1yny
From Proteopedia
(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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| - | [[Image:1yny.gif|left|200px]]<br /><applet load="1yny" size=" | + | [[Image:1yny.gif|left|200px]]<br /><applet load="1yny" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yny, resolution 2.30Å" /> | caption="1yny, resolution 2.30Å" /> | ||
'''Molecular Structure of D-Hydantoinase from a Bacillus sp. AR9: Evidence for mercury inhibition'''<br /> | '''Molecular Structure of D-Hydantoinase from a Bacillus sp. AR9: Evidence for mercury inhibition'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Stereospecific conversion of hydantoins into their carbamoyl acid | + | 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== | ==About this Structure== | ||
| - | 1YNY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.] with MN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Dihydropyrimidinase Dihydropyrimidinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.2 3.5.2.2] Full crystallographic information is available from [http:// | + | 1YNY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.] with <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Dihydropyrimidinase Dihydropyrimidinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.2 3.5.2.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YNY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Agrawal, V.]] | [[Category: Agrawal, V.]] | ||
[[Category: Ganeshan, K.]] | [[Category: Ganeshan, K.]] | ||
| - | [[Category: Kishan, K | + | [[Category: Kishan, K V.Radha.]] |
[[Category: Sharma, R.]] | [[Category: Sharma, R.]] | ||
| - | [[Category: Sharma, V | + | [[Category: Sharma, V M.]] |
| - | [[Category: Vohra, R | + | [[Category: Vohra, R M.]] |
[[Category: MN]] | [[Category: MN]] | ||
[[Category: tim-barrel; hydantoinase; binuclear metal-binding; hydrolase]] | [[Category: tim-barrel; hydantoinase; binuclear metal-binding; hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:07:19 2008'' |
Revision as of 14:07, 21 February 2008
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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 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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