EC - 4-hydroxy-2-oxovalerate aldolase

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IntEnz Enzyme Nomenclature


Accepted name:
4-hydroxy-2-oxovalerate aldolase
Other names:
4-hydroxy-2-ketovalerate aldolase
4-hydroxy-2-oxovalerate pyruvate-lyase
4-hydroxy-2-oxopentanoate pyruvate-lyase
4-hydroxy-2-oxopentanoate pyruvate-lyase (acetaldehyde-forming)
Systematic name:
(S)-4-hydroxy-2-oxopentanoate pyruvate-lyase (acetaldehyde-forming)




Requires Mn2+ for maximal activity [1]. The enzyme from the bacterium Pseudomonas putida is also stimulated by NADH [1]. In some bacterial species, the enzyme forms a bifunctional complex with EC, acetaldehyde dehydrogenase (acetylating). The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC, 4-hydroxy-2-oxohexanoate aldolase [4,5].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , DIAGRAM , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC50991
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008701
CAS Registry Number: 37325-52-3
UniProtKB/Swiss-Prot: (174) [show] [UniProt]


  1. Manjasetty, B.A., Powlowski, J. and Vrielink, A.
    Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a reactive and volatile intermediate.
    Proc. Natl. Acad. Sci. USA 100: 6992-6997 (2003). [PMID: 12764229]
  2. Powlowski, J., Sahlman, L. and Shingler, V.
    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: 377-385 (1993). [PMID: 8419288]
  3. Manjasetty, B.A., Croteau, N., Powlowski, J. and Vrielink, A.
    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: 582-585 (2001). [PMID: 11264589]
  4. Baker, P., Carere, J., Seah, S. Y.
    Probing the molecular basis of substrate specificity, stereospecificity, and catalysis in the class II pyruvate aldolase, BphI.
    Biochemistry 50: 3559-3569 (2011). [PMID: 21425833]
  5. Baker, P., Hillis, C., Carere, J., Seah, S. Y.
    Protein-protein interactions and substrate channeling in orthologous and chimeric aldolase-dehydrogenase complexes.
    Biochemistry 51: 1942-1952 (2012). [PMID: 22316175]
  6. Baker, P., Seah, S. Y.
    Rational design of stereoselectivity in the class II pyruvate aldolase BphI.
    J. Am. Chem. Soc. 134: 507-513 (2012). [PMID: 22081904]

[EC created 2006, modified 2011]