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2-hydroxyacyl-CoA dehydratase
Degradation of glutamate via the hydroxyglutarate pathway involves the syn-elimination of water from 2-hydroxyglutaryl-CoA. This anaerobic process is catalysed by 2-hydroxyglutaryl-CoA dehydratase, an enzyme with two components (A and D) that reversibly associate during reaction cycles. This component contains one non-reducible [4Fe-4S]2+ cluster and a reduced riboflavin 5'-monophosphate [1]. [1]. 11980491. Adenosine triphosphate-induced electron transfer in 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans. Hans M, Bill E, Cirpus I, Pierik AJ, Hetzel M, Alber D, Buckel W;. Biochemistry 2002;41:5873-5882. (from Pfam)
double-cubane-cluster-containing anaerobic reductase
This subfamily of double-cubane proteins occurs strictly in anaerobes (facultative or obligate), such as Escherichia coli and Clostridium difficile. The enzyme always co-occurs with an accessory protein, an ATP-dependent activase. The cofactor contains a pair of 4Fe-4S cubane clusters, bridged by a sulfur atom, for an overall 8Fe-9S cofactor structure. However, we observe that that this family essentially always co-occurs in bacteria with SelD, the selenium donor protein required for biosynthesis of selenoproteins, selenouridine-modified tRNAs, selenium-dependent molybdenum hydroxylases, and selenoneine.
2-hydroxyacyl-CoA dehydratase family protein
2-hydroxyacyl-CoA dehydratase alpha/beta subunit is a component of the heterodimeric 2-hydroxyacyl-CoA dehydratase that catalyzes the reversible elimination of water from a 2-hydroxyacyl-CoA substrate to form the 2-acyl-CoA product
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