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Literature summary for 4.2.1.28 extracted from

  • Mori, K.; Hosokawa, Y.; Yoshinaga, T.; Toraya, T.
    Diol dehydratase-reactivating factor is a reactivase - evidence for multiple turnovers and subunit swapping with diol dehydratase (2010), FEBS J., 277, 4931-4943.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
diol dehydratase-reactivating factor both dehydratase-reactivating factors exist as alpha2beta2 heterotetramers, DdrA or GdrA and DdrB or GdrB, respectively. The diol dehydratase DD-reactivating factor reactivates the inactivated holoenzyme in the presence of ATP and Mg2+ by mediating the exchange of the tightly bound damaged cofactor for free intact coenzyme, overview. Mechanism of the reactivation of inactivated holoenzymes by reactivating factors, overview. The enzyme does not form a complex with the reactivating factor while it exists as an active holoenzyme. The reactivating factor binds ATP and hydrolyzes it to ADP by its own weak ATPase activity. The resulting ADP-bound form of the reactivating factor has a high affinity for the enzyme, and interacts with the inactivated holoenzyme to form a tight apoenzyme/reactivating factor complex, with the concomitant release of the damaged cofactor. The reactivating factor reverts to a low-affinity form through the replacement of bound ADP by free ATP, resulting in the dissociation of the apoenzyme/reactivating factor complex into apoenzyme and the reactivating factor, kinetics, overview Klebsiella oxytoca

Inhibitors

Inhibitors Comment Organism Structure
cyanocobalamin a tightly bound inactive coenzyme analogue lacking the adenine ring in the upper axial ligand, imitates the inactivated cofactor; a tightly bound inactive coenzyme analogue lacking the adenine ring in the upper axial ligand, imitates the inactivated cofactor; a tightly bound inactive coenzyme analogue lacking the adenine ring in the upper axial ligand, imitates the inactivated cofactor Klebsiella oxytoca
glycerol adenosylcobalamin-dependent diol dehydratase 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, it is not displaced by intact adenosylcobalamin, resulting in the irreversible inactivation of the enzyme. The DD-reactivating factor reactivates the inactivated holoenzyme in the presence of ATP and Mg2+ by mediating the exchange of the tightly bound damaged cofactor for free intact coenzyme, overview; adenosylcobalamin-dependent diol dehydratase 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, it is not displaced by intact adenosylcobalmin, resulting in the irreversible inactivation of the enzyme. The DD-reactivating factor reactivates the inactivated holoenzyme in the presence of ATP and Mg2+ by mediating the exchange of the tightly bound damaged cofactor for free intact coenzyme, overview; adenosylcobalamin-dependent diol dehydratase 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, it is not displaced by intact Ado-Cbl, resulting in the irreversible inactivation of the enzyme. The DD-reactivating factor reactivates the inactivated holoenzyme in the presence of ATP and Mg2+ by mediating the exchange of the tightly bound damaged cofactor for free intact coenzyme, overview Klebsiella oxytoca

Organism

Organism UniProt Comment Textmining
Klebsiella oxytoca Q59470 alpha-subunit
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Klebsiella oxytoca Q59471 beta-subunit
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Klebsiella oxytoca Q59472 gamma-subunit
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Synonyms

Synonyms Comment Organism
adenosylcobalamin-dependent diol dehydratase
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Klebsiella oxytoca
diol dehydratase
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Klebsiella oxytoca