Pyridoxal 5′-phosphate synthase (glutamine hydrolysing) (EC 4.3.3.6, PdxST) is an enzyme with systematic name D-ribose 5-phosphate,D-glyceraldehyde 3-phosphate pyridoxal 5′-phosphate-lyase.[1][2][3][4][5][6][7][8] This enzyme catalyses the following chemical reaction
Pyridoxal 5′-phosphate synthase (glutamine hydrolyzing) | |||||||||
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Identifiers | |||||||||
EC no. | 4.3.3.6 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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- D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine pyridoxal 5′-phosphate + L-glutamate + 3 H2O + phosphate (overall reaction)
- (1a) L-glutamine + H2O L-glutamate + NH3
- (1b) D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + NH3 pyridoxal 5′-phosphate + 4 H2O + phosphate
The enzyme can also use ribulose 5-phosphate and dihydroxyacetone phosphate.
References
edit- ^ Burns KE, Xiang Y, Kinsland CL, McLafferty FW, Begley TP (March 2005). "Reconstitution and biochemical characterization of a new pyridoxal-5′-phosphate biosynthetic pathway". Journal of the American Chemical Society. 127 (11): 3682–3. doi:10.1021/ja042792t. PMID 15771487.
- ^ Raschle T, Amrhein N, Fitzpatrick TB (September 2005). "On the two components of pyridoxal 5'-phosphate synthase from Bacillus subtilis". The Journal of Biological Chemistry. 280 (37): 32291–300. doi:10.1074/jbc.m501356200. PMID 16030023.
- ^ Strohmeier M, Raschle T, Mazurkiewicz J, Rippe K, Sinning I, Fitzpatrick TB, Tews I (December 2006). "Structure of a bacterial pyridoxal 5′-phosphate synthase complex". Proceedings of the National Academy of Sciences of the United States of America. 103 (51): 19284–9. doi:10.1073/pnas.0604950103. PMC 1748218. PMID 17159152.
- ^ Raschle T, Arigoni D, Brunisholz R, Rechsteiner H, Amrhein N, Fitzpatrick TB (March 2007). "Reaction mechanism of pyridoxal 5′-phosphate synthase. Detection of an enzyme-bound chromophoric intermediate" (PDF). The Journal of Biological Chemistry. 282 (9): 6098–105. doi:10.1074/jbc.m610614200. PMID 17189272.
- ^ Hanes JW, Keresztes I, Begley TP (2008). "Trapping of a chromophoric intermediate in the Pdx1-catalyzed biosynthesis of pyridoxal 5′-phosphate". Angewandte Chemie. 47 (11): 2102–5. doi:10.1002/anie.200704390. PMID 18260082.
- ^ Hanes JW, Burns KE, Hilmey DG, Chatterjee A, Dorrestein PC, Begley TP (March 2008). "Mechanistic studies on pyridoxal phosphate synthase: the reaction pathway leading to a chromophoric intermediate". Journal of the American Chemical Society. 130 (10): 3043–52. doi:10.1021/ja076604l. PMID 18271580.
- ^ Hanes JW, Keresztes I, Begley TP (July 2008). "13C NMR snapshots of the complex reaction coordinate of pyridoxal phosphate synthase". Nature Chemical Biology. 4 (7): 425–30. doi:10.1038/nchembio.93. PMID 18516049.
- ^ Wallner S, Neuwirth M, Flicker K, Tews I, Macheroux P (March 2009). "Dissection of contributions from invariant amino acids to complex formation and catalysis in the heteromeric pyridoxal 5-phosphate synthase complex from Bacillus subtilis". Biochemistry. 48 (9): 1928–35. doi:10.1021/bi801887r. PMID 19152323.
External links
edit- Pyridoxal+5'-phosphate+synthase+(glutamine+hydrolyzing) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)