DB code: S00023

CATH domain 1.10.590.10 : Chorismate Mutase, subunit A Catalytic domain
E.C. 5.4.99.5
CSA 3csm
M-CSA 3csm
MACiE M0081

CATH domain Related DB codes (homologues)

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P32178 Chorismate mutase
CM
EC 5.4.99.5
NP_015385.1 (Protein)
NM_001184157.1 (DNA/RNA sequence)
PF01817 (CM_2)
[Graphical View]

KEGG enzyme name
chorismate mutase
hydroxyphenylpyruvate synthase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P32178 CHMU_YEAST Chorismate = prephenate. Homodimer.

KEGG Pathways
Map code Pathways E.C.
MAP00400 Phenylalanine, tyrosine and tryptophan biosynthesis

Compound table
Substrates Products Intermediates
KEGG-id C00251 C00254
E.C.
Compound Chorismate Prephenate
Type carbohydrate,carboxyl group carbohydrate,carboxyl group
ChEBI 17333
84387
PubChem 12039
1csmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1csmB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
2csmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
3csmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:TSA
3csmB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:TSA
4csmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:TSA
4csmB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:TSA
5csmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [7], [9], [14]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1csmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 168;GLU 246 mutant T226I
1csmB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 168;GLU 246 mutant T226I
2csmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 168;GLU 246
3csmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 168;GLU 246
3csmB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 168;GLU 246
4csmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 168;GLU 246
4csmB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 168;GLU 246
5csmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 168;GLU 246 mutant T226S

References for Catalytic Mechanism
References Sections No. 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]
Resource
Comments
Medline ID
PubMed ID 2187528
Journal Biochemistry
Year 1990
Volume 29
Pages 3660-8
Authors Schmidheini T, Mosch HU, Evans JN, Braus G
Title Yeast allosteric chorismate mutase is locked in the activated state by a single amino acid substitution.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 8218394
Journal Biochim Biophys Acta
Year 1993
Volume 1203
Pages 71-6
Authors Ramilo C, Braus G, Evans JN
Title A tyrosine residue is involved in the allosteric binding of tryptophan to yeast chorismate mutase.
Related PDB
Related UniProtKB
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
Medline ID 95062155
PubMed ID 7971967
Journal Proc Natl Acad Sci U S A
Year 1994
Volume 91
Pages 10814-8
Authors Xue Y, Lipscomb WN, Graf R, Schnappauf G, Braus G
Title The crystal structure of allosteric chorismate mutase at 2.2-A resolution.
Related PDB 1csm
Related UniProtKB P32178
[4]
Resource
Comments
Medline ID
PubMed ID 7883726
Journal J Bacteriol
Year 1995
Volume 177
Pages 1645-8
Authors Graf R, Dubaquie Y, Braus GH
Title Modulation of the allosteric equilibrium of yeast chorismate mutase by variation of a single amino acid residue.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 7479847
Journal Proc Natl Acad Sci U S A
Year 1995
Volume 92
Pages 10595-8
Authors Xue Y, Lipscomb WN
Title Location of the active site of allosteric chorismate mutase from Saccharomyces cerevisiae, and comments on the catalytic and regulatory mechanisms.
Related PDB
Related UniProtKB
[6]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
Medline ID 96194968
PubMed ID 8622937
Journal Proc Natl Acad Sci U S A
Year 1996
Volume 93
Pages 3330-4
Authors Strater N, Hakansson K, Schnappauf G, Braus G, Lipscomb WN
Title Crystal structure of the T state of allosteric yeast chorismate mutase and comparison with the R state.
Related PDB 2csm
Related UniProtKB P32178
[7]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Medline ID 98046093
PubMed ID 9384560
Journal Structure
Year 1997
Volume 5
Pages 1437-52
Authors Strater N, Schnappauf G, Braus G, Lipscomb WN
Title Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures.
Related PDB 3csm 4csm 5csm
Related UniProtKB P32178
[8]
Resource
Comments
Medline ID
PubMed ID 9299331
Journal J Mol Biol
Year 1997
Volume 271
Pages 838-45
Authors Lin SL, Xu D, Li A, Rosen M, Wolfson HJ, Nussinov R
Title Investigation of the enzymatic mechanism of the yeast chorismate mutase by docking a transition state analog.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 9843942
Journal Proc Natl Acad Sci U S A
Year 1998
Volume 95
Pages 14640-5
Authors Ma J, Zheng X, Schnappauf G, Braus G, Karplus M, Lipscomb WN
Title Yeast chorismate mutase in the R state: simulations of the active site.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 9501182
Journal Proc Natl Acad Sci U S A
Year 1998
Volume 95
Pages 2868-73
Authors Schnappauf G, Lipscomb WN, Braus GH
Title Separation of inhibition and activation of the allosteric yeast chorismate mutase.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 9626703
Journal Proteins
Year 1998
Volume 31
Pages 445-52
Authors Lin SL, Xu D, Li A, Nussinov R
Title Electrostatics, allostery, and activity of the yeast chorismate mutase.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 9843375
Journal Biochemistry
Year 1998
Volume 37
Pages 15703-12
Authors Christendat D, Saridakis VC, Turnbull JL
Title Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by chorismate mutase-prephenate dehydrogenase from Escherichia coli.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 10894726
Journal J Bacteriol
Year 2000
Volume 182
Pages 4188-97
Authors Krappmann S, Pries R, Gellissen G, Hiller M, Braus GH
Title HARO7 encodes chorismate mutase of the methylotrophic yeast Hansenula polymorpha and is derepressed upon methanol utilization.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 11528003
Journal Microbiol Mol Biol Rev
Year 2001
Volume 65
Pages 404-21, table of contents
Authors Helmstaedt K, Krappmann S, Braus GH
Title Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 11481470
Journal Proc Natl Acad Sci U S A
Year 2001
Volume 98
Pages 9032-7
Authors Guo H, Cui Q, Lipscomb WN, Karplus M
Title Substrate conformational transitions in the active site of chorismate mutase: their role in the catalytic mechanism.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 11997452
Journal Proc Natl Acad Sci U S A
Year 2002
Volume 99
Pages 6631-6
Authors Helmstaedt K, Heinrich G, Lipscomb WN, Braus GH
Title Refined molecular hinge between allosteric and catalytic domain determines allosteric regulation and stability of fungal chorismate mutase.
Related PDB
Related UniProtKB

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]).

Created Updated
2005-06-17 2009-02-26