KEGG   ENZYME: 4.3.3.6Help
Entry
EC 4.3.3.6                  Enzyme                                 

Name
pyridoxal 5'-phosphate synthase (glutamine hydrolysing);
PdxST
Class
Lyases;
Carbon-nitrogen lyases;
Amine-lyases
BRITE hierarchy
Sysname
D-ribose 5-phosphate,D-glyceraldehyde 3-phosphate pyridoxal 5'-phosphate-lyase
Reaction(IUBMB)
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate (overall reaction) [RN:R10089];
(1a) L-glutamine + H2O = L-glutamate + NH3 [RN:R00256];
(1b) D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + NH3 = pyridoxal 5'-phosphate + 4 H2O + phosphate [RN:R10088]
Reaction(KEGG)
Substrate
D-ribose 5-phosphate [CPD:C00117];
D-glyceraldehyde 3-phosphate [CPD:C00118];
L-glutamine [CPD:C00064];
H2O [CPD:C00001];
NH3 [CPD:C00014]
Product
pyridoxal 5'-phosphate [CPD:C00018];
L-glutamate [CPD:C00025];
H2O [CPD:C00001];
phosphate [CPD:C00009];
NH3 [CPD:C00014]
Comment
The ammonia is provided by the glutaminase subunit and channeled to the active site of the lyase subunit by a 100 A tunnel. The enzyme can also use ribulose 5-phosphate and dihydroxyacetone phosphate. The enzyme complex is found in aerobic bacteria, archaea, fungi and plants.
Reference
1  [PMID:15771487]
  Authors
Burns KE, Xiang Y, Kinsland CL, McLafferty FW, Begley TP
  Title
Reconstitution and biochemical characterization of a new pyridoxal-5'-phosphate biosynthetic pathway.
  Journal
J. Am. Chem. Soc. 127 (2005) 3682-3.
Reference
2  [PMID:16030023]
  Authors
Raschle T, Amrhein N, Fitzpatrick TB
  Title
On the two components of pyridoxal 5'-phosphate synthase from Bacillus subtilis.
  Journal
J. Biol. Chem. 280 (2005) 32291-300.
Reference
3  [PMID:17159152]
  Authors
Strohmeier M, Raschle T, Mazurkiewicz J, Rippe K, Sinning I, Fitzpatrick TB, Tews I
  Title
Structure of a bacterial pyridoxal 5'-phosphate synthase complex.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 19284-9.
Reference
4  [PMID:17189272]
  Authors
Raschle T, Arigoni D, Brunisholz R, Rechsteiner H, Amrhein N, Fitzpatrick TB
  Title
Reaction mechanism of pyridoxal 5'-phosphate synthase. Detection of an enzyme-bound chromophoric intermediate.
  Journal
J. Biol. Chem. 282 (2007) 6098-105.
Reference
5  [PMID:18260082]
  Authors
Hanes JW, Keresztes I, Begley TP
  Title
Trapping of a chromophoric intermediate in the Pdx1-catalyzed biosynthesis of pyridoxal 5'-phosphate.
  Journal
Angew. Chem. Int. Ed. Engl. 47 (2008) 2102-5.
Reference
6  [PMID:18271580]
  Authors
Hanes JW, Burns KE, Hilmey DG, Chatterjee A, Dorrestein PC, Begley TP
  Title
Mechanistic studies on pyridoxal phosphate synthase: the reaction pathway leading to a chromophoric intermediate.
  Journal
J. Am. Chem. Soc. 130 (2008) 3043-52.
Reference
7  [PMID:18516049]
  Authors
Hanes JW, Keresztes I, Begley TP
  Title
13C NMR snapshots of the complex reaction coordinate of pyridoxal phosphate synthase.
  Journal
Nat. Chem. Biol. 4 (2008) 425-30.
Reference
8  [PMID:19152323]
  Authors
Wallner S, Neuwirth M, Flicker K, Tews I, Macheroux P
  Title
Dissection of contributions from invariant amino acids to complex formation and catalysis in the heteromeric pyridoxal 5-phosphate synthase complex from Bacillus subtilis.
  Journal
Biochemistry. 48 (2009) 1928-35.
Other DBs
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IUBMB Enzyme Nomenclature: 
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BRENDA, the Enzyme Database: 

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