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

BRENDA support

Literature summary 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.
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.167 Acidaminococcus fermentans P11569 and P11570 and P11568 P11569 i.e. subunit alpha, P11570 i.e. subunit beta, P11568 i.e. activator protein
-
4.2.1.167 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

EC Number Cofactor Comment Organism Structure
4.2.1.167 [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