYSTALLOGRAPHY, X-RAY; EVOLUTION, MOLECULAR; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY;

CITROBACTER; CITROBACTER AMALONATICUS; NEGIBACTERIA;

EID: 0036151237     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(01)00696-7     Document Type: Article

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