Pathways & interactions
Citrate lyase beta subunit-like (IPR011206)
Short name: Citrate_lyase_beta/mcl1/mcl2
- Citrate lyase beta subunit-like (IPR011206)
- Citrate lyase, beta subunit, bacteria (IPR006475)
This entry represents a group of proteins belonging to the HpcH/HpaI aldolase family. Proteins in this entry include citrate lyase subunit beta, malyl-CoA lyase and (3S)-malyl-CoA thioesterase. This entry also includes beta-methylmalyl-CoA lyase (rrnAC0690) from Haloarcula marismortui.
Citrate lyase catalyses the magnesium-dependent cleavage of citrate to acetate and oxaloacetate. In bacteria, this reaction is involved in citrate fermentation. The bacterial enzyme is composed of three subunits: alpha, beta and gamma. Catalytic activity resides on the alpha- and beta-subunits, whereas the gamma-subunit serves as an acyl carrier protein (ACP) [PMID: 10924139]. Mammalian citrate lyase beta proteins display similarity to the bacterial enzymes [PMID: 11741334].
Malyl-CoA lyase catalyses the reversible condensation of glyoxylate and acetyl-CoA to L-malyl-CoA and the reversible condensation of glyoxylate and propionyl-CoA to beta-methylmalyl-CoA [PMID: 15687206].
(3S)-malyl-CoA thioesterase catalyses the hydrolysis of (3S)-malyl-CoA to (3S)-malate and free CoA [PMID: 20047909].
Haloarcula marismortui beta-methylmalyl-CoA lyase may be involved in the methylaspartate cycle [PMID: 21252347]. It catalyses the reversible cleavage of beta-methylmalyl-CoA to propionyl-CoA and glyoxylate, as well as the reversible cleavage of (S)-malyl-CoA to acetyl-CoA and glyoxylate with some (S)-malyl-CoA thioesterase activity [PMID: 21252347].
- PIRSF015582 (Cit_lyase_B)