The crystal structure of HpcE, a bifunctional decarboxylase/isomerase with a multifunctional fold
UNSPECIFIED. (2002) The crystal structure of HpcE, a bifunctional decarboxylase/isomerase with a multifunctional fold. BIOCHEMISTRY, 41 (9). pp. 2982-2989. ISSN 0006-2960Full text not available from this repository.
Official URL: http://dx.doi.org/10.1021/bi015717t
The structure of the bifunctional enzyme HpcE (OPET decarboxylase/HHDD isomerase) from Escherichia coli shows that the protein consists of highly similar N and C terminal halves. Sequence matches suggest that this fold is widespread among different species, including man. Many of these homologues are uncharacterized but apparently connected with the metabolism of aromatic compounds, The domain shows similar topology to the C terminal domain of fumarylacetoacetate hydrolase (FAH), a functionally related enzyme, despite lacking significant overall sequence similarity. HpcE is known to catalyze two rather different reactions, and comparisons with FAH allow some tentative conclusions to be drawn about the active sites. Key mutations within the active site apparently allow enzymes with this fold to carry out a variety chemical processes.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry|
|Journal or Publication Title:||BIOCHEMISTRY|
|Publisher:||AMER CHEMICAL SOC|
|Official Date:||5 March 2002|
|Number of Pages:||8|
|Page Range:||pp. 2982-2989|
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