1k1d: Difference between revisions

Revision as of 21:16, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1k1d.png

Template:STRUCTURE 1k1d

Crystal structure of D-hydantoinaseCrystal structure of D-hydantoinase

Template:ABSTRACT PUBMED 12135362

About this StructureAbout this Structure

1K1D is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of D-hydantoinase from Bacillus stearothermophilus: insight into the stereochemistry of enantioselectivity., Cheon YH, Kim HS, Han KH, Abendroth J, Niefind K, Schomburg D, Wang J, Kim Y, Biochemistry. 2002 Jul 30;41(30):9410-7. PMID:12135362

Page seeded by OCA on Tue Jul 1 21:16:30 2008

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OCA

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-'''Crystal structure of D-hydantoinase'''
+===Crystal structure of D-hydantoinase===
-==Overview==
+<!--
-Industrial production of antibiotics, such as semisynthetic penicillins and cephalosporins, requires optically pure D-p-hydroxylphenylglycine and its derivatives as important side-chain precursors. To produce optically pure D-amino acids, microbial D-hydantoinase (E.C. 3.5.2.2) is used for stereospecific hydrolysis of chemically synthesized cyclic hydantoins. We report the apo-crystal structure of D-hydantoinase from B. stearothermophilus SD1 at 3.0 A resolution. The structure has a classic TIM barrel fold. Despite an undetectable similarity in sequence, D-hydantoinase shares a striking structural similarity with the recently solved structure of dihydroorotase. A structural comparison of hydantoinase with dihydroorotase revealed that the catalytic chemistry is conserved, while the substrate recognition is not. This structure provides insight into the stereochemistry of enantioselectivity in hydrolysis and illustrates how the enzyme recognizes stereospecific exocyclic substituents and hydrolyzes hydantoins. It should also provide a rationale for further directed evolution of this enzyme for hydrolysis of new hydantoins with novel exocyclic substituents.
+The line below this paragraph, {{ABSTRACT_PUBMED_12135362}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12135362 is the PubMed ID number.
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 [[Category: Wang, J.]]
 [[Category: D-hydantoinase]]
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