Literature summary for 4.2.1.167 extracted from

Hans, M.; Buckel, W.; Bill, E.
Spectroscopic evidence for an all-ferrous [4Fe-4S]0 cluster in the superreduced activator of 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans (2008), J. Biol. Inorg. Chem., 13, 563-574.

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Organism

Organism	UniProt	Comment	Textmining
Acidaminococcus fermentans	P11569 and P11570 and P11568	P11569 i.e. subunit alpha, P11570 i.e. subunit beta, P11568 i.e. activator protein	-
Acidaminococcus fermentans DSM 20731	P11569 and P11570 and P11568	P11569 i.e. subunit alpha, P11570 i.e. subunit beta, P11568 i.e. activator protein	-

Cofactor

Cofactor	Comment	Organism	Structure
[4Fe-4S]-center	the reduced [4Fe-4S]+ cluster containing activator protein transfers one electron to the dehydratase driven by ATP hydrolysis, which activates the enzyme. With a tenfold excess of titanium(III) citrate at pH 8.0 the activator can be further reduced, yielding about 50% of a superreduced [4Fe-4S]0 cluster in the all-ferrous state. The superreduced cluster has apparent spectroscopic similarities with the corresponding [4Fe-4S]0 cluster described for the nitrogenase Fe-protein. Only one-electron transfer steps are involved in dehydratase catalysis	Acidaminococcus fermentans

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Release 2023.1 (January 2023)