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PROSITE documentation PDOC00813 [for PROSITE entry PS01062]

Hydroxymethylglutaryl-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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Technical section

PROSITE method (with tools and information) covered by this documentation:

HMG_COA_LYASE, PS01062; Hydroxymethylglutaryl-coenzyme A lyase active site  (PATTERN)


References

1AuthorsMitchell 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.
Title3-Hydroxy-3-methylglutaryl coenzyme A lyase (HL). Cloning of human and chicken liver HL cDNAs and characterization of a mutation causing human HL deficiency.
SourceJ. Biol. Chem. 268:4376-4381(1993).
PubMed ID8440722

2AuthorsHruz P.W. Narasimhan C. Miziorko H.M.
Title3-Hydroxy-3-methylglutaryl coenzyme A lyase: affinity labeling of the Pseudomonas mevalonii enzyme and assignment of cysteine-237 to the active site.
SourceBiochemistry 31:6842-6847(1992).
PubMed ID1637819



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