This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1gkr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1gkr.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1gkr.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1gkr| PDB=1gkr | SCENE= }}
{{STRUCTURE_1gkr| PDB=1gkr | SCENE= }}
-
'''L-HYDANTOINASE (DIHYDROPYRIMIDINASE) FROM ARTHROBACTER AURESCENS'''
+
===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 resolution. Each subunit of the tetrameric L-Hyd consists of an elliptically distorted (alpha/beta)(8)-barrel domain, which hosts the active site, and a beta-sheet domain. In the active site, a binuclear zinc center activates a water molecule for nucleophilic attack on the substrates' amide bond. L-Hyd shows a strong homology both in fold and in metal coordination in the active site to another dihydropyrimidinase from Thermus sp. (D-hydantoinase) and to a slightly lesser degree to ureases, dihydroorotase and phosphotriesterase. Using the homology to ureases, a model for the transition state was modeled in the active site of L-Hyd and D-hydantoinase. This model could provide an explanation for the different substrate and enantio selectivities of both dihydropyrimidinases.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12093275}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12093275 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12093275}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Hydantoinase]]
[[Category: Hydantoinase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:42:06 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:27:10 2008''

Revision as of 02:27, 1 July 2008

Image:1gkr.png

Template:STRUCTURE 1gkr

L-HYDANTOINASE (DIHYDROPYRIMIDINASE) FROM ARTHROBACTER AURESCENS

Template:ABSTRACT PUBMED 12093275

About this Structure

1GKR is a Single protein structure of sequence from Arthrobacter aurescens. 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 Jul 1 05:27:10 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1gkr"
Personal tools