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In enzymology, a 4-hydroxy-2-oxovalerate aldolase () is an enzyme that catalyzes the chemical reaction :4-hydroxy-2-oxopentanoate acetaldehyde + pyruvate Hence, this enzyme has one substrate, 4-hydroxy-2-oxopentanoate, and two products, acetaldehyde and pyruvate. Baker ''et al.''. showed that BphI, a member of this family from Burkholderia xenovorans LB400 was able to utilize 4-hydroxy- 2-oxohexanoate (HOHA) with equal catalytic efficiency as 4-hydroxy-2-oxopentanoate, producing propionaldehyde + pyruvate. Furthermore, the enzyme was also able to catalyze the cleavage of 4-hydroxy-2-oxoheptanoate (HOHEP), forming butryaldehyde + pyruvate. Baker ''et al.''. we also able to show that acetaldehyde and propionaldehyde are not released into the bulk solvent, but are channeled to an associated acetaldehyde dehydrogenase known as BphJ. This is the first demonstration of substrate channeling in this family of enzymes. 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, BphI, 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. ==References== * * * * Baker, P., Pan, D., Carere, J., Rossi, A., Wang, W., and Seah, S. Y. (2009) "Characterization of an Aldolase-Dehydrogenase Complex That Exhibits Substrate Channeling in the Polychlorinated Biphenyls Degradation Pathway", Biochemistry. . PMID 19476337 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「4-hydroxy-2-oxovalerate aldolase」の詳細全文を読む スポンサード リンク
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