The thiamine biosynthetic enzyme thic catalyzes multiple turnovers and is inhibited by S-Adenosylmethionine (AdoMet) metabolites

Journal of Biological Chemistry

Volumn 288, Issue 42, 2013, Pages 30693-30699

  Palmer, Lauren D ^a   Downs, Diana M ^a  

^a UNIVERSITY OF GEORGIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHETIC ENZYMES; CATALYTIC RATES; CATALYTIC TURNOVER; S-ADENOSYLMETHIONINE;

ENZYMES; METABOLITES;

BIOMOLECULES;

4 AMINO 5 HYDROXYMETHYL 2 METHYLPYRIMIDINE PHOSPHATE SYNTHASE; 5' DEOXYADENOSINE; ADENOSINE; ADENOSINE DERIVATIVE; DEOXYADENOSINE DERIVATIVE; ENZYME; HOMOCYSTEINE; METHIONINE; PYRIMIDINE DERIVATIVE; S ADENOSYLHOMOCYSTEINE; S ADENOSYLMETHIONINE; S METHYL 5' THIOADENOSINE; THIAMINE BIOSYNTHETIC ENZYME; THIAMINE PYRIMIDINE 4 AMINO 5 HYDROXYMETHYL 2 METHYLPYRIMIDINE PHOSPHATE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME MECHANISM; ENZYME METABOLISM; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; SYNTHESIS;

ENZYME INHIBITORS; IRON-SULFUR PROTEIN; RADICALS; S-ADENOSYLMETHIONINE (ADOMET); THIAMINE; THIAMINE BIOSYNTHESIS;

BACTERIAL PROTEINS; CATALYSIS; KINETICS; S-ADENOSYLMETHIONINE; THIAMINE PYROPHOSPHATE; TREPONEMA DENTICOLA;

EID: 84886893789     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.500280     Document Type: Article

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