Literature summary for 4.2.1.167 extracted from

Hans, M.; Buckel, W.; Bill, E.
The iron-sulfur clusters in 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans. Biochemical and spectroscopic investigations (2000), Eur. J. Biochem., 267, 7082-7093.

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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	-

Storage Stability

Storage Stability	Organism
homodimeric activator, in the presence of 5 mM MgCl2 and 1 mM ADP or ATP, can be stabilized and stored for 4 days at 4°C without loss of activity	Acidaminococcus fermentans

Cofactor

Cofactor	Comment	Organism	Structure
riboflavin	presence of trace amounts	Acidaminococcus fermentans
riboflavin 5'-phosphate	1 mol per mol of heterodimeric dehydratase	Acidaminococcus fermentans
[4Fe-4S]-center	each active component contains an oxygen sensitive diamagnetic [4Fe-4S]2+ cluster. Reduction of the [4Fe-4S]2+ cluster of the activator protein with dithionite yields a paramagnetic [4Fe-4S]1+ cluster with the unusual electron spin ground state S=3/2. Under air the activator protein looses its activity within seconds due to irreversible degradation of its [4Fe-4S]2+ cluster to a [2Fe-2S]2+ cluster. The [4Fe-4S]2+ cluster of the heterodimeric dehydratase cannot be reduced to a [4Fe-4S]1+ cluster	Acidaminococcus fermentans

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Release 2023.1 (January 2023)