Pantothenate synthetase
From Proteopedia
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<StructureSection load='' size='450' side='right' caption='Pantothenate synthetase complex with pantoate, AMPPNP, sulfate, Mg+2 ion (green), ethanol and glycerol (PDB entry [[1n2e]])' scene='52/525165/Cv/1' pspeed='8'> | <StructureSection load='' size='450' side='right' caption='Pantothenate synthetase complex with pantoate, AMPPNP, sulfate, Mg+2 ion (green), ethanol and glycerol (PDB entry [[1n2e]])' scene='52/525165/Cv/1' pspeed='8'> | ||
== Function == | == Function == | ||
- | '''Pantothenate synthetase''' (PS) catalyzes the ATP-dependent condensation of pantoate and β-alanine to form pantothenate<ref>PMID:17932772</ref>. | + | '''Pantothenate synthetase''' or '''pantoate-beta-alanine ligase''' (PS) catalyzes the ATP-dependent condensation of pantoate and β-alanine to form pantothenate<ref>PMID:17932772</ref>. |
== Relevance == | == Relevance == |
Revision as of 09:14, 5 December 2021
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3D structures of pantothenate synthetase
Updated on 05-December-2021
References
- ↑ Jonczyk R, Ronconi S, Rychlik M, Genschel U. Pantothenate synthetase is essential but not limiting for pantothenate biosynthesis in Arabidopsis. Plant Mol Biol. 2008 Jan;66(1-2):1-14. Epub 2007 Oct 12. PMID:17932772 doi:http://dx.doi.org/10.1007/s11103-007-9248-6
- ↑ Hung AW, Silvestre HL, Wen S, George GP, Boland J, Blundell TL, Ciulli A, Abell C. Optimization of Inhibitors of Mycobacterium tuberculosis Pantothenate Synthetase Based on Group Efficiency Analysis. ChemMedChem. 2016 Jan 5;11(1):38-42. doi: 10.1002/cmdc.201500414. Epub 2015 Oct, 21. PMID:26486566 doi:http://dx.doi.org/10.1002/cmdc.201500414
- ↑ Wang S, Eisenberg D. Crystal structures of a pantothenate synthetase from M. tuberculosis and its complexes with substrates and a reaction intermediate. Protein Sci. 2003 May;12(5):1097-108. PMID:12717031