We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC00813Hydroxymethylglutaryl-coenzyme A lyase active site
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00813
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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Technical section
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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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