Crystal structure of saccharopine reductase from Magnaporthe grisea, an enzyme of the α-aminoadipate pathway of lysine biosynthesis

Structure

Volumn 8, Issue 10, 2000, Pages 1037-1047

  Johansson, Eva ^a   Steffens, James J ^b   Lindqvist, Ylva ^a   Schneider, Gunter ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

^b DUPONT COMPANY   (United States)

Author keywords

Dehydrogenase; Enzyme mechanism; Intramolecular catalysis; NADPH; Plant pathogen; Rice blast

Indexed keywords

2 AMINOADIPIC ACID; ASPARTIC ACID; DIAMINOPIMELIC ACID; ENZYME; GLUTAMIC ACID; LYSINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SACCHAROPINE REDUCTASE; SCHIFF BASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; BIOSYNTHESIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIMERIZATION; ENZYME BINDING; ENZYME MECHANISM; EVOLUTION; HYDROGEN BOND; LIGAND BINDING; MAGNAPORTHE GRISEA; NONHUMAN; PRIORITY JOURNAL; SEQUENCE HOMOLOGY;

2-AMINOADIPIC ACID; AMINO ACID SEQUENCE; BINDING SITES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; FUNGAL PROTEINS; HYDROGEN BONDING; LIGANDS; LYSINE; MAGNAPORTHE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NADP; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SACCHAROPINE DEHYDROGENASES;

EID: 0034435381     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)00512-8     Document Type: Article

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