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Information on EC 5.4.99.5 - chorismate mutase and Organism(s) Thermus thermophilus and UniProt Accession Q84FH6
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5.4.99.5 chorismate mutaseSpecify your search results
Word Map
- 5.4.99.5
- shikimate
-
sieve
-
monofunctional
- phloem
- l-phenylalanine
- l-tyrosine
- 7-phosphate
- mutases
-
t-proteins
-
3-deoxy-d-arabino-heptulosonate
- phenylpyruvate
-
claisen
- arogenate
-
pericyclic
-
nonketotic
- hyperglycinemia
- isochorismate
-
cyclohexadienyl
- hydroxyphenylpyruvate
-
photorespiratory
-
preorganization
- drug development
-
3-deoxy-d-arabino-heptulosonate-7-phosphate
- meloidogyne
- synthesis
- agriculture
- analysis
The taxonomic range for the selected organisms is: Thermus thermophilus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
chorismate mutase, p-protein, chorismate mutase/prephenate dehydratase, chorismate mutase-prephenate dehydrogenase, bacillus subtilis chorismate mutase, cm type 2, rv1885c, cm0819, atcm1, chorismate mutase 1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Chorismate mutase/prephenate dehydratase
-
-
-
-
Mutase, chorismate
-
-
-
-
P protein
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Chorismate = prephenate
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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
Chorismate pyruvatemutase
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CAS REGISTRY NUMBER
COMMENTARY
9068-30-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Chorismate
Prephenate
biosynthesis of aromatic amino acids
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Chorismate
Prephenate
biosynthesis of aromatic amino acids
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
tyrosine
competitive inhibition, 0.5 M tyrosine leads to 40% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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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 70°C 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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 70
-
studies that elucidate the dependence of the E-S active site on temperatures 25, 60 and 70°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
trimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
The corresponding positional fluctuations from the MD simulation are in good agreement with those obtained by X-ray crystallography
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Helmstaedt, K.; Heinrich, G.; Merkl, R.; Braus, G.H.
Chorismate mutase of Thermus thermophilus is a monofunctional AroH class enzyme inhibited by tyrosine
Arch. Microbiol.
181
195-203
2004
Thermus thermophilus (Q84FH6), Thermus thermophilus
Zhang, X.; Bruice, T.C.
The proficiency of a thermophilic chorismate mutase enzyme is solely through an entropic advantage in the enzyme reaction
Proc. Natl. Acad. Sci. USA
102
18356-18360
2005
Thermus thermophilus
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