Literature summary for 4.2.1.28 extracted from

Toraya, T.; Tanokuchi, A.; Yamasaki, A.; Nakamura, T.; Ogura, K.; Tobimatsu, T.
Diol dehydratase-reactivase is essential for recycling of coenzyme B12 in diol dehydratase (2016), Biochemistry, 55, 69-78 .

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Organism

Organism	UniProt	Comment	Textmining
Klebsiella oxytoca	Q59470 and Q59471 and Q59472	Q59470 i.e. alpha-subunit pddA, Q59471 i.e. beta-subunit PddB, Q59472 i.e. gamma-subunit PddC	-
Klebsiella oxytoca ATCC 8724	Q59470 and Q59471 and Q59472	Q59470 i.e. alpha-subunit pddA, Q59471 i.e. beta-subunit PddB, Q59472 i.e. gamma-subunit PddC	-

General Information

General Information	Comment	Organism
physiological function	enzyme undergoes mechanism-based inactivation by glycerol and O2 inactivation in the absence of substrate, which accompanies irreversible cleavage of the coenzyme Co-C bond. Diol dehydratase activity is maintained through coenzyme recycling by a reactivating system for diol dehydratase composed of diol dehydratase-reactivase, PduO adenosyltransferase, and a reducing system. The releasing factor diol dehydratase-reactivase is essential for the recycling of adenosycobalamin, and PduO is a specific adenosylating enzyme for the diol dehydratase reactivation, whereas CobA and EutT exert their effects through free synthesized coenzyme	Klebsiella oxytoca

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Release 2023.1 (January 2023)