Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.2.1.120 extracted from

  • Mueh, U.; Cinkaya, I.; Albracht, S.P.J.; Buckel, W.
    4-Hydroxybutyryl-CoA dehydratase from Clostridium aminobutyricum: Characterization of FAD and iron-sulfur clusters involved in an overall non-redox reaction (1996), Biochemistry, 35, 11710-11718.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Clostridium aminobutyricum
-
-
-

Oxidation Stability

Oxidation Stability Organism
upon exposure to air at 0°C, complete loss of dehydration activity within 40 min Clostridium aminobutyricum

Reaction

Reaction Comment Organism Reaction ID
4-hydroxybutanoyl-CoA = (E)-but-2-enoyl-CoA + H2O mechanism involves transient one-electron oxidation of the substrate to activate the beta-C-H-bond. the 4Fe-4S-center could serve a structural role and/or as Lewis acid facilitating the leaving of the hydroxyl group Clostridium aminobutyricum

Cofactor

Cofactor Comment Organism Structure
4Fe-4S-center Fe-S-cluster is difficult to reduce. No equilibration of electrons between the flavin and the Fe-S-center Clostridium aminobutyricum
FAD protein-bound FAD, is easily reduced to the semiquinone and only slowly to the hydroquinone. No equilibration of electrons between the flavin and the Fe-S-center Clostridium aminobutyricum