These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Carboxymethylhydroxymuconic semialdehyde dehydrogenase in the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli.
    Author: Alonso JM, Garrido-Pertierra A.
    Journal: Biochim Biophys Acta; 1982 Oct 28; 719(1):165-7. PubMed ID: 6756482.
    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 micro M for 5-carboxymethyl-2-hydroxymuconic semialdehyde and 52.2 micro M for NAD.
    [Abstract] [Full Text] [Related] [New Search]