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Literature summary extracted from

  • Hans, M.; Bill, E.; Cirpus, I.; Pierik, A.J.; Hetzel, M.; Alber, D.; Buckel, W.
    Adenosine triphosphate-induced electron transfer in 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans (2002), Biochemistry, 41, 5873-5882.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.167 Acidaminococcus fermentans P11569 and P11570 P11569 i.e. subunit alpha, P11570 i.e. subunit beta
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4.2.1.167 Acidaminococcus fermentans DSM 20731 P11569 and P11570 P11569 i.e. subunit alpha, P11570 i.e. subunit beta
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.167 additional information in the presence of ATP one electron is transferred from flavodoxin hydroquinone via the [4Fe-4S]1+/2+ cluster of the activator protein to Mo(VI) of heterodimeric dehydratase, which is thereby reduced to Mo(V) Acidaminococcus fermentans ?
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 ?
4.2.1.167 additional information in the presence of ATP one electron is transferred from flavodoxin hydroquinone via the [4Fe-4S]1+/2+ cluster of the activator protein to Mo(VI) of heterodimeric dehydratase, which is thereby reduced to Mo(V) Acidaminococcus fermentans DSM 20731 ?
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
4.2.1.167 [4Fe-4S]-center the [4Fe-4S](1+/2+) cluster of the activator protein is exposed to the solvent. Upon exchange of the bound ADP by ATP, the chelation rate by iron chelators is 8fold enhanced, indicating a large conformational change. Oxidized activator exhibits ATPase activity of 6 s(-1), which is completely abolished upon reduction by one electron Acidaminococcus fermentans