EzCatDB: S00270

DB codeS00270
CATH domainDomain 13.30.479.10Catalytic domain
E.C.4.2.3.12
CSA1b66
MACiEM0084


Enzyme Name
Swiss-protKEGG

P27213
Protein name6-pyruvoyl tetrahydrobiopterin synthase6-pyruvoyltetrahydropterin synthase
2-amino-4-oxo-6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-dihydroxypteridine triphosphate lyase
6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-dihydropterintriphosphate-lyase (6-pyruvoyl-5,6,7,8-tetrahydropterin-forming)
SynonymsPTP synthase
PTPS
EC 4.2.3.12

KEGG pathways
MAP codePathways
MAP00790Folate biosynthesis

Swiss-prot:Accession NumberP27213
Entry namePTPS_RAT
Activity7,8-dihydroneopterin 3''-triphosphate = 6- pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate.
SubunitHomohexamer formed of two homotrimers in a head to head fashion.
Subcellular location
CofactorBinds 1 zinc ion per subunit.


CofactorsSubstratesProducts
KEGG-idC00038C00305C04895C03684C00536
CompoundZincMagnesium6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-dihydropterin6-pyruvoyl-5,6,7,8-tetrahydropterinTriphosphate
Typeheavy metaldivalent metal (Ca2+, Mg2+)amide group,amine group,aromatic ring (with nitrogen atoms),carbohydrate,phosphate group/phosphate ionamide group,amine group,aromatic ring (with nitrogen atoms),carbohydratephosphate group/phosphate ion
1b66ABound:_ZNUnboundUnboundAnalogue:BIOUnbound
1b66BBound:_ZNUnboundUnboundAnalogue:BIOUnbound
1b6zABound:_ZNUnboundUnboundUnboundUnbound
1b6zBBound:_ZNUnboundUnboundUnboundUnbound
1gtqABound:_ZNUnboundUnboundUnboundUnbound
1gtqBBound:_ZNUnboundUnboundUnboundUnbound

Active-site residues
resource
PDB;1b66,1b6z,1gtq & Swiss-prot;P27213
pdbCatalytic residuesCofactor-binding residues
1b66ACYS 42;HIS 89;GLU 133
HIS 23;HIS 48;HIS 50(Zinc binding)
1b66BCYS 42;HIS 89;GLU 133
HIS 23;HIS 48;HIS 50(Zinc binding)
1b6zACYS 42;HIS 89;GLU 133
HIS 23;HIS 48;HIS 50(Zinc binding)
1b6zBCYS 42;HIS 89;GLU 133
HIS 23;HIS 48;HIS 50(Zinc binding)
1gtqACYS 42;HIS 89;GLU 133
HIS 23;HIS 48;HIS 50(Zinc binding)
1gtqBCYS 42;HIS 89;GLU 133
HIS 23;HIS 48;HIS 50(Zinc binding)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]Scheme 14
[2]p.1259-1261
[3]Fig.8, Fig.9, p.361-362, p.364-3654
[5]Fig.7, p.855-8574

references
[1]
PubMed ID2406138
JournalEur J Biochem
Year1990
Volume187
Pages651-6
AuthorsGhisla S, Kuster T, Steinerstauch P, Leimbacher W, Richter WJ, Raschdorf F, Dahinden R, Curtius HC
Title1H-NMR and mass spectrometric studies of tetrahydropterins. Evidence for the structure of 6-pyruvoyl tetrahydropterin, an intermediate in the biosynthesis of tetrahydrobiopterin.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Medline ID94185630
PubMed ID8137809
JournalEMBO J
Year1994
Volume13
Pages1255-62
AuthorsNar H, Huber R, Heizmann CW, Thony B, Burgisser D
TitleThree-dimensional structure of 6-pyruvoyl tetrahydropterin synthase, an enzyme involved in tetrahydrobiopterin biosynthesis.
Related PDB1gtq
Related Swiss-protP27213
[3]
PubMed ID7563095
JournalJ Mol Biol
Year1995
Volume253
Pages358-69
AuthorsBurgisser DM, Thony B, Redweik U, Hess D, Heizmann CW, Huber R, Nar H
Title6-Pyruvoyl tetrahydropterin synthase, an enzyme with a novel type of active site involving both zinc binding and an intersubunit catalytic triad motif; site-directed mutagenesis of the proposed active center, characterization of the metal binding site and modelling of substrate binding.
[4]
PubMed ID9774432
JournalJ Biol Chem
Year1998
Volume273
Pages28132-41
AuthorsBracher A, Eisenreich W, Schramek N, Ritz H, Gotze E, Herrmann A, Gutlich M, Bacher A
TitleBiosynthesis of pteridines. NMR studies on the reaction mechanisms of GTP cyclohydrolase I, pyruvoyltetrahydropterin synthase, and sepiapterin reductase.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medline ID99150429
PubMed ID10024455
JournalJ Mol Biol
Year1999
Volume286
Pages851-60
AuthorsPloom T, Thony B, Yim J, Lee S, Nar H, Leimbacher W, Richardson J, Huber R, Auerbach G
TitleCrystallographic and kinetic investigations on the mechanism of 6-pyruvoyl tetrahydropterin synthase.
Related PDB1b66,1b6z
Related Swiss-protP27213
[6]
PubMed ID10737935
JournalProteins
Year2000
Volume39
Pages142-54
AuthorsColloc'h N, Poupon A, Mornon JP
TitleSequence and structural features of the T-fold, an original tunnelling building unit.
[7]
PubMed ID12123838
JournalFEBS Lett
Year2002
Volume523
Pages234-8
AuthorsWoo HJ, Hwang YK, Kim YJ, Kang JY, Choi YK, Kim CG, Park YS
TitleEscherichia coli 6-pyruvoyltetrahydropterin synthase ortholog encoded by ygcM has a new catalytic activity for conversion of sepiapterin to 7,8-dihydropterin.

comments
E.C. number was transferred from 4.6.1.10 to 4.2.3.12.

createdupdated
2004-06-282009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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