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Literature summary for 4.2.1.28 extracted from

  • Moore, K.W.; Richards, J.H.
    Stereospecificity and mechanism of adenosylcobalamin-dependent diol dehydratase. Catalysis and inactivation with meso- and DL-2,3-butanediols as substrates (1979), Biochem. Biophys. Res. Commun., 87, 1052-1057.
    View publication on PubMed
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General Stability

General Stability Organism
ternary complex photostable, coenzyme alone photolabile Klebsiella pneumoniae

Inhibitors

Inhibitors Comment Organism Structure
2,3-Butanediol meso isomer strong inactivator and good substrate, Ki: 0.2 mM, same stereospecificity as in normal catalysis, D- and L-isomers competitive inhibitors, Ki: 0.55 mM and 0.59 mM, respectively Klebsiella pneumoniae

Organism

Organism UniProt Comment Textmining
Klebsiella pneumoniae
-
-
-

Oxidation Stability

Oxidation Stability Organism
D- and DL-2,3-Butanediols protect holoenzyme from O2 inactivation Klebsiella pneumoniae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,2-propanediol
-
 Klebsiella pneumoniae propanal
-
 ?
2,3-butanediol meso isomer Klebsiella pneumoniae methyl ethyl ketone
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4
-
 2,3-Butanediol
-
 Klebsiella pneumoniae

Cofactor

Cofactor Comment Organism Structure
cobamide
-
 Klebsiella pneumoniae