Carboxymethylhydroxymuconic semialdehyde dehydrogenase in the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli |
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Authors: | Josefa M Alonso Amando Garrido-Pertierra |
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Institution: | Departamento de Bioquímica, Facultades de Biología y Veterinaria, Universidad de León, León Spain |
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Abstract: | 5-Carboxymethyl-2-hydroxymuconic semialdehyde dehydrogenase in the 4-hydroxyphenylacetate meta-cleavage pathway has been purified to 96% homogeneity. The native enzyme, which appears to be a tetramer, has an apparent molecular weight of 210000. The purified enzyme shows a narrow pH optimum at pH 7.8 and does not require ions for its catalytic activity. Under standard assay conditions the enzyme acts preferentially with NAD but reduces NADP at 11% of the rate observed for NAD, primarily because of a difference in Km. Apparent Km values are 6.4 μM for 5-carboxymethyl-2-hydroxymuconic semialdehyde and 52.2 μM for NAD. |
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Keywords: | Carboxymethylhydroxymuconic semialdehyde dehydrogenase Hydroxyphenylacetate catabolism (E coli) |
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