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Kinetic property and phylogenic relationship of 2-hydroxymuconic semialdehyde dehydrogenase encoded intomC gene ofBurkholderia cepacia G4

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Abstract

2-Hydroxymuconic semialdehyde (2-HMS) dehydrogenase catalyzes the conversion of 2-HMS to 4-oxalocrotonate, which is a step in themeta cleavage pathway of aromatic hydrocarbons in bacteria. AtomC gene that encodes 2-HMS dehydrogenase ofBurkholderia cepacia G4, a soil bacterium that can grow on toluene, cresol, phenol, or benzene, was overexpressed intoE. coli HB101, and its gene product was characterized in this study. 2-HMS dehydrogenase fromB. cepacia G4 has a high catalytic efficiency in terms of Vmax/Km towards 2-hydroxy-5-methylmuconic semialdehyde followed by 2-HMS but has a very low efficiency for 5-chloro-2-hydroxymuconic semialdehyde. However, the enzyme did not utilize 2-hydroxy-6-oxo-hepta-2, 4-dienoic acid and 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid as substrates. The molecular weight of 2-HMS dehydrogenase fromB. cepacia G4 was predicted to be 52 kDa containing 485 amino acid residues from the nucleotide sequence of thetomC gene, and it exhibited the highest identity of 78% with the amino acid sequence of 2-HMS dehydrogenase that is encoded in theaphC gene ofComamonas testosteroni TA441. 2-HMS dehydrogenase fromB. cepacia G4 showed a significant phylogenetic relationship not only with other 2-HMS dehydrogenases, but also with different dehydrogenases from evolutionary distant organisms.

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Correspondence to Youngsoo Kim.

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Reddy, A.M., Min, K.R., Lee, K. et al. Kinetic property and phylogenic relationship of 2-hydroxymuconic semialdehyde dehydrogenase encoded intomC gene ofBurkholderia cepacia G4. Arch Pharm Res 27, 570–575 (2004). https://doi.org/10.1007/BF02980133

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