1gkr
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 1GKR is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Arthrobacter_aurescens Arthrobacter aurescens]] with ZN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ | + | 1GKR is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Arthrobacter_aurescens Arthrobacter aurescens]] with ZN 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]]. Structure known Active Site: ASA. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GKR OCA]]. |
==Reference== | ==Reference== | ||
The structure of L-hydantoinase from Arthobacter aurescens leads to an understanding of dihydropyrimidinase substrate and enantio specificity., Abendroth J, Niefind K, May O, Siemann M, Syldatk C, Schomburg D, Biochemistry. 2002 Jul 9;41(27):8589-97. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12093275 12093275] | The structure of L-hydantoinase from Arthobacter aurescens leads to an understanding of dihydropyrimidinase substrate and enantio specificity., Abendroth J, Niefind K, May O, Siemann M, Syldatk C, Schomburg D, Biochemistry. 2002 Jul 9;41(27):8589-97. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12093275 12093275] | ||
[[Category: Arthrobacter aurescens]] | [[Category: Arthrobacter aurescens]] | ||
| + | [[Category: Dihydropyrimidinase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Abendroth, J.]] | [[Category: Abendroth, J.]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:24:06 2007'' |
Revision as of 08:19, 30 October 2007
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L-HYDANTOINASE (DIHYDROPYRIMIDINASE) FROM ARTHROBACTER AURESCENS
Overview
L-Hydantoinase from Arthrobacter aurescens (L-Hyd) is a member of the, dihydropyrimidinases which in turn belong to the cyclic amidases., Dihydropyrimidinases catalyze the reversible hydrolytic ring opening of, dihydropyrimidines as the second step in the catabolism of pyrimidines. In, biotechnology, their hydroloytic activity on five-membered cyclic diamides, (hydantoins) is used in the enantio-specific production of amino acids, from racemic hydantoins. L-Hyd differs from most of the other, dihydropyrimidinases by an L-enantio specificity and by lacking activity, on possible natural substrates such as dihydropyrimidines. In this paper, we describe the three-dimensional structure of L-Hyd which was solved by, molecular replacement using a homology model and subsequently refined to, 2.6 A ... [(full description)]
About this Structure
1GKR is a [Single protein] structure of sequence from [Arthrobacter aurescens] with ZN as [ligand]. Active as [Dihydropyrimidinase], with EC number [3.5.2.2]. Structure known Active Site: ASA. Full crystallographic information is available from [OCA].
Reference
The structure of L-hydantoinase from Arthobacter aurescens leads to an understanding of dihydropyrimidinase substrate and enantio specificity., Abendroth J, Niefind K, May O, Siemann M, Syldatk C, Schomburg D, Biochemistry. 2002 Jul 9;41(27):8589-97. PMID:12093275
Page seeded by OCA on Tue Oct 30 10:24:06 2007
