PROSITE documentation PDOC00813Hydroxymethylglutaryl-coenzyme A lyase active site
Description
3-hydroxy-3-methylglutaryl-coenzyme A lyase (HMG-CoA lyase or HL) (EC 4.1.3.4) catalyzes the transformation of HMG-CoA into acetyl-CoA and acetoacetate. In vertebrates it is a mitochondrial enyme which is involved in ketogenesis and in leucine catabolism [1]. In some bacteria, such as Pseudomonas mevalonii, it is involved in mevalonate catabolism (gene mvaB). A cysteine has been shown [2], in mvaB, to be required for the activity of the enzyme. The region around this residue is perfectly conserved and is used as a signature pattern.
Last update:November 1995 / First entry.
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References
| 1 | Authors | Mitchell G.A. Robert M.-F. Hruz P.W. Wang S. Fontaine G. Behnke C.E. Mende-Mueller L.M. Schappert K. Lee C. Gibson K.M. |
| Title | 3-Hydroxy-3-methylglutaryl coenzyme A lyase (HL). Cloning of human and chicken liver HL cDNAs and characterization of a mutation causing human HL deficiency. | |
| Source | J. Biol. Chem. 268:4376-4381(1993). | |
| PubMed ID | 8440722 |
| 2 | Authors | Hruz P.W. Narasimhan C. Miziorko H.M. |
| Title | 3-Hydroxy-3-methylglutaryl coenzyme A lyase: affinity labeling of the Pseudomonas mevalonii enzyme and assignment of cysteine-237 to the active site. | |
| Source | Biochemistry 31:6842-6847(1992). | |
| PubMed ID | 1637819 |
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