Allosteric activation and contrasting properties of l-serine dehydratase types 1 and 2

Biochemistry

Volumn 51, Issue 26, 2012, Pages 5320-5328

  Chen, Shawei ^a   Xu, Xiao Lan ^a   Grant, Gregory A ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ALLOSTERIC ACTIVATION; ALLOSTERIC SITE; BACILLUS SUBTILIS; D-3-PHOSPHOGLYCERATE DEHYDROGENASE; D-SERINE; HIGH CONCENTRATION; L-SERINE; LEGIONELLA PNEUMOPHILA; LOW CONCENTRATIONS; MONOVALENT ANIONS; MONOVALENT CATIONS; PROSTHETIC GROUPS; PYRUVATES; SERINE BINDING; SUBSTRATE BINDING; TANDEM ARRANGEMENT;

CHEMICAL ACTIVATION; ENZYMES; MAMMALS; OLIGOMERS; POSITIVE IONS; SULFUR;

AMINO ACIDS;

BACTERIAL ENZYME; CATION; FLUORIDE; IRON; OXYGEN; POTASSIUM; PYRUVIC ACID; SERINE; SERINE DEHYDRATASE; SERINE DEHYDRATASE 1; SERINE DEHYDRATASE 2; SULFUR; UNCLASSIFIED DRUG;

ALLOSTERISM; ARTICLE; BACILLUS SUBTILIS; BINDING COMPETITION; CONCENTRATION RESPONSE; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME KINETICS; ENZYME PURIFICATION; ENZYME SUBSTRATE COMPLEX; ENZYME SUBUNIT; LEGIONELLA PNEUMOPHILA; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION;

ALLOSTERIC REGULATION; BACILLUS SUBTILIS; L-SERINE DEHYDRATASE; LEGIONELLA PNEUMOPHILA; MODELS, BIOLOGICAL;

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS); LEGIONELLA PNEUMOPHILA; MAMMALIA;

EID: 84863531194     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300523p     Document Type: Article

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