1yny
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(New page: 200px<br /><applet load="1yny" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yny, resolution 2.30Å" /> '''Molecular Structure ...)
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Revision as of 02:18, 25 November 2007
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Molecular Structure of D-Hydantoinase from a Bacillus sp. AR9: Evidence for mercury inhibition
Overview
Stereospecific conversion of hydantoins into their carbamoyl acid, derivatives could be achieved by using the enzyme hydantoinase. Specific, hydantoinases convert either the D-form or the L-form of the hydantoin and, the amino acids responsible for stereospecificity have not been, identified. Structural studies on hydantoinases from a few bacterial, species were published recently. The structure of a thermostable, D-hydantoinase from Bacillus sp. AR9 (bar9HYD) was solved to 2.3 angstroms, resolution. The usual modification of carboxylation of the active-site, residue Lys150 did not happen in bar9HYD. Two manganese ions were modelled, in the active site. Through biochemical studies, it was shown that mercury, inhibits the activity of the enzyme. The mercury derivative provided some, information about the binding site of the mercuric inhibitors and a, possible reason for inhibition is presented.
About this Structure
1YNY is a Protein complex structure of sequences from Bacillus sp. with MN as ligand. Active as Dihydropyrimidinase, with EC number 3.5.2.2 Full crystallographic information is available from OCA.
Reference
Molecular structure of D-hydantoinase from Bacillus sp. AR9: evidence for mercury inhibition., Radha Kishan KV, Vohra RM, Ganesan K, Agrawal V, Sharma VM, Sharma R, J Mol Biol. 2005 Mar 18;347(1):95-105. Epub 2005 Jan 27. PMID:15733920
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