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Literature summary 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.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.28 adenosylethylcobalamin strong competitive inhibitor Klebsiella oxytoca
4.2.1.28 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
4.2.1.28 adenosylpentylcobalamin strong competitive inhibitor Klebsiella oxytoca
4.3.1.7 adenosylmethylcobalamin 0.1% coenzyme activity compared to adenosylcobalamin, holoenzyme with adenosylmethylcobalamin undergoes rapid inactivation Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.28 Klebsiella oxytoca
-
recombinant
-
4.3.1.7 Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

Cofactor

EC Number Cofactor Comment Organism Structure
4.2.1.28 adenosylcobalamin KM: 0.0008 mM Klebsiella oxytoca
4.3.1.7 adenosylcobalamin
-
Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.2.1.28 0.0011
-
adenosylmethylcobalamin
-
Klebsiella oxytoca
4.2.1.28 0.0015
-
adenosylethylcobalamin
-
Klebsiella oxytoca