Molecular structure of D-hydantoinase from Bacillus sp. AR9: evidence for mercury inhibition.

Radha Kishan, K V and Vohra, R M and Ganesan, K and Agrawal, Vishal and Sharma, Vishva Mitra and Sharma, Rakesh (2005) Molecular structure of D-hydantoinase from Bacillus sp. AR9: evidence for mercury inhibition. Journal of molecular biology, 347 (1). pp. 95-105. ISSN 0022-2836

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Abstract

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.

Item Type:	Article
Additional Information:	Copyright of this article belongs to Elsevier Science.
Uncontrolled Keywords:	TIM-barrel; hydantoinase; manganese; carboxylated lysine; DHC-motif
Subjects:	Q Science > QR Microbiology
Depositing User:	Dr. K.P.S.Sengar
Date Deposited:	08 Jan 2012 05:42
Last Modified:	09 Jan 2015 10:53
URI:	http://crdd.osdd.net/open/id/eprint/186

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