Literature summary for 4.2.1.30 extracted from

Toraya, T.
Radical catalysis of B12 enzymes: structure, mechanism, inactivation, and reactivation of diol and glycerol dehydratases (2000), Cell. Mol. Life Sci., 57, 106-127.

Search for more literature for 4.2.1.30

Activating Compound

Activating Compound	Comment	Organism	Structure
GdrA	GdrA-GdrB complex reactivates the enzyme in the presence of ATP, Mg2+ and adenosylcobalamin, the reactivating factor mediates ATP-dependent exchange of the enzyme-bound, adenine-lacking cobalamin, for free adenosylcobalamin, an adenine-containing cobalamin, through intermediary formation of apoenzyme in the presence of ATP and Mg2+	Klebsiella pneumoniae
GdrA	GdrA-GdrB complex reactivates the enzyme in the presence of ATP, Mg2+ and adenosylcobalamin, the reactivating factor mediates ATP-dependent exchange of the enzyme-bound, adenine-lacking cobalamin, for free adenosylcobalamin, an adenine-containing cobalamin, through intermediary formation of apoenzyme in the presence of ATP and Mg2+	Klebsiella oxytoca
GdrB	GdrA-GdrB complex reactivates the enzyme in the presence of ATP, Mg2+ and adenosylcobalamin, the reactivating factor mediates ATP-dependent exchange of the enzyme-bound, adenine-lacking cobalamin, for free adenosylcobalamin, an adenine-containing cobalamin, through intermediary formation of apoenzyme in the presence of ATP and Mg2+	Klebsiella pneumoniae
GdrB	GdrA-GdrB complex reactivates the enzyme in the presence of ATP, Mg2+ and adenosylcobalamin, the reactivating factor mediates ATP-dependent exchange of the enzyme-bound, adenine-lacking cobalamin, for free adenosylcobalamin, an adenine-containing cobalamin, through intermediary formation of apoenzyme in the presence of ATP and Mg2+	Klebsiella oxytoca

Inhibitors

Inhibitors	Comment	Organism	Structure
glycerol	irreversible cleavage of the Co-C bond, forming 5'-deoxyadenosine and an unknown cobalamin species. The unknown cobalamin species is converted very slowly to OH-cobalamin. The cobalamin species that is formed remains tightly bound to the enzyme, inactivating the enzyme irreversibly	Klebsiella oxytoca
glycerol	irreversible cleavage of the Co-C bond, forming 5'-deoxyadenosine and an unknown cobalamin species. The unknown cobalamin species is converted very slowly to OH-cobalamin. The cobalamin species that is formed remains tightly bound to the enzyme, inactivating the enzyme irreversibly	Klebsiella pneumoniae

Organism

Organism	UniProt	Comment	Textmining
Klebsiella oxytoca	-	-	-
Klebsiella pneumoniae	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
glycerol	-	Klebsiella pneumoniae	3-hydroxypropanal + H2O	-	?
glycerol	-	Klebsiella oxytoca	3-hydroxypropanal + H2O	-	?

Cofactor

Cofactor	Comment	Organism	Structure
coenzyme B12	-	Klebsiella pneumoniae
coenzyme B12	-	Klebsiella oxytoca

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Release 2023.1 (January 2023)