4-Hydroxy-2-oxovalerate aldolase

Part of the Springer Handbook of Enzymes book series (HDBKENZYMES, volume S7)


Ammonium Sulfate Pseudomonas Putida Active Site Structure Acetaldehyde Dehydrogenase UNIPROT Accession 
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  1. [1]
    Powlowski, J.; Sahlman, L.; 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)PubMedGoogle Scholar
  2. [2]
    Manjasetty, B.A.; Croteau, N.; Powlowski, J.; 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. Sect. D, 57, 582–585 (2001)CrossRefGoogle Scholar
  3. [3]
    Manjasetty, B.A.; Powlowski, J.; Vrielink, A.: Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a reactive and volatile intermediate. Proc. Natl. Acad. Sci. USA, 100, 6992–6997 (2003)CrossRefPubMedGoogle Scholar
  4. [4]
    Platt, A.; Shingler, V.; Taylor, S.C.; Williams, P.A.: The 4-hydroxy-2-oxovalerate aldolase and acetaldehyde dehydrogenase (acylating) encoded by the nahM and nahO genes of the naphthalene catabolic plasmid pWW60-22 provide further evidence of conservation of meta-cleavage pathway gene sequences. Microbiology, 141 (Pt 9), 2223–2233 (1995)CrossRefPubMedGoogle Scholar

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