Literature summary for 4.2.1.28 extracted from

Fukuoka, M.; Nakanishi, Y.; Hannak, R.B.; Krautler, B.; Toraya, T.
Homoadenosylcobalamins as probes for exploring the active sites of coenzyme B12-dependent diol dehydratase and ethanolamine ammonia-lyase (2005), FEBS J., 272, 4787-4796.

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Inhibitors

Inhibitors	Comment	Organism	Structure
adenosylethylcobalamin	strong competitive inhibitor	Klebsiella oxytoca
adenosylmethylcobalamin	catalytic efficiency (turnover number to Km-value) of the holoenzyme with adenosylmethylcobalamin is 0.15% of that for the regular coenzyme adenosylcobalamin, Km: 0.0017 mM	Klebsiella oxytoca
adenosylpentylcobalamin	strong competitive inhibitor	Klebsiella oxytoca

Organism

Organism	UniProt	Comment	Textmining
Klebsiella oxytoca	-	recombinant	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
propane-1,2-diol	-	Klebsiella oxytoca	propanal + H2O	-	?

Cofactor

Cofactor	Comment	Organism	Structure
adenosylcobalamin	KM: 0.0008 mM	Klebsiella oxytoca

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.0011	-	adenosylmethylcobalamin	-	Klebsiella oxytoca
0.0015	-	adenosylethylcobalamin	-	Klebsiella oxytoca

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Release 2023.1 (January 2023)