Developing structure-based models to predict substrate specificity of D-group (Type II) molybdenum enzymes: Application to a molybdo-enzyme of unknown function from Archaeoglobus fulgidus.

Dridge, E.J., Richardson, D.J., Lewis, R.J. and Butler, C.S. (2006) Developing structure-based models to predict substrate specificity of D-group (Type II) molybdenum enzymes: Application to a molybdo-enzyme of unknown function from Archaeoglobus fulgidus. Biochemical Society Transactions, 34. pp. 118-121. ISSN 1470-8752

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Abstract

The AF0174–AF0176 gene cluster in Archaeoglobus fulgidus encodes a putative oxyanion reductase of the D-type (Type II) family of molybdo-enzymes. Sequence analysis reveals that the catalytic subunit AF0176 shares low identity (31–32%) and similarity (41–42%) to both NarG and SerA, the catalytic components of the respiratory nitrate and selenate reductases respectively. Consequently, predicting the oxyanion substrate selectivity of AF0176 has proved difficult based solely on sequence alignments. In the present study, we have modelled both AF0176 and SerA on the recently determined X-ray structure of the NAR (nitrate reductase) from Escherichia coli and have identified a number of key amino acid residues, conserved in all known NAR sequences, including AF0176, that we speculate may enhance selectivity towards trigonal planar (NO3−) rather than tetrahedral (SeO42− and ClO4−) substrates.

Item Type:	Article
Faculty \ School:	Faculty of Science > School of Biological Sciences
UEA Research Groups:	Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Groups > Organisms and the Environment Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry
Depositing User:	EPrints Services
Date Deposited:	01 Oct 2010 13:37
Last Modified:	28 Mar 2025 03:59
URI:	https://ueaeprints.uea.ac.uk/id/eprint/1159
DOI:	10.1042/BST0340118

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