Thiamin diphosphate-dependent enzymes: From enzymology to metabolic regulation, drug design and disease models

FEBS Journal

Volumn 280, Issue 24, 2013, Pages 6412-6442

  Bunik, Victoria I ^a   Tylicki, Adam ^b   Lukashev, Nikolay V ^a  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

^b UNIVERSITY OF BIALYSTOK   (Poland)

Author keywords

2 oxoglutarate dehydrogenase; amprolium; metabolic reprogramming in cancer; molecular mechanisms of neurodegeneration; oxythiamin; phosphonate analog of 2 oxo acid; pyrithiamin; pyruvate dehydrogenase; succinyl phosphonate; transketolase

Indexed keywords

5 KETOCLOMAZONE; ACETYL PHOSPHINATE; ACETYL PHOSPHONATE; AMPROLIUM; ANTIINFECTIVE AGENT; ANTIMETABOLITE; CARBOXY ETHYL ESTER; CLOMAZONE; FUNGICIDE; HERBICIDE; IMATINIB; METHYL ACETYL PHOSPHINATE; METRONIDAZOLE; OXYTHIAMINE; PHOSPHONIC ACID DERIVATIVE; PHOSPHONO ETHYL ESTER; PHOSPHONO METHYL ESTER; PRASTERONE; PYRITHIAMINE; PYRUVATE DEHYDROGENASE; SUCCINYL PHOSPHONATE; THIAMIN DIPHOSPHATE DEPENDENT ENZYME; THIAMINE; UNCLASSIFIED DRUG;

ANTINEOPLASTIC ACTIVITY; BINDING AFFINITY; CANCER CELL; CANCER COMBINATION CHEMOTHERAPY; CELL PROLIFERATION; COCCIDIOSIS; CONCENTRATION RESPONSE; DRUG BINDING SITE; DRUG DESIGN; DRUG MECHANISM; DRUG SELECTIVITY; DRUG STRUCTURE; ELECTROPHILICITY; ENZYME ACTIVE SITE; ENZYME INHIBITION; ENZYME MECHANISM; ENZYME METABOLISM; ENZYME PHOSPHORYLATION; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SYNTHESIS; HOMEOSTASIS; HUMAN; HYDROLYSIS; IC 50; METABOLIC REGULATION; NERVE DEGENERATION; NONHUMAN; PHARMACOLOGICAL BLOCKING; PRIORITY JOURNAL; PROTEIN TARGETING; REVIEW; THIAMINE DEFICIENCY;

2-OXOGLUTARATE DEHYDROGENASE; AMPROLIUM; METABOLIC REPROGRAMMING IN CANCER; MOLECULAR MECHANISMS OF NEURODEGENERATION; OXYTHIAMIN; PHOSPHONATE ANALOG OF 2-OXO ACID; PYRITHIAMIN; PYRUVATE DEHYDROGENASE; SUCCINYL PHOSPHONATE; TRANSKETOLASE;

ANIMALS; DISEASE MODELS, ANIMAL; DRUG DESIGN; ENZYMES; HUMANS; METABOLISM; THIAMINE PYROPHOSPHATE;

ANIMALIA; FUNGI; MAMMALIA;

EID: 84889667074     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12512     Document Type: Review

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