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2vl1

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{{STRUCTURE_2vl1| PDB=2vl1 | SCENE= }}
{{STRUCTURE_2vl1| PDB=2vl1 | SCENE= }}
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'''CRYSTAL STRUCTURE OF BETA-ALANINE SYNTHASE FROM SACCHAROMYCES KLUYVERI IN COMPLEX WITH THE A GLY-GLY PEPTIDE'''
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===CRYSTAL STRUCTURE OF BETA-ALANINE SYNTHASE FROM SACCHAROMYCES KLUYVERI IN COMPLEX WITH THE A GLY-GLY PEPTIDE===
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==Overview==
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In nature, the same biochemical reaction can be catalyzed by enzymes having fundamentally different folds, reaction mechanisms and origins. For example, the third step of the reductive catabolism of pyrimidines, the conversion of N-carbamyl-beta-alanine to beta-alanine, is catalyzed by two beta-alanine synthase (beta ASase, EC 3.5.1.6) subfamilies. We show that the "prototype" eukaryote beta ASases, such as those from Drosophila melanogaster and Arabidopsis thaliana, are relatively efficient in the conversion of N-carbamyl-beta A compared with a representative of fungal beta ASases, the yeast Saccharomyces kluyveri beta ASase, which has a high K(m) value (71 mM). S. kluyveri beta ASase is specifically inhibited by dipeptides and tripeptides, and the apparent K(i) value of glycyl-glycine is in the same range as the substrate K(m). We show that this inhibitor binds to the enzyme active center in a similar way as the substrate. The observed structural similarities and inhibition behavior, as well as the phylogenetic relationship, suggest that the ancestor of the fungal beta ASase was a protease that had modified its profession and become involved in the metabolism of nucleic acid precursors.
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{{ABSTRACT_PUBMED_18448119}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
A recruited protease is involved in catabolism of pyrimidines., Andersen B, Lundgren S, Dobritzsch D, Piskur J, J Mol Biol. 2008 May 30;379(2):243-50. Epub 2008 Apr 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18448119 18448119]
A recruited protease is involved in catabolism of pyrimidines., Andersen B, Lundgren S, Dobritzsch D, Piskur J, J Mol Biol. 2008 May 30;379(2):243-50. Epub 2008 Apr 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18448119 18448119]
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Yeast beta-alanine synthase shares a structural scaffold and origin with dizinc-dependent exopeptidases., Lundgren S, Gojkovic Z, Piskur J, Dobritzsch D, J Biol Chem. 2003 Dec 19;278(51):51851-62. Epub 2003 Oct 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14534321 14534321]
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Crystallization and preliminary X-ray analysis of beta-alanine synthase from the yeast Saccharomyces kluyveri., Dobritzsch D, Gojkovic Z, Andersen B, Piskur J, Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1267-9. Epub 2003, Jun 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12832781 12832781]
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Crystal structures of yeast beta-alanine synthase complexes reveal the mode of substrate binding and large scale domain closure movements., Lundgren S, Andersen B, Piskur J, Dobritzsch D, J Biol Chem. 2007 Dec 7;282(49):36037-47. Epub 2007 Oct 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17916556 17916556]
[[Category: Beta-ureidopropionase]]
[[Category: Beta-ureidopropionase]]
[[Category: Lachancea kluyveri]]
[[Category: Lachancea kluyveri]]
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[[Category: Di-zinc center]]
[[Category: Di-zinc center]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:15:47 2008''

Revision as of 10:15, 28 July 2008

Image:2vl1.png

Template:STRUCTURE 2vl1

CRYSTAL STRUCTURE OF BETA-ALANINE SYNTHASE FROM SACCHAROMYCES KLUYVERI IN COMPLEX WITH THE A GLY-GLY PEPTIDE

Template:ABSTRACT PUBMED 18448119

About this Structure

2VL1 is a Single protein structure of sequence from Lachancea kluyveri. Full crystallographic information is available from OCA.

Reference

A recruited protease is involved in catabolism of pyrimidines., Andersen B, Lundgren S, Dobritzsch D, Piskur J, J Mol Biol. 2008 May 30;379(2):243-50. Epub 2008 Apr 7. PMID:18448119

Yeast beta-alanine synthase shares a structural scaffold and origin with dizinc-dependent exopeptidases., Lundgren S, Gojkovic Z, Piskur J, Dobritzsch D, J Biol Chem. 2003 Dec 19;278(51):51851-62. Epub 2003 Oct 8. PMID:14534321

Crystallization and preliminary X-ray analysis of beta-alanine synthase from the yeast Saccharomyces kluyveri., Dobritzsch D, Gojkovic Z, Andersen B, Piskur J, Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1267-9. Epub 2003, Jun 27. PMID:12832781

Crystal structures of yeast beta-alanine synthase complexes reveal the mode of substrate binding and large scale domain closure movements., Lundgren S, Andersen B, Piskur J, Dobritzsch D, J Biol Chem. 2007 Dec 7;282(49):36037-47. Epub 2007 Oct 4. PMID:17916556

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