Structural studies of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica: The apo, substrate, and product-aldimine complexes

Biochemistry

Volumn 41, Issue 29, 2002, Pages 9079-9089

  Cheong, Cheom Gil ^a   Escalante Semerena, Jorge C ^a   Rayment, Ivan ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

STEREOCHEMICAL PROPERTIES;

BIOSYNTHESIS; DECARBONIZATION; ENZYMES; HYDROGEN; PHOSPHATES;

BIOCHEMISTRY;

AMINOTRANSFERASE; BACTERIAL ENZYME; CARBOXYLYASE; COBALAMIN; HISTIDINOL; HISTIDINOL PHOSPHATASE; PROPANOL; THREONINE; THREONINE O 3 PHOSPHATE DECARBOXYLASE; UNCLASSIFIED DRUG;

ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; DECARBOXYLATION; ENZYME ANALYSIS; ENZYME STRUCTURE; ENZYME SUBSTRATE; MOLECULAR EVOLUTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; REACTION ANALYSIS; SALMONELLA ENTERICA; STEREOCHEMISTRY; STRUCTURE ANALYSIS; SYNTHESIS;

BINDING SITES; CARBOXY-LYASES; CRYSTALLIZATION; IMINES; MODELS, MOLECULAR; PROTEIN CONFORMATION; SALMONELLA ENTERICA; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); NEGIBACTERIA; SALMONELLA; SALMONELLA ENTERICA;

EID: 0037162411     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi020294w     Document Type: Article

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