Diol dehydratase‐reactivating factor is a reactivase - evidence for multiple turnovers and subunit swapping with diol dehydratase

Adenosylcobalamin‐dependent diol dehydratase (DD) undergoes suicide inactivation by glycerol, one of its physiological substrates, resulting in the irreversible cleavage of the coenzyme Co-C bond. The damaged cofactor remains tightly bound to the active site. The DD‐reactivating factor reactivates t...

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Veröffentlicht in:	The FEBS journal 2010-12, Vol.277 (23), p.4931-4943
Hauptverfasser:	Mori, Koichi, Hosokawa, Yasuhiro, Yoshinaga, Toshiyuki, Toraya, Tetsuo
Format:	Artikel
Sprache:	eng
Schlagworte:	active sites adenine adenosine diphosphate adenosine triphosphate Adenosine Triphosphate - metabolism adenosylcobalamin ADP amino acid sequences Bacterial Proteins - chemistry Bacterial Proteins - metabolism Biochemistry Catalysis Chemical bonds Cobamides coenzyme B12 coenzymes Coenzymes - metabolism crystal structure diol dehydratase diol dehydratase‐reactivating factor dissociation enzyme activation enzyme inactivation Enzyme Reactivators - chemistry Enzyme Reactivators - metabolism Enzymes glycerol Holoenzymes - metabolism Kinetics Klebsiella - metabolism Klebsiella pneumoniae - metabolism magnesium Magnesium - metabolism metal ions Models, Biological Models, Molecular Multiprotein Complexes - chemistry Multiprotein Complexes - metabolism nucleosides propanediol dehydratase Propanediol Dehydratase - chemistry Propanediol Dehydratase - metabolism Protein Subunits reactivase Recombinant Proteins - chemistry Recombinant Proteins - metabolism Substrates Vitamin B 12 - metabolism vitamin B12
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