2VL1
Crystal structure of beta-alanine synthase from Saccharomyces kluyveri in complex with a gly-gly peptide
Summary for 2VL1
| Entry DOI | 10.2210/pdb2vl1/pdb |
| Related | 1R3N 1R43 2V8D 2V8G 2V8H 2V8V |
| Descriptor | BETA-ALANINE SYNTHASE, GLYCINE, ZINC ION, ... (4 entities in total) |
| Functional Keywords | hydrolase, di-zinc center, amidohydrolase, alpha and beta protein, complex with glycine-glycine |
| Biological source | SACCHAROMYCES KLUYVERI |
| Total number of polymer chains | 4 |
| Total formula weight | 209555.35 |
| Authors | Andersen, B.,Lundgren, S.,Dobritzsch, D.,Piskur, J. (deposition date: 2008-01-07, release date: 2008-05-13, Last modification date: 2023-12-13) |
| Primary citation | Andersen, B.,Lundgren, S.,Dobritzsch, D.,Piskur, J. A Recruited Protease is Involved in Catabolism of Pyrimidines. J.Mol.Biol., 379:243-, 2008 Cited by PubMed Abstract: 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. PubMed: 18448119DOI: 10.1016/J.JMB.2008.03.073 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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