Citramalyl-CoA lyase, mitochondrial (CLYBL)

Citramalyl-CoA lyase, mitochondrial (CLYBL) is a mitochondrial matrix enzyme that catalyzes the cleavage of citramalyl-CoA to acetyl-CoA and pyruvate, a key step in the C5-dicarboxylate catabolic pathway involved in the metabolism and detoxification of itaconate and related metabolites[1][4][5]. CLYBL activity is required for maintaining mitochondrial vitamin B12 metabolism; loss of function leads to accumulation of upstream intermediates and a mild but consistent reduction in circulating B12. The enzyme is structurally a homotrimer and binds magnesium, demonstrating additional in vitro catalytic activities such as malate synthase and malyl-CoA thioesterase, though its primary physiological function is citramalyl-CoA cleavage[1][3]. CLYBL is highly conserved and ubiquitously expressed, and its disruption does not produce overt phenotypes apart from the B12 defect[1][3]. Notes: - There is no evidence of approved or investigational drugs targeting CLYBL, and no clear role for this protein in major disease categories (such as cancer or neurodegenerative disorders) established in the literature[3]. - The enzyme is categorized as a lyase, more specifically an oxo-acid-lyase, and is distinct from citrate lyase complexes due to lack of other complex subunits in mammals[1][5]. - The gene symbol is "CLYBL," and the main standardized protein/gene name is "citramalyl-CoA lyase, mitochondrial (CLYBL)"[3][4][5].

Other names

citrate lyase beta-like proteinCLB(3S)-malyl-CoA thioesterasebeta-methylmalate synthasemalate synthasecitrate lyase subunit beta-like protein