creators_name: Radha Kishan, K V
creators_name: Vohra, R M
creators_name: Ganesan, K
creators_name: Agrawal, Vishal
creators_name: Sharma, Vishva Mitra
creators_name: Sharma, Rakesh
type: article
datestamp: 2012-01-08 05:42:39
lastmod: 2015-01-09 10:53:41
metadata_visibility: show
title: Molecular structure of D-hydantoinase from Bacillus sp. AR9: evidence for mercury inhibition.
ispublished: pub
subjects: QR
full_text_status: restricted
keywords: TIM-barrel; hydantoinase; manganese; carboxylated lysine; DHC-motif
note: Copyright of this article belongs to Elsevier Science.
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.
date: 2005-03-18
date_type: published
publication: Journal of molecular biology
volume: 347
number: 1
publisher: Elsevier Science
pagerange: 95-105
refereed: TRUE
issn: 0022-2836
official_url: http://www.sciencedirect.com/science/article/pii/S0022283605000471
related_url_url: http://www.sciencedirect.com/science/article/pii/S0022283605000471
related_url_type: pub
citation:   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     
document_url: http://crdd.osdd.net/open/186/1/radha2005.pdf