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

DIR@IMTECH: CSIR-Institute of Microbial Technology

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Title Molecular structure of D-hydantoinase from Bacillus sp. AR9: evidence for mercury inhibition.
 
Creator Radha Kishan, K V
Vohra, R M
Ganesan, K
Agrawal, Vishal
Sharma, Vishva Mitra
Sharma, Rakesh
 
Subject QR Microbiology
 
Description 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.
 
Publisher Elsevier Science
 
Date 2005-03-18
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://crdd.osdd.net/open/186/1/radha2005.pdf
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
 
Relation http://www.sciencedirect.com/science/article/pii/S0022283605000471
http://crdd.osdd.net/open/186/