UNSPECIFIED. (2002) The crystal structure of HpcE, a bifunctional decarboxylase/isomerase with a multifunctional fold. BIOCHEMISTRY, 41 (9). pp. 2982-2989. ISSN 0006-2960

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Abstract

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
ISSN:	0006-2960
Date:	5 March 2002
Volume:	41
Number:	9
Number of Pages:	8
Page Range:	pp. 2982-2989
Identification Number:	10.1021/bi015717t
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/11201

Data sourced from Thomson Reuters' Web of Knowledge

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