Information on EC 5.4.99.5 - Chorismate mutase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
5.4.99.5
-
RECOMMENDED NAME
GeneOntology No.
Chorismate mutase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Chorismate = prephenate
show the reaction diagram
-
-
-
-
Chorismate = prephenate
show the reaction diagram
Three active sites are formed in the interstices between three subunits. Each active site is composed of the residues of two adjacent subunits. The two Arg hold the chorismate. Crucial distance between Arg6 and Arg63* controls the conformation of the chorismate. The residues in the close vicinity to the chorismate substrate are Arg6, Glu77, Arg89, Tyr 107, Leu114, and Arg115 from one subunit and Phe57*, Ala59*, Arg63*, Leu72*, and Leu73* from the other subunit. The family of the chorismate mutase enzymes shares a common E.S active site
-
Chorismate = prephenate
show the reaction diagram
the active site is formed within a single chain without any contribution from the second chain in a dimer
-
Chorismate = prephenate
show the reaction diagram
CMs are extremly versatile enzymes and can be strucurally divided into two major groups: the type I or AroH class, which comprises CMs characterized by a trimericpseudo alpha/beta-barrel structure, and the type II or AroQ class, which comprises CMs, can also be monofunctional, bifunctional (generally fused to another shikimate pathway member), exported, and/or allosterically regulated
-
-
Chorismate = prephenate
show the reaction diagram
CMs are extremly versatile enzymes and can be structurally divided into two major groups: the type I or AroH class, which comprises CMs characterized by a trimericpseudo alpha/beta-barrel structure, and the type II or AroQ class, which comprises CMs can also be monofunctional, bifunctional (generally fused to another shikimate pathway member), exported, and/or allosterically regulated
A0QU81, -
Chorismate = prephenate
show the reaction diagram
Wild-type-reaction: Arg63, Arg116, Arg7, and Tyr108 required for the relative orientation of the substrate at the active site, the structural rearrangement in the Glu78-Arg90-substrate controls the strength of the hydrogen bonds. The hydrogen bonds connecting the Glu78-Arg90-substrate cooperatively control the stability of TS relative to the ES complex and the positive charge on Arg90 polarizes the substrate in the TS region to gain more electrostatic stabilization. Method: electron quantum chemical calculations by fragment molecular orbital (FMO) method. The structural refinement and reaction path search are performed by the ab initio QM/MM treatment. Usage of the AMBER standard parameter set (parm.96) for the MM force-field calculations. Reaction path search: On the basis of the gas-phase IRC (intrinsic reaction coordinate) profile of chorismate isomerization, the linear reaction path is calculated first
-
Chorismate = prephenate
show the reaction diagram
The active site of the enzyme which is found in a pocket formed by two different chains is shown. Applying the TPS method of Chandler and co-workers to study the chorismate to prephenate reaction
P19080
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
group transfer
-
-
intramolecular
-
isomerization
-
-
-
-
isomerization
-
Claisen rearrangement
rearrangement
-
Claisen rearrangement
rearrangement
-
Claisen rearrangement
rearrangement
-
-
example of an enzyme-catalyzed pericyclic process known as Claisen rearrangement
rearrangement
A0QU81, -
example of an enzyme-catalyzed pericyclic process known as Claisen rearrangement
rearrangement
-
Claisen rearrangement
rearrangement
P19080
The CM reaction is a Claisen rearrangement and is one of the few examples of a biochemical sigmatropic rearrangements
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
Metabolic pathways
-
phenylalanine biosynthesis I
-
phenylalanine biosynthesis II
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
salinosporamide A biosynthesis
-
tyrosine biosynthesis I
-
tyrosine biosynthesis II
-
tyrosine biosynthesis III
-
SYSTEMATIC NAME
IUBMB Comments
Chorismate pyruvatemutase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4-Amino-4-deoxychorismate mutase
-
-
-
-
Bacillus subtilis chorismate mutase
-
-
chorismate mutase
-
-
-
chorismate mutase
P19080
-
chorismate mutase
-
-
chorismate mutase
Escherichia coli JFM-30
-
-
-
chorismate mutase
-
-
chorismate mutase
-
-
chorismate mutase
A0QU81
-
chorismate mutase
-
belongs to the *AroQclass of chorismate mutases
chorismate mutase
-
-
chorismate mutase
-
-
chorismate mutase
Q84FH6
-
chorismate mutase 1
-
-
chorismate mutase-prephenate dehydrogenase
-
bifunctional enzyme
chorismate mutase-prephenate dehydrogenase
Escherichia coli JM101
-
bifunctional enzyme
-
Chorismate mutase/prephenate dehydratase
-
-
-
-
Chorismate mutase/prephenate dehydratase
-
-
CM-1
B6C761
isozyme
CM-prephenate dehydratase
-
bifunctional enzyme
CM-prephenate dehydratase
Escherichia coli JM101
-
bifunctional enzyme
-
CM-TyrAp
-
bifunctional enzyme
CM-TyrAp
Escherichia coli JM101
-
bifunctional enzyme
-
CM/PDT
-
bi-functional chorismate mutase/prephenate dehydratase
CM1
D2CSU4
isozyme
CM2
D2CSU5
isozyme
Mutase, chorismate
-
-
-
-
Mycobacterium tuberculosis chorismate mutase
-
-
Mycobacterium tuberculosis H37Rv chorismate mutase
-
-
P protein
-
-
-
-
P-protein
-
-
y2828
Q7CHH5
-
CAS REGISTRY NUMBER
COMMENTARY
9068-30-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
bifunctional enzyme: chorismate mutase/prephenate dehydratase
-
-
Manually annotated by BRENDA team
Anthophyta
contain 3 isoenzymes with the exception of some closely related Leguminosae
-
-
Manually annotated by BRENDA team
cytosolic and plastidic isoenzyme
-
-
Manually annotated by BRENDA team
monofunctional enzyme
-
-
Manually annotated by BRENDA team
strain 23 and its derivatives have 3 distinct enzyme species: CM1, CM2, and CM3. Strain 168 has only the CM3 form. Enzyme forms CM1 and CM2 may represent different aggregation states involving at least one common subunit
-
-
Manually annotated by BRENDA team
There are four published structures of the Bacillus subtilis wild-type chroismate mutase (CM) with Protein Data Bank (PDB) codes 1COM, 2CHS, 2CHT, and 1DBF
swissprot
Manually annotated by BRENDA team
Bacillus subtilis 23
strain 23 and its derivatives have 3 distinct enzyme species: CM1, CM2, and CM3. Strain 168 has only the CM3 form. Enzyme forms CM1 and CM2 may represent different aggregation states involving at least one common subunit
-
-
Manually annotated by BRENDA team
bifunctional enzyme: chorismate mutase/prephenate dehydratase
-
-
Manually annotated by BRENDA team
Pb 156, 2 enzyme forms: MW 55000 and MW 59000
-
-
Manually annotated by BRENDA team
Claviceps sp.
SD 58
-
-
Manually annotated by BRENDA team
Claviceps sp. SD 58
SD 58
-
-
Manually annotated by BRENDA team
strain ATCC 13032
-
-
Manually annotated by BRENDA team
basonym Alcaligenes eutrophus
-
-
Manually annotated by BRENDA team
Orchard grass
-
-
Manually annotated by BRENDA team
2 enzyme forms: chorismate mutase P and chorismate mutase T. Chorismate mutase P is associated with prephenate dehydratase, chorismate mutase T is associated with prephenate dehydrogenase
-
-
Manually annotated by BRENDA team
chorismate mutase/prephenate dehydratase
-
-
Manually annotated by BRENDA team
bifunctional enzyme chorismate mutase/prephenate dehydratase
-
-
Manually annotated by BRENDA team
bifunctional enzyme chorismate mutase/prephenate dehydratase; K12
-
-
Manually annotated by BRENDA team
monofunctional enzyme
-
-
Manually annotated by BRENDA team
mutant enzymes Lys39Arg, Lys39Asn, Lys39Gln, Gln88Arg, and Gln88Glu
-
-
Manually annotated by BRENDA team
strain JFM-30
-
-
Manually annotated by BRENDA team
strain JM101
-
-
Manually annotated by BRENDA team
Escherichia coli JFM-30
strain JFM-30
-
-
Manually annotated by BRENDA team
Escherichia coli JM101
strain JM101
-
-
Manually annotated by BRENDA team
Escherichia coli K12
K12
-
-
Manually annotated by BRENDA team
isozyme CM-1; pathotype Ro1
UniProt
Manually annotated by BRENDA team
enzyme forms: CM1, CM2, and CM3
-
-
Manually annotated by BRENDA team
nonpathogenic species, Analysis of promoter activity described
Swissprot
Manually annotated by BRENDA team
encoded by Rv1885c
Uniprot
Manually annotated by BRENDA team
recombinant protein coded by the open reading frame Rv0948; recombinant protein coded by the open reading frame Rv1885c
-
-
Manually annotated by BRENDA team
Sequence data for Mycobacterium tuberculosis H37Rv and Mycobacterium leprae TN were obtained from the TubercuList (http://genolist.pasteur.fr/TubercuList/) and Leproma (http://genolist.pasteur.fr/Leproma/) databases; intracellular pathogen, studies of construction of mycobacterial reporter plasmids, organization of Rv0948c and Rv1885c promoter region, analysis of promoter activity
-
-
Manually annotated by BRENDA team
Nephrolysis sp.
2 isoenzymes: CM1, CM2
-
-
Manually annotated by BRENDA team
one enzyme form: CM1
-
-
Manually annotated by BRENDA team
2 enzyme forms: CM1 and CM2
-
-
Manually annotated by BRENDA team
no activity in Corynebacterium diphtheriae
-
-
-
Manually annotated by BRENDA team
no activity in Mycobacterium leprae
-
-
-
Manually annotated by BRENDA team
no activity in Nocardia farcinica
-
-
-
Manually annotated by BRENDA team
2 enzyme forms: CM1 and CM3
-
-
Manually annotated by BRENDA team
Penicillium duponti
3 enzyme forms: CM1, CM2, CM3
-
-
Manually annotated by BRENDA team
cultivar Mitchell Diploid
UniProt
Manually annotated by BRENDA team
Pinus sp.
2 isoenzymes: CM1, CM2
-
-
Manually annotated by BRENDA team
2 isoenzymes: CM1 and CM2
-
-
Manually annotated by BRENDA team
Thr226Ile mutant
-
-
Manually annotated by BRENDA team
Selaginella sp.
2 isoenzymes: CM1, CM2
-
-
Manually annotated by BRENDA team
2 enzyme forms: CM1 and CM2
-
-
Manually annotated by BRENDA team
2 enzyme forms: CM1 and CM2; the enzyme form CM1 and CM2 show no immunological similarity
-
-
Manually annotated by BRENDA team
Streptomyces aureofaciens tue 24
tue 24
-
-
Manually annotated by BRENDA team
2 enzyme forms: CM1 and CM2
-
-
Manually annotated by BRENDA team
2 isoenzymes
-
-
Manually annotated by BRENDA team
Xanthomonas oryzae pv. oryzae XKK.12
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
single-cell transient-induced gene silencing of CM1 in mildew resistance locus a (Mla) compromised cells results in increased susceptibility to Blumeria graminis f. sp. hordei
malfunction
-
Xanthomonas oryzae pv. oryzae chorismate mutase knock-out mutants are hypervirulent to rice
metabolism
-
chorismate mutase is the first and the key enzyme that diverges the shikimate pathway to either tryptophan or phenylalanine and tyrosine
metabolism
-
transgenic Arabidopsis plants expressing a truncated, feedback-insensitive chorismate mutase/prephenate dehydratase gene accumulate Phe (up to 100fold compared to control plants) and are more sensitive than wild-type plants to the Trp biosynthesis inhibitor 5-methyl-Trp. Thus Phe biosynthesis competes with Trp biosynthesis from their common precursor chorismate. A number of secondary metabolites derived from all three aromatic amino acids (Phe, Trp and Tyr) are altered in the transgenic plants, implying regulatory cross-interactions between the flux of aromatic amino acid biosynthesis from chorismate and their further metabolism into various secondary metabolites. Truncated PheA expression has a minimal effect on primary metabolism and on the Arabidopsis transcriptome. A high proportion of the feedback-insensitive chorismate mutase/prephenate dehydratase polypeptide produced by this transgene is translocated into the plastids
physiological function
-
CM0819 significantly stimulates 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (DS2098) activity, CM0819 interacts with 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase DS2098 from Corynebacterium glutamicum and this interaction results in allosteric regulation of DS2098 synthase activity
physiological function
D2CSU4, D2CSU5, -
isoform CM1 is the principal chorismate mutase responsible for the coupling of metabolites from the shikimate pathway to the synthesis of floral volatile benzenoid/phenylpropanoids in the corolla
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
carbachorismate
carbaprephenate
show the reaction diagram
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
P19080
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
P0A9J8
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
P32178
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-, Q9Y7B2
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-, Q9P4D8
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
O07746
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
O07746
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
Claviceps sp., Claviceps paspali
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
Penicillium duponti
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
Anthophyta, Selaginella sp., Nephrolysis sp., Pinus sp., Dactylis glomerata
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
Q84FH6, -
-
-
?
Chorismate
Prephenate
show the reaction diagram
P19080
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
A0QU81, -
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
P64767
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
Q7CHH5, -
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
B6C761, -
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
B6C761
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
D2CSU4, D2CSU5, -
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-, Q3LUD9, Q3LUE0
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
F2W4Z4
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
F2W4Z1
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
(-)-chorismate. No activity with (+)-chorismate
-
-
Chorismate
Prephenate
show the reaction diagram
-
reversible only in presence of P-protein
-
r
Chorismate
Prephenate
show the reaction diagram
P19080
biosynthesis of aromatic amino acids
-
?
Chorismate
Prephenate
show the reaction diagram
-
biosynthesis of aromatic amino acids
-
?
Chorismate
Prephenate
show the reaction diagram
-
biosynthesis of aromatic amino acids
-
?
Chorismate
Prephenate
show the reaction diagram
P0A9J8
biosynthesis of aromatic amino acids
-
?
Chorismate
Prephenate
show the reaction diagram
P32178
biosynthesis of aromatic amino acids
-
?
Chorismate
Prephenate
show the reaction diagram
-, Q9P4D8
biosynthesis of aromatic amino acids
-
?
Chorismate
Prephenate
show the reaction diagram
-
biosynthesis of aromatic amino acids
-
?
Chorismate
Prephenate
show the reaction diagram
Q84FH6, -
biosynthesis of aromatic amino acids
-
?
Chorismate
Prephenate
show the reaction diagram
-
enzyme of the first branch point of aromatic amino acid biosynthesis
-
?
Chorismate
Prephenate
show the reaction diagram
Q9Y7B2
enzyme of the first branch point of aromatic amino acid biosynthesis
-
?
Chorismate
Prephenate
show the reaction diagram
-
first committed step in the biosynthesis of the aromatic amino acids tyrosine and phenylalanine in bacteria, fungi and higher plants
-
?
Chorismate
Prephenate
show the reaction diagram
-
phenylalanine biosynthesis
-
r
Chorismate
Prephenate
show the reaction diagram
-
shikimate pathway in bacteria, fungi and higher plants that leads to tyrosine and phenylalanine
-
?
Chorismate
Prephenate
show the reaction diagram
P64767
the enzyme catalyzes the Claisen rearrangement of chorismate to prephenate
-
-
?
Chorismate
Prephenate
show the reaction diagram
Escherichia coli JFM-30
-
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
Bacillus subtilis 23
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
Escherichia coli JM101
-
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
Escherichia coli K12
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
Escherichia coli K12
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
Escherichia coli K12
-
(-)-chorismate. No activity with (+)-chorismate
-
-
Chorismate
Prephenate
show the reaction diagram
Escherichia coli K12
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
Escherichia coli K12
-
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
Streptomyces aureofaciens tue 24
-
-
-
-
Chorismate
Prephenate
show the reaction diagram
Streptomyces aureofaciens tue 24
-
(-)-chorismate. No activity with (+)-chorismate
-
-
Chorismate
Prephenate
show the reaction diagram
Claviceps sp. SD 58
-
-
-
-
Chorismate
?
show the reaction diagram
-
-
-
-
-
Chorismate
?
show the reaction diagram
-
-
-
-
-
Chorismate
?
show the reaction diagram
-
the first enzyme of the terminal biosynthetic pathway of Phe and Tyr
-
-
-
Chorismate
?
show the reaction diagram
-
catalyzes the first step in the branch of the shikimate pathway which leads to the aromatic amino acids, Phe and Tyr
-
-
-
Chorismate
?
show the reaction diagram
-
the existence of a cytosolic isoenzyme in addition to the plastidic isoenzyme implies that either a cytosolic pathway, partial or complete, for the biosynthesis of Phe and Tyr exists, or that prephenate, originating from chorismate in the cytosol, is utilized for the synthesis of metabolites other than these two aromatic amino acids
-
-
-
Chorismate
?
show the reaction diagram
-
in the biosynthesis of Phe and Tyr, there are two enzymes or enzyme complexes metabolizing chorismate, one leading through prephenate to phenylpyruvate and the other leading through prephenate to 4-hydroxyphenylpyruvate
-
-
-
Chorismate
?
show the reaction diagram
-
plastidic isoenzyme is elicitor-inducible and pathogen-inducible
-
-
-
Chorismate
?
show the reaction diagram
Escherichia coli K12
-
-
-
-
-
additional information
?
-
A0QU81, -
It is possible that an extracellular biosynthetic pathway from chorismate to phenylalanine exists in Mycobacterium smegmatis, even if the function of such putative route is presently obscure
-
-
-
additional information
?
-
-
The enzymatic reaction is considered to proceed via a pericyclic transition state
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Chorismate
Prephenate
show the reaction diagram
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
O07746
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
O07746
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
P19080
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
A0QU81, -
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
-
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
P19080
biosynthesis of aromatic amino acids
-
?
Chorismate
Prephenate
show the reaction diagram
-
biosynthesis of aromatic amino acids
-
?
Chorismate
Prephenate
show the reaction diagram
-
biosynthesis of aromatic amino acids
-
?
Chorismate
Prephenate
show the reaction diagram
P0A9J8
biosynthesis of aromatic amino acids
-
?
Chorismate
Prephenate
show the reaction diagram
P32178
biosynthesis of aromatic amino acids
-
?
Chorismate
Prephenate
show the reaction diagram
-, Q9P4D8
biosynthesis of aromatic amino acids
-
?
Chorismate
Prephenate
show the reaction diagram
-
biosynthesis of aromatic amino acids
-
?
Chorismate
Prephenate
show the reaction diagram
Q84FH6, -
biosynthesis of aromatic amino acids
-
?
Chorismate
Prephenate
show the reaction diagram
-
enzyme of the first branch point of aromatic amino acid biosynthesis
-
?
Chorismate
Prephenate
show the reaction diagram
Q9Y7B2
enzyme of the first branch point of aromatic amino acid biosynthesis
-
?
Chorismate
Prephenate
show the reaction diagram
-
first committed step in the biosynthesis of the aromatic amino acids tyrosine and phenylalanine in bacteria, fungi and higher plants
-
?
Chorismate
Prephenate
show the reaction diagram
-
phenylalanine biosynthesis
-
r
Chorismate
Prephenate
show the reaction diagram
-
shikimate pathway in bacteria, fungi and higher plants that leads to tyrosine and phenylalanine
-
?
Chorismate
?
show the reaction diagram
-
-
-
-
-
Chorismate
?
show the reaction diagram
-
-
-
-
-
Chorismate
?
show the reaction diagram
-
the first enzyme of the terminal biosynthetic pathway of Phe and Tyr
-
-
-
Chorismate
?
show the reaction diagram
-
catalyzes the first step in the branch of the shikimate pathway which leads to the aromatic amino acids, Phe and Tyr
-
-
-
Chorismate
?
show the reaction diagram
-
the existence of a cytosolic isoenzyme in addition to the plastidic isoenzyme implies that either a cytosolic pathway, partial or complete, for the biosynthesis of Phe and Tyr exists, or that prephenate, originating from chorismate in the cytosol, is utilized for the synthesis of metabolites other than these two aromatic amino acids
-
-
-
Chorismate
?
show the reaction diagram
-
in the biosynthesis of Phe and Tyr, there are two enzymes or enzyme complexes metabolizing chorismate, one leading through prephenate to phenylpyruvate and the other leading through prephenate to 4-hydroxyphenylpyruvate
-
-
-
Chorismate
?
show the reaction diagram
-
plastidic isoenzyme is elicitor-inducible and pathogen-inducible
-
-
-
Chorismate
Prephenate
show the reaction diagram
Escherichia coli JFM-30
-
-
-
-
?
Chorismate
?
show the reaction diagram
Escherichia coli K12
-
-
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD+
-
enhances activity
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
Mg2+ at concentrations of 0.1-2 mM does not affect CM0819 activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(1R,2S,3S,5S,7S)-10-hydroxy-3-oxo-2-oxa-5-azatricyclo[4.3.1.1(4,8)]undecane-8-carboxylate, sodium salt
-
does not display tighter binding to the enzyme than the native substrate chorismate or greater inhibitory action than the ether analogue
-
(1R,3R,5S)-3-carboxy-1-hydroxy-2-oxabicyclo[3.3.1]non-6-ene-5-carboxylate
-
-
(1R,3R,5S,8R)-2-azatricyclo[3.3.1.0(1,8)]-non-6-ene-3,5-dicarboxylate, disodium salt
-
exo arizidine analogue, no time-dependent loss of activity is observed in the presence of this potentially reactive aza inhibitor
-
(1R,3R,5S,8S)-8-hydroxy-2-azabicyclo[3.3.1]non-6-ene-3,5-dicarboxylate, disodium salt
-
does not display tighter binding to the enzyme than the native substrate chorismate or greater inhibitory action than the ether analogue
-
(1R,3S,5S,8S)-8-hydroxy-2-azabicyclo[3.3.1]non-6-ene-3,5-dicarboxylate, disodium salt
-
does not display tighter binding to the enzyme than the native substrate chorismate or greater inhibitory action than the ether analogue
-
(1S,3R,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
-
(1S,3S,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
-
(1S,3S,5R,6R)-6-hydroxy-4-oxabicyclo[3.3.1]non-7-ene-1,3-dicarboxylate
-
endo-oxabicyclic dicarboxylic acid is a good geometric mimic of transition state
(1S,4S,6R,8S,10S)-3-oxo-5-aza-2-oxa-tetracyclo[4.3.1.(4,8).0(6,10)]undecane-8-carboxylate, sodium salt
-
tetracyclic lactone, no time-dependent loss of activity is observed in the presence of this potentially reactive aza inhibitor
-
(2E)-8-exo-3-Hydroximino-8-hydroxy-2-oxabicyclo-[3.3.1]non-6-ene-5-carboxylic acid
-
poor
(2Z)-2-(4-chlorophenyl)-3-(4,5-dimethoxy-2-nitrophenyl)prop-2-enoic acid
-
-
(3R,6Z)-8-hydroxy-2-azabicyclo[3.3.3]undec-6-ene-3,5-dicarboxylic acid
-
-
(3S,6Z)-8-hydroxy-2-azabicyclo[3.3.3]undec-6-ene-3,5-dicarboxylic acid
-
-
(3S,6Z)-8-hydroxy-2-oxabicyclo[3.3.3]undec-6-ene-3,5-dicarboxylic acid
-
-
1-Substituted adamantane derivatives
-
order of decreasing inhibitory activity with the various substituents: -PO32-, -P(OCH3)O2, CO2-, -CH2CO2-, -SO2-,Y -SO3-
2-(1-Carboxy-1,4-dihydrobenzyl)acrylic acid
-
-
3-Chloroadamantane-1-acetic acid
-
-
3-endo,6-exo-6-Hydroxy-7-bicyclo[3.3.1]-nonene-1,3-dicarboxylic acid
-
poor
3-endo,8-exo-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid
-
potent
4-Methyl-DL-Trp
-
enzyme form CM1 is inhibited, enzyme form CM2 not
4-[[2-(3,4-dimethoxyphenyl)ethyl]amino]-3-nitro-5-sulfamoylbenzoic acid
-
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
6-Methyl-DL-Trp
-
enzyme form CM1 is inhibited, enzyme form CM2 not
8-exo-8-Hydroxy-2-oxabicyclo[3.3.1]nona-3,6-diene-3,5-dicarboxylic acid
-
slight
8-hydroxy-2-oxa-bicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid
-
competitive inhibition
-
Adamantane-1-acetic acid
-
-
adamantane-1-phosphonate
-
no inhibitory effect up to concentrations of 0.1 and 1 mM
caffeic acid
-
enzyme forms CM1 and CM2 are inhibited, enzyme form CM3 is unaffected
caffeic acid
-
enzyme form CM1 is inhibited
caffeic acid
Penicillium duponti
-
enzyme form CM1 is inhibited; enzyme form CM2 is inhibited
chlorogenic acid
-
enzyme forms CM1 and CM2 are inhibited, enzyme form CM3 is unaffected
chorismate
-
strain WB672, inhibition above 2 mM
chorismate
-, Q9Y7B2
-
Co2+
-
2 mM Co2+ decreases CM0819 activity by 52.4%
Cu2+
-
strong
DL-3-fluoro-Phe
-
enzyme form CM1 is inhibited, enzyme form CM2 not
DL-5-Fluoro-Trp
-
enzyme form CM1 is inhibited, enzyme form CM2 not
DL-5-hydroxy-Trp
-
enzyme form CM1 is inhibited, enzyme form CM2 not
endo-Oxabicylic transition state analogue inhibitor
-
-
-
Fe2+
-
-
-
ferulic acid
-
inhibits enzyme form CM3
iodoacetamide
-
-
L-Phe
-
55000 MW enzyme form. The 59000 MW enzyme form is not inhibited
L-Phe
Claviceps sp.
-
-
L-Phe
-
chorismate mutase P is strongly inhibited, chorismate mutase T is not inhibited
L-Phe
-
no inhibition
L-Phe
-
enzyme form CM1 and CM3 are inhibited
L-Phe
-
enzyme form CM1 is inhibited
L-Phe
-
enzyme form CM1 is inhibited; enzyme form CM3 is inhibited
L-Phe
Penicillium duponti
-
enzyme form CM1 is inhibited; enzyme form CM2 is not inhibited; enzyme form CM3 is inhibited
L-Phe
-
Trp reverses inhibition
L-Phe
-
enzyme form CM1 is inhibited; enzyme form CM2 is not inhibited
L-Phe
-
plastidic isoenzyme is inhibited, cytosolic enzyme not
L-Phe
-
enzyme form CM1 is inhibited; Trp reverses inhibition
L-Phe
-
poor noncompetitive
L-Phe
-
28% residual activity at 0.2 mM
L-Trp
-
96% residual activity at 0.2 mM
L-tryptophan
-
allosteric inhibitor
L-tryptophan
-
allosteric. The Trp at the dimer interface interacts extensively with residues from both subunits. The unexpected gene duplication possibly leads to a different allosteric regulation mechanism than that is known for other CMs
L-Tyr
-
55000 MW enzyme form. The 59000 MW enzyme form is not inhibited
L-Tyr
Claviceps sp.
-
-
L-Tyr
-
slight inhibition of chorismate mutase P and no inhibition of chorismate mutase T
L-Tyr
-
enzyme forms CM1 and CM3 are inhibited
L-Tyr
-
enzyme form CM1 is inhibited
L-Tyr
-
enzyme form CM1 is inhibited; enzyme form CM3 is inhibited
L-Tyr
Penicillium duponti
-
enzyme form CM1 is inhibited; enzyme form CM2 is not inhibited; enzyme form CM3 is inhibited
L-Tyr
-
1.25 mM, 85% inhibition; Trp reverses inhibition
L-Tyr
-
enzyme form CM2 is not inhibited
L-Tyr
-
no inhibition
L-Tyr
-
no inhibition
L-Tyr
-
plastidic isoenzyme is inhibited, cytosolic enzyme not
L-Tyr
-
enzyme form CM1 is inhibited; enzyme form CM2 is not inhibited; Trp reverses inhibition
L-Tyr
-
wild-type enzyme is inhibited. Mutant enzymes with amino acid exchange at Thr234, especially Tyr234Phe, mutant enzyme Ile225Thr and Ile225Thr/Thr226Ile are insensitive
L-Tyr
-
63% residual activity at 0.2 mM
methyl 4-(methylamino)-3-nitrobenzoate
-
-
N-[[3-(tert-butoxycarbonyl)-2-phenyl-1,3-thiazolidin-4-yl]carbonyl]leucine
-
-
NaCl
-
inhibition is cooperative, NaCl also increases the sensitivity of the enzyme to inhibition by Phe
Ni2+
-
2 mM Ni2+ decreases CM0819 activity by 41.8%
oxabicyclic dicarboxylic acid
-
transition state analogon, competitive inhibition
p-coumaric acid
-
inhibits enzyme form CM1, CM2 and CM3
prephenate
-
competitive
prephenate
-
competitive
prephenate
-
competitive inhibition
Transition state analogue inhibitor
-
-
-
tyrosine
Q84FH6
competitive inhibition, 0.5 M tyrosine leads to 40% inhibition
tyrosine
-, Q9P4D8
heterotrophic feedback inhibitor
tyrosine
-
heterotrophic feedback inhibitor
tyrosine
-, Q9Y7B2
0.05 mM, heterotrophic feedback-inhibitor
Zn2+
-
strong
Mn2+
-
2 mM Mn2+ decreases CM0819 activity by 38.9%
additional information
-
the enzyme is greatly inhibited at acidic pH. L-phenylalanine, L-tyrosine, and L-tryptophan moderately enhance activity at low concentrations, but they inhibit the enzyme at higher concentrations
-
additional information
-
Unlike the other known prokaryotic CMs, the Mycobacterium tuberculosis enzyme exhibits allosteric regulation by aromatic amino acids, a feature limited to the eukaryotic CMs. The active site of MtbCM is seen to be blocked due to the presence of a sulfate ion in the structure. It therefore appears that sulphate acts as an inhibitor of the enzyme by blocking the entry of the substrate into the active site. In MtbCM the allosteric site is close to the active site
-
additional information
-
aza inhibitors. Competitive inhibition, Saccharomyces cerevisiae chorismate mutase inhibitors and the substrate chorismic acid used for pharmacophore model generation. These inhibitors do not alter Vmax at the higher concentration of substrate (1-5 mM)
-
additional information
-
*MtCM is not regulated by the aromatic amino acids. The x-ray structure of *MtCM does not have an allosteric regulatory site in the protein
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3,4-dimethoxycinnamic acid
-
activates enzyme form CM3
3,4-dimethoxycinnamic acid
-
enzyme form CM1 is unaffected
3,4-dimethoxycinnamic acid
Penicillium duponti
-
activates enzyme form CM3; enzyme form CM1 is unaffected; enzyme form CM2 is unaffected
3-deoxy-D-arabino-heptulosonate-7-phosphate synthase
P64767
-
-
3-deoxy-D-arabino-heptulosonate-7-phosphate synthase
-
the catalytic efficiency of chorismate mutase increases 140fold on addition of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase, chorismate mutase forms a complex with 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase and that complex formation both increases the CM activity by more than two orders of magnitude and endows chorismate mutase with regulatory features
-
arabinose
B6C761, -
expression can be induced by arabinose under the control of the araBAD promoter
caffeic acid
Penicillium chrysogenum, Penicillium duponti
-
enzyme form CM3 is activated
L-Trp
Claviceps paspali, Claviceps sp.
-
activates
L-Trp
-
activates enzyme forms CM1 and CM3
L-Trp
-
activates; enzyme form CM1 is activated
L-Trp
-
enzyme form CM1 is activated; enzyme form CM3 is activated
L-Trp
Penicillium duponti
-
enzyme form CM1 is activated; enzyme form CM2 is unaffected; enzyme form CM3 is activated
L-Trp
-
activates; enzyme form CM2 is unaffected
L-Trp
-
plastidic isoenzyme is activated, cytosolic isoenzyme is inactive
L-Trp
-
enzyme form CM1 is activated; enzyme form CM2 is unaffected
tryptophan
-, Q9P4D8
heterotrophic positive effector
tryptophan
-
heterotrophic positive effector
tryptophan
-, Q9Y7B2
0.005 mM, heterotrophic activator
L-Trp
-
wild-type enzyme, mutant enzyme Ile225Thr/Thr226Ile and enzymes with mutations at Tyr234 are activated. No activation of mutant enzyme Thr226Ile
additional information
-
Most essential residue in BsCM is Arg90, the lack of Arg90 leads to a charge loss of catalytic activity. Two important catalytic roles of Arg90: one is to control the relative stability of the substrate through the collective hydrogen-bonding network in the Glu78-Arg90-substrate, and the other is to polarize the substrate at the appropriate location on the reaction path to gain the maximum electrostatic stabilisation factor for TSS
-
additional information
-
neither pH variation between 5.9 and 8.7, nor provision of 0.1 mg/ml bovine serum albumin, 2 mM Ca2+, 10 mM Mg2+, 1 mM EDTA, 1 mM EGTA, 1 mM 1,10-phenanthroline, 1 mM L-phenylalanine, 1 mM L-tyrosine, 1 mM L-tryptophan, or 0.6 mM salicylate affect catalytic activity by more than a factor of 2
-
additional information
-
the CM0819 activity is not affected by L-Phe, L-Tyr or L-Trp (0.01-10 mM), EDTA at concentrations of 0.1-2 mM does not affect CM0819 activity
-
additional information
D2CSU4, D2CSU5, -
CM1 is allosterically regulated by L-tryptophan but not L-phenylalanine or L-tyrosine; CM2 is not allosterically regulated by L-tryptophan, L-phenylalanine, or L-tyrosine
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.03
-
chorismate
-
mutant enzyme V35A, in PBS buffer (pH 7.5) at 20C
0.04
-
chorismate
-
in presence of NAD+
0.041
-
chorismate
-
30C, pH 7.2, mutant H347N
0.041
-
chorismate
-
30C
0.045
-
chorismate
-
in presence of Trp
0.045
-
chorismate
-
30C, pH 7.2, wild-type
0.051
-
chorismate
-
30C, pH 7.2, mutant H153N
0.053
-
chorismate
-
30C, pH 7.2, mutant H131A
0.054
-
chorismate
-
wild type enzyme, in PBS buffer (pH 7.5) at 20C
0.059
-
chorismate
-
mutant enzyme D48G, in PBS buffer (pH 7.5) at 20C
0.067
-
chorismate
-
30C, pH 7, wild-type
0.068
-
chorismate
-
30C, pH 7.2, mutant H197N
0.073
-
chorismate
-
mutant enzyme F77W, in PBS buffer (pH 7.5) at 20C
0.074
-
chorismate
-
wild-type
0.081
-
chorismate
-
30C, pH 7.5, wild-type, with 4 mM substrate
0.092
-
chorismate
-
pH 7.5, in absence of NAD+
0.098
-
chorismate
-
30C, pH 7.2, mutant H257A
0.099
-
chorismate
-
30C, pH 7.2, mutant H265A
0.1
-
chorismate
-
-
0.126
-
chorismate
-
30C, pH 7.2, mutant H239N
0.15
-
chorismate
-
30C, pH 7, mutant R90G
0.15
-
chorismate
-
leaderless MtCM with C-terminal His tag, at 30C and pH 7.5
0.18
-
chorismate
-
untagged enzyme, at 30C and pH 7.5
0.185
-
chorismate
-
in absence of Trp
0.22
-
chorismate
-
mutant A32S
0.225
-
chorismate
-
30C, pH 7.2, mutant H245N
0.226
-
chorismate
-
37C, pH 7.8, in presence of P-protein
0.24
-
chorismate
-
enzyme form CM2
0.249
-
chorismate
-
mutant L7I
0.29
-
chorismate
-
genetically engineered monofunctional chorismate mutase that contains only 109 amino acids
0.29
-
chorismate
Q84FH6
70C, pH 7.6
0.296
-
chorismate
-
37C, pH 7.8
0.3
-
chorismate
-
wild-type enzyme
0.304
-
chorismate
-
wild type
0.365
-
chorismate
-
mutant V35I
0.38
-
chorismate
-
-
0.39
-
chorismate
-
chorismate mutase domain of P-protein
0.4
-
chorismate
-
chorismate, mutant enzyme Thr226Ile, activated by 0.01 mM Trp; wild-type enzyme, activated by 0.01 mM Trp
0.45
-
chorismate
-
mutant enzyme Lys39Asn
0.46
-
chorismate
-
-
0.5
-
chorismate
-
enzyme form CM2
0.5
-
chorismate
Q7CHH5, -
at 37C and pH 7.5
0.53
-
chorismate
-
-
0.55
-
chorismate
-
-
0.57
-
chorismate
-
mutant enzyme G86A
0.59
1
chorismate
-
37C, pH 7.8, DELTA102-285 in presence of 2 mM phenylalanine
0.59
-
chorismate
-
mutant enzyme Lys39Arg
0.628
-
chorismate
-
37C, pH 7.8, DELTA102-285 in presence of 0.5 mM phenylalanine
0.669
-
chorismate
-
mutant I81L/V85I
0.7
-
chorismate
-
mutant enzyme Tyr234Phe, activated by 0.01 mM Trp
0.8
-
chorismate
-
mutant enzyme Tyr234Ala, activated by 0.01 mM Trp
1
-
chorismate
-
strain WB672
1.036
-
chorismate
-
37C, pH 7.8, DELTA102-285 in presence of 0.05 mM phenylalanine
1.1
-
chorismate
-
enzyme CM1
1.14
-
chorismate
-
wild type enzyme
1.16
-
chorismate
-
mutant enzyme Lys39Gln
1.2
-
chorismate
-
mutant enzyme Q88N, in PBS buffer (pH 7.5) at 20C
1.3
-
chorismate
-
mutant enzyme Tyr234Ser, activated by 0.01 mM Trp
1.3
-
chorismate
-
mutant enzyme R51Q, in PBS buffer (pH 7.5) at 20C
1.5
-
chorismate
-
mutant enzyme Ile225Thr/Thr226Ile, activated by 0.01 mM Trp
1.5
-
chorismate
-
at 37C and pH 7.5
1.6
-
chorismate
-
mutant enzyme Glu23Asp, activated by 0.01 mM Trp
1.6
-
chorismate
-, Q9P4D8
37C, in presence of 0.01 mM tryptophan
1.7
-
chorismate
-
enzyme form CM1, weak positive cooperativity
1.9
-
chorismate
-
30C, pH 7, mutant C88K/R90S
2.547
-
chorismate
-
37C, pH 7.8, DELTA102-285
2.6
-
chorismate
-
strain 168
2.83
-
chorismate
-
at 37C
3.9
-
chorismate
-
30C, pH 7.5, mutant DELTA118-127, with 5.8 mM substrate
4
-
chorismate
-
30C, pH 7.5, mutant DELTA119-127/D118N, with 5.8 mM substrate
4.1
-
chorismate
-
30C, pH 7.5, mutant DELTA118-127, with 3.4 mM substrate
4.3
-
chorismate
-
30C, pH 7, mutant C88S/R90K
5.2
-
chorismate
-
mutant enzyme Glu23Ala, activated by 0.01 mM Trp
6
-
chorismate
-
mutant enzyme Glu23Gln, activated by 0.01 mM Trp
6.3
-
chorismate
-
mutant enzyme Tyr234Glu, activated by 0.01 mM Trp
9.3
-
chorismate
-
30C, pH 7.5, mutant DELTA117-127, with 3.8 mM substrate
9.6
-
chorismate
-
DELTA 117-127
15
-
chorismate
-
30C, pH 7.5, mutant DELTA118-127/K111N/A112S/V113N, with 4 mM substrate
0.47
1
prephenate
-
-
0.549
-
prephenate
-
37C, pH 7.8, in presence of P-protein
16
-
chorismate
-
30C, pH 7.5, mutant DELTA118-127/R116L/P117T, with 3.9 mM substrate
additional information
-
Chorismic acid
-
Competetive inhibition by I IV Structur: increase the Km
additional information
-
additional information
-
when the pH increases from pH 6.2 to pH 8.6 the Km-values for prephenate and chorismate increase substantially
-
additional information
-
additional information
-, Q9P4D8
sigmoid substrate saturation curve with S0.5: 16.7 mM for chorismate at 37C and S0.5: 12 mM for chorismate at 37C in presence of 0.1 mM tyrosine
-
additional information
-
additional information
-
The Km of the active complementations (position 7, 32, 35, 48, 81 and 85) is shown
-
additional information
-
additional information
-
A lower Km of 0.5 +/-0.05 mM is obtained with a 27.5 nM protein concentration (11 pmol) whereas a Km of 0.67 +/-0.05 nM is obtained with a 8 nM protein concentration (3.2 pmol)
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0003
-
chorismate
-
30C, pH 7, mutant R90G
0.00983
-
chorismate
-
mutant enzyme Lys39Arg
0.042
-
chorismate
-
mutant enzyme Q88N, in PBS buffer (pH 7.5) at 20C
0.0492
-
chorismate
-
mutant enzyme Lys39Asn
0.11
-
chorismate
-
mutant enzyme G86A
0.123
-
chorismate
-
mutant enzyme Lys39Arg
0.29
-
chorismate
-
30C, pH 7, mutant C88S/R90K
0.32
-
chorismate
-
30C, pH 7, mutant C88K/R90S
0.41
-
chorismate
-
mutant enzyme F77W, in PBS buffer (pH 7.5) at 20C
0.5
-
chorismate
-
mutant enzyme V35A, in PBS buffer (pH 7.5) at 20C
1.05
-
chorismate
-
at 37C
1.3
-
chorismate
-
mutant enzyme D48G, in PBS buffer (pH 7.5) at 20C
2
8
chorismate
-
mutant DELTA117-127
2
-
chorismate
-
wild type enzyme
2.3
-
chorismate
-
30C, pH 7.2, mutant H239N
2.6
-
chorismate
-
mutant enzyme R51Q, in PBS buffer (pH 7.5) at 20C
3
-
chorismate
-
wild type enzyme, in PBS buffer (pH 7.5) at 20C
4.8
-
chorismate
-
30C, pH 7.2, mutant H245N
5.5
-
chorismate
-
at 37C and pH 7.5
6
-
chorismate
-
30C, pH 7.2, mutant H347N
7.2
-
chorismate
-
30C, pH 7.2, mutant H131A
8
-
chorismate
-
30C, pH 7.2, mutant H257A
10
-
chorismate
-
30C, pH 7.2, mutant H153N
14
-
chorismate
-
mutant enzyme Glu23Ala, activated by 0.01 mM Trp
15
-
chorismate
-
30C, pH 7.2, mutant H265A
16
-
chorismate
-
30C, pH 7.2, mutant H197N
22
-
chorismate
-
30C, pH 7.5, mutant DELTA118-127, with 5.8 mM substrate
23
-
chorismate
-
30C, pH 7.5, mutant DELTA119-127/D118N, with 5.8 mM substrate
23.8
-
chorismate
-, Q9P4D8
37C, in presence of 0.1 mM tyrosine
24
-
chorismate
-
30C, pH 7.5, mutant DELTA118-127, with 3.4 mM substrate
26
-
chorismate
-
30C, pH 7.5, mutant DELTA117-127, with 3.8 mM substrate and DELTA 118-127/R116L/P117T, with 3.9 mM substrate
27
-
chorismate
-
30C, pH 7.2, wild-type
30
-
chorismate
-
30C, pH 7.5, mutant DELTA118-127/K111N/A112S/V113N, with 4 mM substrate
33.4
-
chorismate
-
mutant I81L/V85I
36.55
-
chorismate
-
mutant L7I
38.87
-
chorismate
-
wild type
39
-
chorismate
-
wild-type enzyme
40.7
-
chorismate
-
genetically engineered enzyme containg the amino acid residues 1-300
41
-
chorismate
-
wild-type
41.4
-
chorismate
-
wild-type enzyme
44
-
chorismate
-
mutant enzyme Tyr234Glu, activated by 0.01 mM Trp
44.3
-
chorismate
-
genetically engineered enzyme containg the amino acid residues 1-285
45.13
-
chorismate
-
mutant A32S
46
-
chorismate
-
30C, pH 7, wild-type
47
-
chorismate
-
30C, pH 7.5, wild-type, with 4 mM substrate
50
-
chorismate
-
-
50
-
chorismate
-
untagged enzyme, at 30C and pH 7.5
50.77
-
chorismate
-
mutant V35I
52
-
chorismate
Q84FH6
70C, pH 7.6
56
-
chorismate
-
leaderless MtCM with C-terminal His tag, at 30C and pH 7.5
64
-
chorismate
-
chorismate mutase domain of P-protein
70
-
chorismate
Q7CHH5, -
at 37C and pH 7.5
74
-
chorismate
-
mutant enzyme Tyr234Ser, activated by 0.01 mM Trp
82
-
chorismate
-, Q9Y7B2
30C, pH 7.6
89.3
-
chorismate
-, Q9P4D8
37C, in presence of 0.1 mM tyrosine
92
-
chorismate
-, Q9Y7B2
30C, pH 7.6, in presence of 0.005 mM tryptophan
171
-
chorismate
-
mutant enzyme Glu23Gln, activated by 0.01 mM Trp
252
-
chorismate
-
mutant enzyme Tyr234Ala, activated by 0.01 mM Trp
351
-
chorismate
-
mutant enzyme Thr226Ile, activated by 0.01 mM Trp
361
-
chorismate
-
wild-type enzyme, activated by 0.01 mM Trp
367
-
chorismate
-, Q9P4D8
37C
535
-
chorismate
-
mutant enzyme Ile225Thr/Thr226Ile, activated by 0.01 mM Trp
565
-
chorismate
-
mutant enzyme Tyr234Phe, activated by 0.01 mM Trp
625
-
chorismate
-
mutant enzyme Glu23Asp, activated by 0.01 mM Trp
140500
-
chorismate
-
37C, pH 7.8, in presence of P-protein
141000
-
chorismate
-
37C, pH 7.8, in presence of P-protein
148900
-
chorismate
-
37C, pH 7.8, chorismate mutase
149000
-
chorismate
-
37C, pH 7.8, chorismate mutase
234000
-
chorismate
-
37C, pH 7.8, DELTA102-285 in presence of 0.05 mM phenylalanine
234100
-
chorismate
-
37C, pH 7.8, DELTA102-285 in presence of 0.05 mM phenylalanine
253000
-
chorismate
-
37C, pH 7.8, DELTA102-285 in presence of 0.5 mM phenylalanine
253400
-
chorismate
-
37C, pH 7.8, DELTA102-285 in presence of 0.5 mM phenylalanine
257900
-
chorismate
-
37C, pH 7.8, DELTA102-285 in presence of 2 mM phenylalanine
258000
-
chorismate
-
37C, pH 7.8, DELTA102-285 in presence of 2 mM phenylalanine
365600
-
chorismate
-
37C, pH 7.8, DELTA102-285
94100
-
prephenate
-
37C, pH 7.8, in presence of P-protein
94140
-
prephenate
-
37C, pH 7.8, in presence of P-protein
additional information
-
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
-
turnover of mutant H189N enzyme is lower than 0.0025 per second
366000
-
chorismate
-
37C, pH 7.8, DELTA102-285
additional information
-
additional information
-
The kcat of the active complementations (position 7, 32, 35, 48, 81 and 85) is shown
-
additional information
-
additional information
-
CM spezific activity in Escherichia coli extracts: Control (M. Tuberculosis) Sp act (U/mg) 0.889 Cloned extract/control 1 AroQMt (Rv0948c) Sp act (U/mg) 127.38 Cloned extract/control 143.28 *AroQMt (Rv1885c) Sp act (U/mg) 94.23 Cloned extract/control 105.9. CM specific activity in Escherichia coli cells expressing either the AroQMt or the *AroQMt protein is determined to be, repectively, 143- and 106-fold higher than the enzyme activity obtained for Escherichia coli cells carrying the pET-23a(+) expression vector
-
additional information
-
additional information
-
R90Cit 10E4-fold decrease in the catalytic activity of kcat. R90K 10E4-fold decrease in the catalytic activity of kcat/Km is obtained
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.19
-
chorismate
-
mutant enzyme G86A
8588
1.75
-
chorismate
-
wild type enzyme
8588
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.001
-
(1R,3R,5S)-3-carboxy-1-hydroxy-2-oxabicyclo[3.3.1]non-6-ene-5-carboxylate
-
30C, pH 7.5, wild-type
0.0023
-
(1R,3R,5S)-3-carboxy-1-hydroxy-2-oxabicyclo[3.3.1]non-6-ene-5-carboxylate
-
30C, pH 7.5, chorismate mutase domain of P-protein
0.051
-
(1R,3R,5S)-3-carboxy-1-hydroxy-2-oxabicyclo[3.3.1]non-6-ene-5-carboxylate
-
30C, pH 7.5, mutant DELTA117-127
0.00032
-
(1S,3R,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
30C, pH 7.5, wild-type
0.0029
-
(1S,3R,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
30C, pH 7.5, mutant DELTA117-127
0.0076
-
(1S,3R,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
30C, pH 7.5, chorismate mutase domain of P-protein
0.23
-
(1S,3S,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
30C, pH 7.5, wild-type
0.01771
-
(2Z)-2-(4-chlorophenyl)-3-(4,5-dimethoxy-2-nitrophenyl)prop-2-enoic acid
-
-
0.0057
-
4-[[2-(3,4-dimethoxyphenyl)ethyl]amino]-3-nitro-5-sulfamoylbenzoic acid
-
4-[[2-(3,4-dimethoxyphenyl)ethyl]amino]-3-nitro-5-sulfamoylbenzoic acid shows the most potent inhibition with Ki value of 0.0057 mM against MtCM
-
0.0037
-
8-hydroxy-2-oxa-bicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid
-
-
-
0.0028
-
chorismate
-, Q9Y7B2
30C, pH 7.6, in presence of 0.005 mM tyrosine
0.0288
-
methyl 4-(methylamino)-3-nitrobenzoate
-
-
0.003
-
oxabicyclic dicarboxylic acid
-
30C, pH 7, wild-type
0.004
-
oxabicyclic dicarboxylic acid
-
30C, pH 7, mutant R90G
1.1
-
oxabicyclic dicarboxylic acid
-
30C, pH 7, mutant C88K/R90S
0.07
-
prephenate
-
dimeric chorismate mutase, at 20C
0.17
-
prephenate
-
monomeric chorismate mutase, at 20C
0.034
-
tyrosine
Q84FH6
70C, pH 7.6
0.0211
-
N-[[3-(tert-butoxycarbonyl)-2-phenyl-1,3-thiazolidin-4-yl]carbonyl]leucine
-
-
additional information
-
oxabicyclic dicarboxylic acid
-
>> 1 mM mutant C88S/R90K
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.007
-
Saccharomyces cerevisiae chorismate mutase inhibitors
-
(3S,6Z)-8-hydroxy-2-oxabicyclo[3.3.3]undec-6-ene-3,5-dicarboxylic acid
-
1.2
-
Saccharomyces cerevisiae chorismate mutase inhibitors
-
(3S,6Z)-8-hydroxy-2-azabicyclo[3.3.3]undec-6-ene-3,5-dicarboxylic acid
-
18
-
Saccharomyces cerevisiae chorismate mutase inhibitors
-
(3R,6Z)-8-hydroxy-2-azabicyclo[3.3.3]undec-6-ene-3,5-dicarboxylic acid
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.44
-
-
cell-free supernatant
21.7
-
-
-
25
-
Q84FH6
after affinity chromatography
48.6
-
-
after 110.4fold purification
168
-
-, Q9P4D8
Superdex 200pg pool
210
-
-
recombinant enzyme
1200
-
-
0.1 mM tyrosine, wild-type
3300
-
-
0.1 mM tyrosine, mutant T226D
3700
-
-
unliganded, mutant T226D
4800
-
-
unliganded, wild-type
8400
-
-, Q9Y7B2
0.1 mM tyrosine, wild-type
11100
-
-
0.5 mM tryptophan, mutant T226D
13400
-
-, Q9Y7B2
0.1 mM tyrosine, mutant D233I
20600
-
-
unliganded, mutant T226I
21700
-
-
0.1 mM tyrosine, mutant T226I
22000
-
-, Q9Y7B2
0.1 mM tyrosine, mutant D233T
26400
-
-
0.5 mM tryptophan, mutant T226I
30300
-
-, Q9Y7B2
unliganded, mutant D233I
32500
-
-, Q9Y7B2
unliganded, wild-type
40200
-
-
0.5 mM tryptophan, wild-type
41300
-
-, Q9Y7B2
unliganded, mutant D233T
63000
-
-, Q9Y7B2
0.5 mM tryptophan, mutant D233I
64300
-
-, Q9Y7B2
0.5 mM tryptophan, mutant D233T
88500
-
-, Q9Y7B2
0.5 mM tryptophan, wild-type
additional information
-
-
-
additional information
-
-
Activation Energies in the enzyme reactions by AMBER and FMO calculations for wild-type and mutants are shown. These results are potential energy, not free energy
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.4
-
-, Q9Y7B2
catalytic maximum in presence of tyrosine
6
10
-
enzyme form CM1
6
10
-
enzyme form CM2
6
8
-
enzyme form CM1 and CM2
6.2
-
-
55000 MW enzyme form
6.4
-
-
low-activity strain 168
6.6
7
-
59000 MW enzyme form
6.9
-
-
-
7.1
-
-, Q9Y7B2
catalytic maximum in presence of tryptophan
7.5
9.5
-
enzyme form CM2
7.5
-
-
in presence of Trp
7.5
-
O07746
assay at
7.5
-
A0QU81, -
assay at
7.8
-
-
enzyme form CM1
8
-
-
in absence of Trp
8.9
-
-
high activity strain WB672
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
9
-
the catalytic efficiency (kcat/Km) of *MtCM increases by two orders of magnitude upon decreasing the pH from 9 to 5
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
O07746
assay at
35
37
-
enzyme form CM1
37
-
-
assay at
37
-
A0QU81, -
assay at
38
-
-
decrease in turnover at temperatures higher than 38C
48
-
-, Q9P4D8
maximum enzymatic activity
56
-
-
enzyme form CM2
70
-
-
As the temperature is lowered, distances of electrostatic and hydrophobic interactions decrease. The distance between Glu77-COOH and the hydroxyl oxygen decreases from the optimum
additional information
-
-
The average structures of the thermophilic E.S complex at three different temperatures are obtained from the MD simulations. A snapshot of the most important features of the active site of the TtCM E.S complex at 70C is shown. At this temperature the Boltzmann distribution is primarily composed of reactive conformers - near attack conformers (NACs). The effects of the different temperatures on the distances in the structure are shown. The distances between electrostatic and hydrophobic pairs decrease as temperature decreases
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
70
-
studies that elucidate the dependence of the E-S active site on temperatures 25, 60 and 70C
37
50
-
maximally active in this range
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.7
4.8
-, Q9Y7B2
isoelectric focusing, pH-gradient 3.5-9.5
4.9
-
-
calculated
7.7
-
-, Q3LUD9, Q3LUE0
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
the major fraction is formed by enzyme form CM2
Manually annotated by BRENDA team
-
esophageal gland cell
Manually annotated by BRENDA team
-
all three enzyme forms are present: CM1, CM2, and CM3
Manually annotated by BRENDA team
-
enzyme forms: CM1, CM2, and CM3
Manually annotated by BRENDA team
-
major fraction is formed by enzyme form CM1
Manually annotated by BRENDA team
-, Q3LUD9, Q3LUE0
subventral and dorsal pharyngeal glands; subventral and dorsal pharyngeal glands
Manually annotated by BRENDA team
-
all three enzyme forms are present: CM1, CM2, and CM3; green or etiolated
Manually annotated by BRENDA team
-
green or etiolated
Manually annotated by BRENDA team
-
enzyme forms are present: CM1, CM2, and CM3
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
D2CSU4, D2CSU5, -
isoform CM1 is localized to the chloroplast stroma
Manually annotated by BRENDA team
-
Mycobacterium tuberculosis enzyme has been shown to be secreted into the extracellular medium
-
Manually annotated by BRENDA team
-
MtCM is secreted out of the cell to provide support to Mycobacterium tuberculosis in aromatic amino acid deficient medium
-
Manually annotated by BRENDA team
-
absence of a discrete periplasmic compartment in Mycobacterium tuberculosis. *MtCM is secreted out of the cytoplasm and through the unusual architecture of the mycobacterial cell wall
-
Manually annotated by BRENDA team
-
-
Rv0948c, the presence of a cleavable signal peptide in Rv1885c strongly suggests that they are exported
-
Manually annotated by BRENDA team
-
chloroplasts or proplastids, enzyme form CM1
Manually annotated by BRENDA team
D2CSU4, D2CSU5, -
isoform CM1 is imported into the plastid and processed to a mature size
Manually annotated by BRENDA team
-
from mesophyll
-
Manually annotated by BRENDA team
additional information
-
Only one of the gene products is secreted into the extracellular space. This observation strongly suggests that while the cytosolic enzyme might have retained its role in the aromatic amino acid synthesis pathway, the secreted enzyme is likely to have evolved a distinct role, such as aiding the bacterium in its pathogenesis
-
Manually annotated by BRENDA team
additional information
D2CSU4, D2CSU5, -
isoform CM2 does not enter the plastid and is most likely not located in the chloroplast
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bartonella henselae (strain ATCC 49882 / Houston 1)
Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10090
-
-
90-MtCM, MALDI-TOF mass spectrometry and calculated from amino acid sequence
11300
-
-
subunit, calculated from amino acid sequence
11700
-
A0QU81, -
the recombinant protein AroQMs in Escherichia coli
11770
-
-
105-MtCM, MALDI-TOF mass spectrometry and calculated from amino acid sequence
17800
-
A0QU81, -
in Escherichia coli for the mature *AroQMs protein
18540
-
-
subunit, calculated from amino acid sequence
18600
-
-
monomer, calculated, 167-residue untagged lederless MtCM; monomer, mass spectrometry, 167-residue untagged lederless MtCM
19540
-
-
monomer, calculated from the variant that lacks 33 N-terminal residues; monomer, mass spectrometry
19670
-
-
monomer, calculated from the leaderless variant with additional start methionine; monomer, mass, spectrometry, leaderless variant with additional start methionine
22000
-
-
monomer, SDS-PAGE
23000
-
-
monomer, SDS-PAGE, 167-residue untagged lederless MtCM
23500
-
-
gel filtration
25790
-
-
gel filtration
27900
-
-, Q3LUD9, Q3LUE0
calculated from amino acid sequence
29390
-
-
gel filtration
30110
-
B6C761, -
predicted from amino acid sequence
35400
-
-
ultracentrifugation
36000
-
-
enzyme form CM2, gel filtration
37000
-
-
monomeric molecular mass 18474 Da. Absorbance, liquid chromatography-mass spectrometry
40000
-
-
gel filtration
43400
-
-
gel filtration
45000
-
-
enzyme form CM2, gel filtration
47590
-
Q84FH6
gel filtration
48000
-
-
enzyme form CM2, gel filtration
50000
-
-
sucrose density gradient centrifugation
50000
-
-
enzyme form CM1, gel filtration
51000
-
-
sucrose density gradient centrifugation
52000
-
-
enzyme form CM1, gel filtration
55000
-
-
gel filtration, another enzyme form with MW 59000 exists
55000
-
-
gel filtration
56000
-
-
enzyme form CM1, gel filtration
56000
-
-
enzyme form CM1, gel filtration
59000
-
-
gel filtration, another enzyme form with MW 55000 exists
60000
-
Claviceps sp.
-
gel filtration
61000
-
-
gel filtration
62200
-
-, Q9Y7B2
gel filtration
63000
-
-
gel filtration
65000
-
-
enzyme form CM2, gel filtration
65000
-
-, Q9Y7B2
PAGE
70000
-
-, Q9P4D8
PAGE
75000
-
-
enzyme form CM1, gel filtration
78000
-
-
sedimentation equilibrium analysis
91000
-
-
gel filtration, in presence of Phe or Tyr a MW of 175000 is measured
140000
-
-
chorismate mutase/prephenate dehydratase, enzyme form CM2, gel filtration
160000
180000
-
disc gel electrophoresis
187000
-
-
chorismate mutase/prephenate dehydratase, gel filtration
320000
-
-
chorismate mutase/prephenate dehydratase, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 40000, chorismate mutase/prephenate dehydratase, tryptic fingerprinting suggests that the 40000 MW subunits are closely similar if not identical
?
-
two different components are detected by gel filtration, component A with MW 250000 and component B with MW 25000. The two components associate reversibly to give an active enzyme complex with MW 320000
?
-
x * 14500, at least 3 subunits not linked together by disulfide bridges, SDS-PAGE
?
-
x * 40000, the smallest native species of the enzyme, determined by sedimentation equilibrium, appears to be a dimer
?
Escherichia coli K12
-
x * 40000, chorismate mutase/prephenate dehydratase, tryptic fingerprinting suggests that the 40000 MW subunits are closely similar if not identical; x * 40000, the smallest native species of the enzyme, determined by sedimentation equilibrium, appears to be a dimer
-
?
Streptomyces aureofaciens tue 24
-
x * 14500, at least 3 subunits not linked together by disulfide bridges, SDS-PAGE
-
dimer
-
2 * 39000, SDS-PAGE; 2 * 42042, calculation from nucleotide sequence
dimer
-
2 * 14500, SDS-PAGE
dimer
-
2 * 45000, SDS-PAGE
dimer
-
SDS-PAGE and gel filtration
dimer
-, Q9P4D8
32000, SDS-PAGE
dimer
-
alpha2, ultracentrifugation, gel filtration
dimer
-
2 * 22000, gel filtration, SDS-PAGE
dimer
-
Each assymmetric unit contains a homodimer, corresponding to the two protomers (A and B) of the biological dimer. The structure of a *MtCM protomer strongly resembles the fold of the EcCM dimer, which consists of two intertwined subunits of three helices each and which comprises two active sites
dimer
-
the dimeric chorismate mutase is a thermostable and conventionally folded enzyme, X-ray chrystallography
heterodimer
-
x-ray crystallography
homodimer
-
alpha2, 2 * 11883-11887, deduced from amino acid sequence, ESI-MS, MALDI-MS
homodimer
-
alpha2, 2 * 12843-12848, deduced from amino acid sequence, ESI-MS, MALDI-MS
homodimer
-, Q9Y7B2
alpha2, 2 * 30000, calculated from amino acid sequence, homology modeling, electron microscopy
homodimer
-
The regulating Trp ligand is found to be sandwiched between the two monomers in a dimer containing residues 66-68
homodimer
-
2 * 18747, all alpha-helical bundle structure, two monomeric subunits
homodimer
-
2 * 6000, SDS-PAGE
homodimer
Q7CHH5, -
x-ray crystallography
homodimer
B6C761, -
recombinant enzyme, low-temperature SDS-PAGE
homodimer
-
native enzyme
homodimer
-
2 * 12000, SDS-Page
homodimer
-
2 * 19000, SDS-PAGE
monomer
-
monomeric chorismate mutase combines high catalytic activity with the characteristics of a molten globule, X-ray crystallography
tetramer
-
4 * 47000, chorismate mutase/prephenate dehydratase, SDS-PAGE
trimer
-
alpha3, crystallization studies
trimer
Q84FH6
alpha3, 3 * 15800, SDS-PAGE
trimer
-
crystal structure
trimer
-
constisting of three pseudo-alpha/beta barrels
monomer
-
provides essentially the same catalytic power as the native enzyme, behaves like a molten globule (an ensemble of poorly packed and rapidly interconverting conformers)
additional information
-
In MtbCM, while one face of helix 3 contributes to residues involved in monomer-monomer contracts and the allosteric site, the other face contributes to residues involved in the interaction with the substrate. The active site in the gene duplicated monomer is occupied by a sulfate ion and is located in the second half of the polypeptide
additional information
-
Ligand-induced structural changes are shown. Experiments neither show evidence for an equilibrium between the dimer and a *MtCM dimer of an intertwined nature, nor for an equilibrium with a monomer at lower protein concentrations as observed for engineered topology variants of chorismate mutases. The active site of *MtCM is highly similar to the catalytic sites of the other structurally characterized AroQ chorismate mutases
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structures of double mutants C88S/R90K and C88K/R90S, hanging drop vapour diffusion method at room temperature, space group R3 with a and b: 82.6 A and c: 42.8 A
-
hanging drop vapor-diffusion method at room temperature and high ionic strength, orthorhombic space group P212121 with a: 52.2 A, b: 83.8 A, c: 86.0 A, nine sulfate ions, five glycerol molecules, 424 water molecules
-
Performance of molecular dynamics simulations for the three enzyme-ligand complexes(CHOR,PRE and TSA) in addition to the TPS calculations. 8-hydroxy-2-oxa-bicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid as a TSA. The principal component analysis (PCA) to analyze structures is used
P19080
*MtCM, encoded by ORF Rv1885c in strain H37Rv. First characterized example of an AroQgamma fold. Description of the crystal optimization of a protein target that crystallizes very rapidly. 1. 175-residue version of *MtCM (encoded on plasmid pKTU3-HCT, dissolved in 20 mM potassium phosphate buffer pH7.5. 2. leaderless untagged 167-residue version of *MtCM encoded by plasmid pKTU3-HT used, buffered with 20 mM Tris-HCl pH 8.0)
O07746
37.2 kDa. Each asymmetric unit contains a homodimer, corresponding to the two protomers of the biological dimer. *MtCM as a model system for the *AroQ subclass and determined its crystal structure at high resolution, both in its unliganded form and in complex with transition state analog (1S,3S,5R,6R)-6-hydroxy-4-oxabicyco[3.3.1]non-7-ene-1,3-dicarboxylic acid. Heavy-atom derivatives prepared. Successful heavy-atom compounds are lead (II) acetate and thallium (III) acetate
-
alone and in complex with 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase, hanging drop vapor diffusion method, using 25% (w/v) PEG 1500 and 0.1 M MMT buffer (L-malic acid, MES, Tris) pH 8.0-9.0
P64767
Analysis of the structure shows a novel fold topology for the protein with a topologically rearranged helix containing R134. *MtCM does not have an allosteric regulation site
-
analysis reveals the presence of two monomers in the asymmetric unit
-
in complex with L-malate, hanging drop vapor diffusion method, using 15% (w/v) PEG 1500 and 0.1 M of the L-malate-containing MMT buffer system pH 8.0-9.0
-
MtCM (Rv1885c) (PDB ID-2F6L), docked conformation of (3S,6Z)-8-hydroxy-2-oxabicyclo[3.3.3]undec-6-ene-3,5-dicarboxylic acid, 4-[[2-(3,4-dimethoxyphenyl)ethyl]amino]-3-nitro-5-sulfamoylbenzoic acid, and (3S,6Z)-8-hydroxy-2-azabicyclo[3.3.3]undec-6-ene-3,5-dicarboxylic acid, (2Z)-2-(4-chlorophenyl)-3-(4,5-dimethoxy-2-nitrophenyl)prop-2-enoic acid in the catalytic site of MtCM x-ray crystal structure is shown
-
of the homodimeric chorismate mutase (Rv1885c). The crystal structure corresponds to the AroQ class CM of Mycobacterium tuberculosis. Determination of the crystal structure of the unique extracytoplasmic MtbCM in complex with its allosteric ligand, L-Trp. Se-Met MtbCM crystallizes in space group C2 in the presence of Trp. The Mycobacterium tuberculosis enzyme is an all-helical protein. Structural comparisons show that CMs from different organisms have envolved into two completely unrelated protein folds, suggesting separate evolutionary origins of the enzyme. On the basis of the structural fold adopted by the protein, CMs have been classified into the AroH and AroQ classes
-
sitting drop vapour diffusion method, using 0.1 M Tris-HCl (pH 8.6), 0.2 M MgCl2, and 20% poly(ethylene glycol) 400 for the 90 amino acid enzyme 90-MtCM
-
crystal structure of the T state of the allosteric enzyme and comparison with the R state
-
crystal structure of wild-type enzyme cocrystallized with Trp and an endo-exabicyclic transition state analogue inhibitor, of wild-type enzyme cocrystallized with Tyr and the endo-oxabicyclic transition state analogue inhibitor and of the Thr226Ser mutant enzyme in complex with Trp
-
Thr226Ile mutant enzyme
-
The corresponding positional fluctuations from the MD simulation are in good agreement with those obtained by X-ray crystallography
-
hanging drop vapour diffusion method, in 2 M ammonium sulfate, 0.1 M citrate/phosphate buffer, pH 4.2
Q7CHH5, -
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
20 min, stable
30
-
Q84FH6
half-life of 61.7 min
37
-
-
heat inactivation above
42
-
-
4 min, 59% loss of chorismate mutase P activity, no effect on chorismate mutase T activity
45
-
-
20 min, no denaturation, enzyme form CM1 and CM2
45
-
-
5 min, enzyme form CM1, 50% loss of activity
50
60
-
5 min, enzyme form CM2, stable
50
-
Q84FH6
half-life of 42.7 min
52
-
-
20 min, 50% loss of activity, enzyme form CM1; 5 min, more than 50% loss of activity, enzyme form CM2
54
-
-
1 h, 50% loss of activity, wild-type enzyme
55
-
-
pH 9.0, 5 min, enzyme form CM2, 15% loss of activity
58
-
-
1 h, 50% inactivation, genetically engineered enzyme with amino acid residues 1-285
60
-
-
10 min, strain 672, 90% loss of activity; 14 min, strain 168, stable
60
-
-
reversible heat inactivation above
60
-
-
pH 9.0, 5 min, stable up to
60
-
-
reversible heat inactivation above
60
-
-
complete denaturation of the enzyme occurs at a temperature close to 60C
62
-
-
1 h, 50% inactivation, genetically engineered enzyme with amino acid residues 1-300
63
-
-
midpoint of unfolding transitions
70
-
Q84FH6
half-life of 8.1 min
80
-
Q84FH6
half-life of 6.5 min
88
-
-
midpoint of unfolding transitions
100
-
-
15 min, activity can be restored
100
-
Q84FH6
half-life of 1.4 min
additional information
-
-
calculated Tm: 48C
additional information
-
-
The melting point of the active complementations (changes in position 7, 32, 35, 48, 81 and 85) is shown
additional information
-
-
*MtCM melting temperature of 48C
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the enzyme is stable in high concentrations of glycerol, above 10% v/v, pH 7.5-8.0, and in the presence of thiols, citrate, and NAD+
-
chorismate mutase irreversibly immobilized by n-decylamine-substituted agarose allows repeated quantitative conversion of chorismate to prephenate
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-78C, 100 mM N-ethylmorpholine, 1.0 mM dithioerythritol, 1.0 mM N-ethylene-diaminetetraacetic acid, 21 mM trisodium citrate, 10% (v/v) glycerol in doubly distilled water adjusted to pH 7.0 with concentrated HCl
-
0C or -20C, enzyme form CM1, stable for at least 1 month
-
0C or -20C, enzyme form CM2, stable for at least 2 weeks
-
-20C, enzyme form CM1 and CM2 are stable
-
4C, 0.1 mM Trp, stable for 5 days with a rapid loss in activity after this time
-
0C or -20C, enzyme forms CM1 and CM2, stable for at least 6 weeks
-
-25C, in presence of PMSF, stable for at least 2 months
-
4C, in presence of PMSF, stable for at least 1 month
-
4C, stable for 1 month
-
-20C, partially purified enzyme, stable for 7 days
-
-20C, enzyme form CM2, less than 10% loss of activity after 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
His-Bind protein purification column chromatography
-
in association with prephenate dehydratase
-
chorismate mutase/prephenate dehydratase
-
N-terminal Met1 is in most samples removed
-
Ni-NTA column chromatography
-
Ni2+ affinity column chromatography and gel filtration
-
*MtCM, which has a melting temperature of 48C, rapidly renatures after heat denaturation, and have subsequently exploited this feature for purifying the enzyme
-
ammonium sulfate precipitation, Ni-NTA agarose column chromatography, and Superdex 75 gel filtration
P64767
anion exchange column chromatography, Superdex 75 gel filtration
-
subtilisin column chromatography and Sephadex G-75 gel filtration
-
to near homogeneity
-
-
-, Q9P4D8
Ni2+-affinity column chromatography; Ni2+-affinity column chromatography
D2CSU4, D2CSU5, -
partial
-
enzyme form CM1 and CM2
-
enzyme form CM1 and CM2
-
Q Sepharose column chromatography and Sephacryl HR 200 gel filtration
-
gel filtration
Q7CHH5, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
expression in Escherichia coli
-
overexpression in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
overexpression in a Saccharomyces cerevisiae aro7DELTA mutant strain
-, Q9Y7B2
expressed in Arabidopsis thaliana; generation of transgenic Arabidopsis plants expressing a bacterial feedback-insensitive chorismate mutase/prephenate dehydratase gene (truncated PheA) under the control of the 35S CaMV promoter, fused inframe at the 3' end of the coding sequence to DNA encoding a hemagglutinin epitope tag. Two chimeric constructs: in one, DNA encoding a Rubisco small subunit-3A plastid transit peptide is fused in-frame to the 5' end of the PheA open reading frame to direct the bacterial enzyme in to the plastid where aromatic amino acid biosynthesis is localized. The second construct lacks the Rubisco small subunit-3A plastid transit peptide in order to test whether aromatic amino acid metabolism is strictly localized to the plastid or whether at least some parts of it operate in the cytosol. Both constructs transformed into Arabidopsis plants, and homozygous T2 plants are generated
-
expressed in Escherichia coli strain FA114
-
expression in Escherichia coli
-
expression in Escherichia coli BL21(DE3)
-
expressed in Escherichia coli strain BL21
B6C761, -
-
-, Q3LUD9, Q3LUE0
expression in a chorismate mutase deficient Escherichia coli mutant
-
expressed in Escherichia coli
-
expressed in Escherichia coli KA13 cells
-
expressed in Escherichia coli strain KA13
-
expression in Escherichia coli
-
Construction of mycobacterial reporter plasmids is described. In contrast to the studies in Mycobacterium tuberculosis, very little is known of CMs in Mycobacterium smegmatis. Homolouges of Rv1885c and Rv0948c are present in the MSMEG5513 have been recently annotated as potential CMs. Rv1885c protein used as a control for the experiments describing Rv0948c and the two Mycobacterium smegmatis homologues; in Mycobacterium smegmatis: homologues of each CM from Mycobacterium tuberculosis are found in Mycobacterium smegmatis, a nonpathogenic species. These homologues (which correspond to ORFs MSMEG5513 and MSMEG2114 respectively) cloned, expressed in Escherichia coli (strains DH5alpha, DH10B and BL21(DE3)), and demonstrate to possess CM activity as their Mycobacterium tuberculosis counterparts
A0QU81, -
*MtCM prepared from Escherichia coli strain KA29
O07746
Escherichia coli strain KA29
-
Escherichia coli strains C600lambda lysogen, MZ1, Nova Blue, BL21(DE3)
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli strain KA13
-
expression in Escherichia coli
-
expression in Escherichia coli BL21
-
expression in Escherichia coli BL21 (DE3)
-
overexpressed in Escherichia coli BL21 (DE3). Mycobacterium tuberculosis CMs are believed to have evolved from duplication of an ancestral CM gene, formation of the active site in a single polypeptide chain appears to be a consequence of this duplication event
-
expression in a Saccharomyces cerevisiae aro7DELTA strain; overexpression in Hansenula polymorpha
-, Q9P4D8
expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
D2CSU4, D2CSU5, -
expression in Escherichia coli with a His-tag
Q84FH6
expressed in Escherichia coli BL21(DE3) cells
Q7CHH5, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C75S
-
viscosity-insensitive
C88K/R90S
-
lower activity than wild-type enzyme
C88S/R90K
-
lower activity than wild-type enzyme
DELTA117-127
-
large increase in KM and slower turnover relative to wild-type enzyme
DELTA117-127
-
lower turnover and lower KM than wild-type enzyme
DELTA118-127
-
large increase in KM and slower turnover relative to wild-type enzyme
DELTA118-127/K111N/A112S/V113N
-
large increase in KM and slower turnover relative to wild-type enzyme
DELTA118-127/R116L/P117T
-
large increase in KM and slower turnover relative to wild-type enzyme
DELTA119-127/D118N
-
large increase in KM and slower turnover relative to wild-type enzyme
R90A
-
no activity detectable
R90G
-
very low activity
R90K
-
The ES, TS, and product structures of the mutants are determined based on the wild-type structure. The hydrogen-bond lengths of the mutants differ from the wild-type. The two mutants chemical reaction progresses in a similar way. No large geometrical changes in and around the active site along the reaction path: only a small rearrangement of the hydrogen-bond sites. As for Lys90/Cit90 mutant reactions, no large conformational change is observed in the overall protein structure except for the geometries around the mutation point. Although the catalytic activity of R90K is inferior to that of the wild-type, the enzymatic mechanism of the R90K mutant is similar to the wild-type. The main anticatalytic factor of R90Cit mutant is the ES stabilization as a result of destabilizing the substrate by the surrounding electrostatic field because of the mutated enzyme. Therefore the TS stabilization mechanism of the Cit90 mutant is quite different from that of the wild-type BsCM
R90Q
-
complete inactivation of enzyme
D233I
-, Q9Y7B2
little reduced regulatory range through tyrosine and tryptophan than wild-type enzyme
D233T
-, Q9Y7B2
strong reduced regulatory range through tyrosine and tryptophan than wild-type enzyme
A32S
-
increased catalytic efficiency
D48I
-
no activity
DELTA102-285
-
hybrid of chorismate mutase and allosteric domain from P-protein without prephrenate dehydratase
H131A
-
30% activity compared to wild-type enzyme
H153N
-
lower turnover and higher KM than wild-type enzyme
H189N
-
much lower turnover than wild-type enzyme
H197N
-
lower turnover and higher KM than wild-type enzyme
H239N
-
lower turnover and higher KM than wild-type enzyme
H245N
-
lower turnover and higher KM than wild-type enzyme
H257A
-
lower turnover and higher KM than wild-type enzyme
H265A
-
lower turnover and higher KM than wild-type enzyme
H347N
-
lower turnover than wild-type enzyme
I81L/V85I
-
reduced catalytic efficiency, alters packing against the hydrophobic ring face of the reacting molecule
K37A
-
more poorly expressed than wild-type, inactive and instable
K37Q
-
no activity
K39N
-
the mutant enzymes Lys39Arg, Lys39Asn, Lys39Gln, Gln88Arg, and Gln88Glu show similar structures to the wild-type enzyme, as indicated by circular dichroism spectra, with Lys39Gln showing small deviation. The turnover numbers for the mutant enzymes Lys39Arg, Lys39Asn and Lys39Gln are 335fold, 820fold and 4090fold lower than the turnover number of the wild-type enzyme, no significant differences in Km-value for chorismate between Lys39Arg, Lys39Asn, and the wild-type enzyme
K39Q
-
the mutant enzymes Lys39Arg, Lys39Asn, Lys39Gln, Gln88Arg, and Gln88Glu show similar structures to the wild-type enzyme, as indicated by circular dichroism spectra, with Lys39Gln showing small deviation. The turnover numbers for the mutant enzymes Lys39Arg, Lys39Asn and Lys39Gln are 335fold, 820fold and 4090fold lower than the turnover number of the wild-type enzyme, no significant differences in Km-value for chorismate between Lys39Arg, Lys39Asn, and the wild-type enzyme
K39R
-
the mutant enzymes Lys39Arg, Lys39Asn, Lys39Gln, Gln88Arg, and Gln88Glu show similar structures to the wild-type enzyme, as indicated by circular dichroism spectra, with Lys39Gln showing small deviation. The turnover numbers for the mutant enzymes Lys39Arg, Lys39Asn and Lys39Gln are 335fold, 820fold and 4090fold lower than the turnover number of the wild-type enzyme, no significant differences in Km-value for chorismate between Lys39Arg, Lys39Asn, and the wild-type enzyme
Q88E
-
mutation of Gln88 to Glu in the monofunctional chorismate mutase results in an enzyme with a pH profile of activity significantly different from that of the wild-type protein
Q88E
-
mutation of Gln88 to Glu in the monofunctional chorismate mutase results in an enzyme with a pH profile of activity significantly different from that of the wild-type protein; the mutant enzymes Lys39Arg, Lys39Asn, Lys39Gln, Gln88Arg, and Gln88Glu show similar structures to the wild-type enzyme, as indicated by circular dichroism spectra, with Lys39Gln showing small deviation. The turnover numbers for the mutant enzymes Lys39Arg, Lys39Asn and Lys39Gln are 335fold, 820fold and 4090fold lower than the turnover number of the wild-type enzyme, no significant differences in Km-value for chorismate between Lys39Arg, Lys39Asn, and the wild-type enzyme
Q88R
-
the mutant enzymes Lys39Arg, Lys39Asn, Lys39Gln, Gln88Arg, and Gln88Glu show similar structures to the wild-type enzyme, as indicated by circular dichroism spectra, with Lys39Gln showing small deviation. The turnover numbers for the mutant enzymes Lys39Arg, Lys39Asn and Lys39Gln are 335fold, 820fold and 4090fold lower than the turnover number of the wild-type enzyme, no significant differences in Km-value for chorismate between Lys39Arg, Lys39Asn, and the wild-type enzyme
D48G
-
the mutation causes kcat/Km to decrease by 3 fold
F77W
-
mutant exhibits decreased activity compared to the wild type enzyme
Q88N
-
mutant exhibits decreased activity compared to the wild type enzyme
R51Q
-
mutant exhibits decreased activity compared to the wild type enzyme
V35A
-
mutant exhibits decreased activity compared to the wild type enzyme
D69A
-
site directed mutagenesis constitute the catalytic site
E109A
-
site directed mutagenesis constitute the catalytic site
E109Q
-
site directed mutagenesis constitute the catalytic site
G86A
-
mutant shows reduced kcat and Km values compared to the wild type enzyme
K60A
-
site directed mutagenesis constitute the catalytic site
R134A
-
site directed mutagenesis constitute the catalytic site
R49A
-
site directed mutagenesis constitute the catalytic site
R72A
-
site directed mutagenesis constitute the catalytic site
Y105A
-
site directed mutagenesis constitute the catalytic site
E23D
-
abolishes the substrate-induced homotrophic effect, but retains the effector-induced heterotrophic effecs, the coupling between helix 11 and helix 12 is weakened
I225T
-
mutant enzyme Ile225Thr is activated by Trp, but is insensitive to Tyr
N139L/R156L
-
increase in global flexibility
T226D
-
reduced regulatory range through tyrosine and tryptophan than wild-type enzyme
T226I
-
mutant Thr226Ile
T226I
-
reduced regulatory range through tyrosine and tryptophan than wild-type enzyme
Y234F
-
enzymes with mutations of Tyr234, especially Tyr234Phe are unresponsive to Tyr but are activated by Trp
additional information
-
-
CM enzymes, which are not precisely annotated in the original genome sequence of Mycobacterium tuberculosis H37Rv and the subsequent reannotation. In the annotation, two ORFs (Rv0948c and Rv1885) with some similarity to CMs, including the well-known monofunctional periplasmic CM from Erwinia herbicola, are found, although these ORFs are described as conserved hypothetical proteins
L7I
-
no significant effect on catalytic efficiency
additional information
-
genetically engineered monofunctional chorismate mutase that contains only 109 amino acids starting with the bifunctional P protein that also exhibits prephenate dehydratase activity and is composed of 386 amino acids
additional information
-
proteins containing residues 1-285 and residues 1-300 retain full chorismate mutase activity and prephenate dehydratase activity, but exhibit no feedback inhibition. Proteins containing residues 101-386 and residues 101-300 retain full prephenate dehydratase activity, but lack mutase activity
additional information
-
EcCM active-site residues (Leu7, Ala32, Val35, Asp48, Ile81, Val85) that mutated in our previous computational design experiment. Each of the 114 variants tested for complementation of the chorismate mutase deficiency of the auxotrophic Escherichia coli KA12/pKIMP-UAUC system. 34% of all single mutants are scored as biological active
V35I
-
increased KM and turnover values compared to wild type
additional information
B6C761, -
Gr-cm-1-IRII, generated by retention of intron 2 of the Gr-cm-1 pre-mRNA through alternative splicing encodes a truncated protein (GR-CM-1t) lacking the chorismate mutase domain with no activity
additional information
-
The results of the mutagenesis and the activity show that Arg49, Lys 60, Arg72, and Arg134 are essential for catalysis
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
misfolded, higher-order aggregates convert into fully active dimeric protein by denaturation with guanidinium chloride and subsequent renaturation upon dilution into native buffer; refolding after treatment with urea
-
refolding after treatment with guanidinium chloride
-
thermal denaturation shows a sharp transition from the native to the denatured state, with a calculated Tm of 48C. Upon subsequent cooling, the protein renatured easily
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enzyme can be inactivated in a boiling water bath and afterwards reactivated at 30 C to 100% of its original activity
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renaturation of heat-denatured enzyme
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
drug development
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Since this enzyme is absent from mammals, it represents a promising target for the development of new antimycobacterial drugs, which are needed to combat Mycobacterium tuberculosis, the causative agent of tuberculosis
analysis
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As an intramolecular reaction that appears to be catalyzed without intermediate steps, covalent catalysis, or modification of the reaction pathway, the chorismate-prephenate rearrangement has become an important model system for theoretical approaches to the study of enzyme catalysis
agriculture
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the widespread presence of chorismate mutases in the specialized sedentary endoparasitic nematode species suggests that this multifunctional enzyme may be a key factor in modulating plant parasitism
drug development
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the enzyme serves as a potential target for the development of inhibitors specific to the pathogen
drug development
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MtCM might play a role in host-pathogen interactions, making it an important target for designing inhibitor molecules against the deadly pathogen
drug development
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multiple-drug-resistant tuberculoses bacillus and its synergism with HIV-characterization of new enzyme targets and the development of new drugs
drug development
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advantage of the nonoccurance of CMs in human, develop antimicrobial drugs to combat dreaded human pathogens such as Mycobacterium tuberculosis
drug development
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fighting diseases such as tuberculosis. Since vertebrates lack the shikimate pathway for the biosynthesis of aromatic compounds and thus do not possess chorismate mutase activity, this enzyme represents a prime target for the development of antibiotics, fungicides and herbicides