EzCatDB: S00252

DB codeS00252
CATH domainDomain 13.30.1330.40Catalytic domain
E.C.5.4.99.5
CSA1dbf


Enzyme Name
Swiss-protKEGG

P19080Q84FH6
Protein nameChorismate mutase
chorismate mutase
hydroxyphenylpyruvate synthase
SynonymsCM
EC 5.4.99.5
Chorismate mutase
EC 5.4.99.5

KEGG pathways
MAP codePathways
MAP00400Phenylalanine, tyrosine and tryptophan biosynthesis

Swiss-prot:Accession NumberP19080Q84FH6
Entry nameCHMU_BACSUQ84FH6_THETH
ActivityChorismate = prephenate.
SubunitHomotrimer.
Subcellular locationCytoplasm.
Cofactor



SubstratesProductsintermediates
KEGG-idC00251C00254
CompoundChorismatePrephenate
Typecarbohydrate,carboxyl groupcarbohydrate,carboxyl group
1comAUnboundBound:PREUnbound
1comBUnboundBound:PREUnbound
1comCUnboundBound:PREUnbound
1comDUnboundBound:PREUnbound
1comEUnboundBound:PREUnbound
1comFUnboundBound:PREUnbound
1comGUnboundBound:PREUnbound
1comHUnboundBound:PREUnbound
1comIUnboundUnboundUnbound
1comJUnboundUnboundUnbound
1comKUnboundBound:PREUnbound
1comLUnboundUnboundUnbound
1dbfAUnboundUnboundUnbound
1dbfBUnboundUnboundUnbound
1dbfCUnboundUnboundUnbound
1fnjAUnboundUnboundUnbound
1fnkAUnboundUnboundUnbound
2chsAUnboundUnboundUnbound
2chsBUnboundUnboundUnbound
2chsCUnboundUnboundUnbound
2chsDUnboundUnboundUnbound
2chsEUnboundUnboundUnbound
2chsFUnboundUnboundUnbound
2chsGUnboundUnboundUnbound
2chsHUnboundUnboundUnbound
2chsIUnboundUnboundUnbound
2chsJUnboundUnboundUnbound
2chsKUnboundUnboundUnbound
2chsLUnboundUnboundUnbound
2chtAUnboundUnboundTransition-state-analogue:TSA
2chtBUnboundUnboundTransition-state-analogue:TSA
2chtCUnboundUnboundTransition-state-analogue:TSA
2chtDUnboundUnboundTransition-state-analogue:TSA
2chtEUnboundUnboundTransition-state-analogue:TSA
2chtFUnboundUnboundTransition-state-analogue:TSA
2chtGUnboundUnboundTransition-state-analogue:TSA
2chtHUnboundUnboundTransition-state-analogue:TSA
2chtIUnboundUnboundTransition-state-analogue:TSA
2chtJUnboundUnboundTransition-state-analogue:TSA
2chtKUnboundUnboundTransition-state-analogue:TSA
2chtLUnboundUnboundTransition-state-analogue:TSA
1odeAUnboundUnboundUnbound
1odeBUnboundUnboundUnbound
1odeCUnboundUnboundUnbound
1ufyAAnalogue:MLIUnboundUnbound
1ui9AUnboundUnboundUnbound

Active-site residues
resource
literature [5], [12], [14]
pdbCatalytic residuescomment
1comAARG 90

1comBARG 90

1comCARG 90

1comDARG 90

1comEARG 90

1comFARG 90

1comGARG 90

1comHARG 90

1comIARG 90

1comJARG 90

1comKARG 90

1comLARG 90

1dbfAARG 90

1dbfBARG 90

1dbfCARG 90

1fnjA      
mutant C88S, R90K
1fnkA      
mutant C88K, R90S
2chsAARG 90

2chsBARG 90

2chsCARG 90

2chsDARG 90

2chsEARG 90

2chsFARG 90

2chsGARG 90

2chsHARG 90

2chsIARG 90

2chsJARG 90

2chsKARG 90

2chsLARG 90

2chtAARG 90

2chtBARG 90

2chtCARG 90

2chtDARG 90

2chtEARG 90

2chtFARG 90

2chtGARG 90

2chtHARG 90

2chtIARG 90

2chtJARG 90

2chtKARG 90

2chtLARG 90

1odeAARG 89

1odeBARG 89

1odeCARG 89

1ufyAARG 89

1ui9AARG 89


References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]1FIG.1, p.8602
[5]Fig.1, p.494-498
[6]Fig.1, Fig.6, Fig.7, p.650-651
[7]Fig.1, Fig.5, Fig.6, p.200-201
[9]Fig.1, Fig.2, p.5047-5048
[12]p.678-679, p.681-682
[15]Fig.1, Fig.4, p.36836-36838
[16]Scheme 1
[20]Fig.1
[21]Fig.2
[22]Scheme 1
[23]Scheme 1
[24]Fig.1, p.3206
[25]p.5598
[27]Scheme 1
[28]Scheme 1

references
[1]
PubMed ID2125470
JournalBiochemistry
Year1990
Volume29
Pages8872-8
AuthorsGray JV, Eren D, Knowles JR
TitleMonofunctional chorismate mutase from Bacillus subtilis: kinetic and 13C NMR studies on the interactions of the enzyme with its ligands.
[2]
CommentsSTRUCTURE BY NMR.
Medline ID93229495
PubMed ID8471608
JournalBiochemistry
Year1993
Volume32
Pages3965-72
AuthorsRajagopalan JS, Taylor KM, Jaffe EK
Title13C NMR studies of the enzyme-product complex of Bacillus subtilis chorismate mutase.
Related Swiss-protP19080
[3]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medline ID93391402
PubMed ID8378335
JournalProc Natl Acad Sci U S A
Year1993
Volume90
Pages8600-3
AuthorsChook YM, Ke H, Lipscomb WN
TitleCrystal structures of the monofunctional chorismate mutase from Bacillus subtilis and its complex with a transition state analog.
Related PDB2chs,2cht
Related Swiss-protP19080
[4]
PubMed ID8061004
JournalBiochemistry
Year1994
Volume33
Pages9953-9
AuthorsGray JV, Knowles JR
TitleMonofunctional chorismate mutase from Bacillus subtilis: FTIR studies and the mechanism of action of the enzyme.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
Medline ID94322390
PubMed ID8046752
JournalJ Mol Biol
Year1994
Volume240
Pages476-500
AuthorsChook YM, Gray JV, Ke H, Lipscomb WN
TitleThe monofunctional chorismate mutase from Bacillus subtilis. Structure determination of chorismate mutase and its complexes with a transition state analog and prephenate, and implications for the mechanism of the enzymatic reaction.
Related PDB1com
Related Swiss-protP19080
[6]
PubMed ID8303271
JournalScience
Year1994
Volume263
Pages646-52
AuthorsHaynes MR, Stura EA, Hilvert D, Wilson IA
TitleRoutes to catalysis: structure of a catalytic antibody and comparison with its natural counterpart.
[7]
PubMed ID9383421
JournalChem Biol
Year1995
Volume2
Pages195-203
AuthorsLee AY, Stewart JD, Clardy J, Ganem B
TitleNew insight into the catalytic mechanism of chorismate mutases from structural studies.
[8]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-109
JournalJ Am Chem Soc
Year1995
Volume117
Pages3627-8
AuthorsLee AY, Karplus PA, Ganem B, Clardy J
TitleAtomic structure of the buried catalytic pocket of Escherichia coli horismate mutase.
[9]
PubMed ID8643526
JournalProc Natl Acad Sci U S A
Year1996
Volume93
Pages5043-8
AuthorsKast P, Asif-Ullah M, Jiang N, Hilvert D
TitleExploring the active site of chorismate mutase by combinatorial mutagenesis and selection: the importance of electrostatic catalysis.
[10]
PubMed ID9384560
JournalStructure
Year1997
Volume5
Pages1437-52
AuthorsStrater N, Schnappauf G, Braus G, Lipscomb WN
TitleMechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures.
[11]
PubMed ID10103029
JournalEur J Biochem
Year1999
Volume261
Pages25-32
AuthorsMattei P, Kast P, Hilvert D
TitleBacillus subtilis chorismate mutase is partially diffusion-controlled.
[12]
CommentsX-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS).
Medline ID20280181
PubMed ID10818343
JournalActa Crystallogr D Biol Crystallogr
Year2000
Volume56
Pages673-83
AuthorsLadner JE, Reddy P, Davis A, Tordova M, Howard AJ, Gilliland GL
TitleThe 1.30 A resolution structure of the Bacillus subtilis chorismate mutase catalytic homotrimer.
Related PDB1dbf
Related Swiss-protP19080
[13]
PubMed ID11087356
JournalBiochemistry
Year2000
Volume39
Pages14087-94
AuthorsGamper M, Hilvert D, Kast P
TitleProbing the role of the C-terminus of Bacillus subtilis chorismate mutase by a novel random protein-termination strategy.
[14]
PubMed ID10815997
JournalComput Chem
Year2000
Volume24
Pages275-85
AuthorsWorthington SE, Krauss M
TitleEffective fragment potentials and the enzyme active site.
[15]
CommentsX-ray crystallography
PubMed ID10960481
JournalJ Biol Chem
Year2000
Volume275
Pages36832-8
AuthorsKast P, Grisostomi C, Chen IA, Li S, Krengel U, Xue Y, Hilvert D
TitleA strategically positioned cation is crucial for efficient catalysis by chorismate mutase.
Related PDB1fnj,1fnk
[16]
PubMed ID11456771
JournalJ Am Chem Soc
Year2001
Volume123
Pages1709-12
AuthorsMarti S, Andres J, Moliner V, Silla E, Tunon I, Bertran J, Field MJ
TitleA hybrid potential reaction path and free energy study of the chorismate mutase reaction.
[17]
PubMed ID11495249
JournalJ Biomol NMR
Year2001
Volume20
Pages177-80
AuthorsEletsky A, Kienhofer A, Pervushin K
TitleTROSY NMR with partially deuterated proteins.
[18]
PubMed ID12392438
JournalJ Am Chem Soc
Year2002
Volume124
Pages12898-902
AuthorsPervushin K, Vogeli B, Eletsky A
TitleLongitudinal (1)H relaxation optimization in TROSY NMR spectroscopy.
[19]
PubMed ID12449416
JournalJ Biomol NMR
Year2002
Volume24
Pages31-9
AuthorsEletsky A, Heinz T, Moreira O, Kienhofer A, Hilvert D, Pervushi K
TitleDirect NMR observation and DFT calculations of a hydrogen bond at the active site of a 44 kDa enzyme.
[20]
PubMed ID12698486
JournalAngew Chem Int Ed Engl
Year2003
Volume42
Pages1508-11
AuthorsGuo H, Cui Q, Lipscomb WN, Karplus M
TitleUnderstanding the role of active-site residues in chorismate mutase catalysis from molecular-dynamics simulations.
[21]
PubMed ID12584715
JournalChemistry
Year2003
Volume9
Pages984-91
AuthorsMarti S, Andres J, Moliner V, Silla E, Tunon I, Bertran J
TitlePreorganization and reorganization as related factors in enzyme catalysis: the chorismate mutase case.
[22]
PubMed ID12783541
JournalJ Am Chem Soc
Year2003
Volume125
Pages6892-9
AuthorsGuimaraes CR, Repasky MP, Chandrasekhar J, Tirado-Rives J, Jorgensen WL
TitleContributions of conformational compression and preferential transition state stabilization to the rate enhancement by chorismate mutase.
[23]
PubMed ID12940735
JournalJ Am Chem Soc
Year2003
Volume125
Pages10540-2
AuthorsHur S, Bruice TC
TitleJust a near attack conformer for catalysis (chorismate to prephenate rearrangements in water, antibody, enzymes, and their mutants).
[24]
PubMed ID12630863
JournalJ Am Chem Soc
Year2003
Volume125
Pages3206-7
AuthorsKienhofer A, Kast P, Hilvert D
TitleSelective stabilization of the chorismate mutase transition state by a positively charged hydrogen bond donor.
[25]
PubMed ID12733875
JournalJ Am Chem Soc
Year2003
Volume125
Pages5598-9
AuthorsMandal A, Hilvert D
TitleCharge optimization increases the potency and selectivity of a chorismate mutase inhibitor.
[26]
PubMed ID12766412
JournalJ Biomol NMR
Year2003
Volume26
Pages167-79
AuthorsEletsky A, Moreira O, Kovacs H, Pervushin K
TitleA novel strategy for the assignment of side-chain resonances in completely deuterated large proteins using 13C spectroscopy.
[27]
PubMed ID12926249
JournalOrg Biomol Chem
Year2003
Volume1
Pages483-7
AuthorsMarti S, Moliner V, Tunon I, Williams IH
TitleQM/MM calculations of kinetic isotope effects in the chorismate mutase active site.
[28]
PubMed ID14523243
JournalProc Natl Acad Sci U S A
Year2003
Volume100
Pages12015-20
AuthorsHur S, Bruice TC
TitleThe near attack conformation approach to the study of the chorismate to prephenate reaction.
[29]
PubMed ID14727008
JournalArch Microbiol
Year2004
Volume181
Pages195-203
AuthorsHelmstaedt K, Heinrich G, Merkl R, Braus GH
TitleChorismate mutase of Thermus thermophilus is a monofunctional AroH class enzyme inhibited by tyrosine.
Related Swiss-protQ84FH6
[30]
PubMed ID15136856
JournalChem Commun (Camb)
Year2004
Volume(10)
Pages1238-9
AuthorsRanaghan KE, Mulholland AJ
TitleConformational effects in enzyme catalysis: QM/MM free energy calculation of the 'NAC' contribution in chorismate mutase.
[31]
PubMed ID15096202
JournalEur J Biochem
Year2004
Volume271
Pages1630-7
AuthorsWoycechowsky KJ, Hilvert D
TitleDeciphering enzymes. Genetic selection as a probe of structure and mechanism.

comments
This enzyme catalyzes Claisen rearrangement (or concerted addition and elimination).

createdupdated
2005-07-112009-02-26


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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