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Literature summary for 4.2.1.167 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
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Organism

Organism UniProt Comment Textmining
Acidaminococcus fermentans P11569 and P11570 P11569 i.e. subunit alpha, P11570 i.e. subunit beta
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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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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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 ?
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

Cofactor Comment Organism Structure
[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