EzCatDB: S00023
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DB codeS00023
CATH domainDomain 11.10.590.10 : Chorismate Mutase, subunit ACatalytic domain
E.C.5.4.99.5
CSA3csm
MACiEM0081


Enzyme Name
UniProtKBKEGG

P32178
Protein nameChorismate mutasechorismate mutase
hydroxyphenylpyruvate synthase
SynonymsCM
EC 5.4.99.5
RefSeqNP_015385.1 (Protein)
NM_001184157.1 (DNA/RNA sequence)
PfamPF01817 (CM_2)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00400Phenylalanine, tyrosine and tryptophan biosynthesis

UniProtKB:Accession NumberP32178
Entry nameCHMU_YEAST
ActivityChorismate = prephenate.
SubunitHomodimer.
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00251C00254
CompoundChorismatePrephenate
Typecarbohydrate,carboxyl groupcarbohydrate,carboxyl group
ChEBI17333
84387

PubChem12039


           
1csmAUnboundUnboundUnbound
1csmBUnboundUnboundUnbound
2csmAUnboundUnboundUnbound
3csmAUnboundUnboundTransition-state-analogue:TSA
3csmBUnboundUnboundTransition-state-analogue:TSA
4csmAUnboundUnboundTransition-state-analogue:TSA
4csmBUnboundUnboundTransition-state-analogue:TSA
5csmAUnboundUnboundUnbound

Active-site residues
resource
literature [7], [9], [14]
pdbCatalytic residuescomment
          
1csmALYS 168;GLU 246
mutant T226I
1csmBLYS 168;GLU 246
mutant T226I
2csmALYS 168;GLU 246
 
3csmALYS 168;GLU 246
 
3csmBLYS 168;GLU 246
 
4csmALYS 168;GLU 246
 
4csmBLYS 168;GLU 246
 
5csmALYS 168;GLU 246
mutant T226S

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[5]Fig.1, p.10597-10598
[6]p.3332-3333
[7]Fig.1, p.1446
[9]Fig.2, p.14644-14645
[14]Fig.2, p.410-411
[15]Fig.1

references
[1]
PubMed ID2187528
JournalBiochemistry
Year1990
Volume29
Pages3660-8
AuthorsSchmidheini T, Mosch HU, Evans JN, Braus G
TitleYeast allosteric chorismate mutase is locked in the activated state by a single amino acid substitution.
[2]
PubMed ID8218394
JournalBiochim Biophys Acta
Year1993
Volume1203
Pages71-6
AuthorsRamilo C, Braus G, Evans JN
TitleA tyrosine residue is involved in the allosteric binding of tryptophan to yeast chorismate mutase.
[3]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
Medline ID95062155
PubMed ID7971967
JournalProc Natl Acad Sci U S A
Year1994
Volume91
Pages10814-8
AuthorsXue Y, Lipscomb WN, Graf R, Schnappauf G, Braus G
TitleThe crystal structure of allosteric chorismate mutase at 2.2-A resolution.
Related PDB1csm
Related UniProtKBP32178
[4]
PubMed ID7883726
JournalJ Bacteriol
Year1995
Volume177
Pages1645-8
AuthorsGraf R, Dubaquie Y, Braus GH
TitleModulation of the allosteric equilibrium of yeast chorismate mutase by variation of a single amino acid residue.
[5]
PubMed ID7479847
JournalProc Natl Acad Sci U S A
Year1995
Volume92
Pages10595-8
AuthorsXue Y, Lipscomb WN
TitleLocation of the active site of allosteric chorismate mutase from Saccharomyces cerevisiae, and comments on the catalytic and regulatory mechanisms.
[6]
CommentsX-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
Medline ID96194968
PubMed ID8622937
JournalProc Natl Acad Sci U S A
Year1996
Volume93
Pages3330-4
AuthorsStrater N, Hakansson K, Schnappauf G, Braus G, Lipscomb WN
TitleCrystal structure of the T state of allosteric yeast chorismate mutase and comparison with the R state.
Related PDB2csm
Related UniProtKBP32178
[7]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Medline ID98046093
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.
Related PDB3csm,4csm,5csm
Related UniProtKBP32178
[8]
PubMed ID9299331
JournalJ Mol Biol
Year1997
Volume271
Pages838-45
AuthorsLin SL, Xu D, Li A, Rosen M, Wolfson HJ, Nussinov R
TitleInvestigation of the enzymatic mechanism of the yeast chorismate mutase by docking a transition state analog.
[9]
PubMed ID9843942
JournalProc Natl Acad Sci U S A
Year1998
Volume95
Pages14640-5
AuthorsMa J, Zheng X, Schnappauf G, Braus G, Karplus M, Lipscomb WN
TitleYeast chorismate mutase in the R state: simulations of the active site.
[10]
PubMed ID9501182
JournalProc Natl Acad Sci U S A
Year1998
Volume95
Pages2868-73
AuthorsSchnappauf G, Lipscomb WN, Braus GH
TitleSeparation of inhibition and activation of the allosteric yeast chorismate mutase.
[11]
PubMed ID9626703
JournalProteins
Year1998
Volume31
Pages445-52
AuthorsLin SL, Xu D, Li A, Nussinov R
TitleElectrostatics, allostery, and activity of the yeast chorismate mutase.
[12]
PubMed ID9843375
JournalBiochemistry
Year1998
Volume37
Pages15703-12
AuthorsChristendat D, Saridakis VC, Turnbull JL
TitleUse of site-directed mutagenesis to identify residues specific for each reaction catalyzed by chorismate mutase-prephenate dehydrogenase from Escherichia coli.
[13]
PubMed ID10894726
JournalJ Bacteriol
Year2000
Volume182
Pages4188-97
AuthorsKrappmann S, Pries R, Gellissen G, Hiller M, Braus GH
TitleHARO7 encodes chorismate mutase of the methylotrophic yeast Hansenula polymorpha and is derepressed upon methanol utilization.
[14]
PubMed ID11528003
JournalMicrobiol Mol Biol Rev
Year2001
Volume65
Pages404-21, table of contents
AuthorsHelmstaedt K, Krappmann S, Braus GH
TitleAllosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase.
[15]
PubMed ID11481470
JournalProc Natl Acad Sci U S A
Year2001
Volume98
Pages9032-7
AuthorsGuo H, Cui Q, Lipscomb WN, Karplus M
TitleSubstrate conformational transitions in the active site of chorismate mutase: their role in the catalytic mechanism.
[16]
PubMed ID11997452
JournalProc Natl Acad Sci U S A
Year2002
Volume99
Pages6631-6
AuthorsHelmstaedt K, Heinrich G, Lipscomb WN, Braus GH
TitleRefined molecular hinge between allosteric and catalytic domain determines allosteric regulation and stability of fungal chorismate mutase.

comments
This enzyme has an allosteric site, to which tryptophan (for activation) or tyrosine (for inhibition) is bound. The site is separate from the active site.
According to the literature [9] & [14], this enzyme catalyzes Claisen rearrangement or concerted addition and elimination.
According to the literature [7], [9] & [14], Glu246 can be mutated to glutamine residue, as it is a glutamine residue in the counterparts of E. coli and bacteria. Although the wild-type enzyme has an optimum in acidic pH, E246Q mutant has catalytic activity over a broad pH range (see [14]).

createdupdated
2005-06-172009-02-26
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 2008)
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)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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