Literature summary for 4.2.1.175 extracted from

Kim, J.; Hetzel, M.; Boiangiu, C.; Buckel, W.
Dehydration of (R)-2-hydroxyacyl-CoA to enoyl-CoA in the fermentation of alpha-amino acids by anaerobic bacteria (2004), FEMS Microbiol. Rev., 28, 455-468 .

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Organism

Organism	UniProt	Comment	Textmining
Clostridium sporogenes	Q93AL9 and Q93AL8	Q93AL9 i.e. alpha-subunit FldB, Q93AL8 i.e. beta-subunit FldC	-

General Information

General Information	Comment	Organism
physiological function	comparison of 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans, Clostridium symbiosum and Fusobacterium nucleatum, 2-phenyllactate dehydratase from Clostridium sporogenes, 2-hydroxyisocaproyl-CoA dehydratase from Clostridium difficile, and lactyl-CoA dehydratase from Clostridium propionicum. The 2-hydroxyacyl-CoA dehydratases are two-component systems composed of an extremely oxygen-sensitive component A, an activator, and component D, the actual dehydratase. Component A, a homodimer with one [4Fe-4S]cluster, transfers an electron to component D, a heterodimer with 1-2 [4Fe-4S] clusters and FMN, concomitant with hydrolysis of two ATP. From component D the electron is further transferred to the substrate, where it facilitates elimination of the hydroxyl group. In the resulting enoxyradical the beta-hydrogen is activated. After elimination the electron is handed-over to the next incoming substrate without further hydrolysis of ATP. The helix-cluster-helix architecture of component A forms an angle of 105°, which probably opens to 180° upon binding of ATP resembling an archer shooting arrows	Clostridium sporogenes

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Release 2023.1 (January 2023)