4-hydroxy-2-oxovalerate aldolase

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In enzymology, a 4-hydroxy-2-oxovalerate aldolase (EC 4.1.3.39) is an enzyme that catalyzes the chemical reaction

4-hydroxy-2-oxopentanoate $\rightleftharpoons$ acetaldehyde + pyruvate

Hence, this enzyme has one substrate, 4-hydroxy-2-oxopentanoate, and two products, acetaldehyde and pyruvate.

This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 4-hydroxy-2-oxopentanoate pyruvate-lyase (acetaldehyde-forming). Other names in common use include 4-hydroxy-2-ketovalerate aldolase, HOA, DmpG, 4-hydroxy-2-oxovalerate pyruvate-lyase, and 4-hydroxy-2-oxopentanoate pyruvate-lyase. This enzyme participates in 8 metabolic pathways: phenylalanine metabolism, benzoate degradation via hydroxylation, biphenyl degradation, toluene and xylene degradation, 1,4-dichlorobenzene degradation, fluorene degradation, carbazole degradation, and styrene degradation.

[edit] References

IUBMB entry for 4.1.3.39
BRENDA references for 4.1.3.39 (Recommended.)
PubMed references for 4.1.3.39
PubMed Central references for 4.1.3.39
Google Scholar references for 4.1.3.39
Manjasetty BA, Powlowski J, Vrielink A (2003). "Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a reactive and volatile intermediate". Proc. Natl. Acad. Sci. U. S. A. 100: 6992–7. doi:10.1073/pnas.1236794100. PMID 12764229.
Powlowski J, Sahlman L, Shingler V (1993). "Purification and properties of the physically associated meta-cleavage pathway enzymes 4-hydroxy-2-ketovalerate aldolase and aldehyde dehydrogenase (acylating) from Pseudomonas sp. strain CF600". J. Bacteriol. 175: 377–85. PMID 8419288.
Manjasetty BA, Croteau N, Powlowski J, Vrielink A (2001). "Crystallization and preliminary X-ray analysis of dmpFG-encoded 4-hydroxy-2-ketovalerate aldolase--aldehyde dehydrogenase (acylating) from Pseudomonas sp. strain CF600". Acta. Crystallogr. D. Biol. Crystallogr. 57: 582–5. doi:10.1107/S0907444901000439. PMID 11264589.