Information on EC 4.2.1.19 - imidazoleglycerol-phosphate dehydratase

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

EC NUMBER
COMMENTARY
4.2.1.19
-
RECOMMENDED NAME
GeneOntology No.
imidazoleglycerol-phosphate dehydratase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
-
-
-
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
energy of activation 15900 cal/mol
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
energy of activation 14700 cal/mol
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
highly stereospecific, inversion of configuration at C3
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
elimination
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
histidine biosynthesis
-
Histidine metabolism
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
D-erythro-1-(imidazol-4-yl)glycerol-3-phosphate hydro-lyase [3-(imidazol-4-yl)-2-oxopropyl-phosphate-forming]
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dehydratase, imidazoleglycerol phosphate
-
-
-
-
IGP dehydratase
-
-
-
-
IGPD
-
-
-
-
imidazoleglycerol phosphate dehydratase
-
-
-
-
imidazoleglycerolphoshate dehydratase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9024-35-5
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
-
-
-
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
-
-
-
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
-
-
-
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
-
-
-
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
-
-
-
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
-
-
-
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
-
-
-
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
-
-
-
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
-
-
-
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
-
-
-
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
-
-
-
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
P0CO22
removal of a non-acidic hydrogen atom in the dehydration reaction
-
?
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
?
show the reaction diagram
-
-
-
-
-
additional information
?
-
P0CO22
sixth step in histidine biosynthesis
-
?
additional information
?
-
E9KPK5
enzyme activity is measured with 4-nitrophenyl phosphate as substrate
-
-
-
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
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
?
show the reaction diagram
-
-
-
-
-
additional information
?
-
P0CO22
sixth step in histidine biosynthesis
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
P0CO22
metalloprotein, transition metals induce aggregation and are required for catalysis, 1 equivalent of Mn2+ per subunit induces the formation of 24-mers from the trimeric enzyme
Mn
-
the manganese cluster is critical in converting the inactive trimeric state of the enzyme into its biologically active 24-mer and also forms the active site. The substrate is bound to the manganese cluster as an imidazole moiety that subsequently collapse to yield a diazafulvene intermediate
Mn2+
-
activity dependent on
Mn2+
-
Km: 0.0076 mM
Mn2+
-
0.5 mM enhances the activity 7fold
Mn2+
-
essential for assembly of subunits
additional information
-
not activated by Mg2+, Ni2+, Cd2+, Fe2+, Co2+
additional information
-
not activated by Mg2+, Ni2+, Cd2+, Fe2+, Co2+, Fe3+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3-Amino-1,2,4-triazole
-
Ki: 0.03 mM
3-Amino-1,2,4-triazole
-
-
3-Amino-1,2,4-triazole
-
-
3-Amino-1,2,4-triazole
-
-
3-Amino-1,2,4-triazole
-
-
3-Amino-1,2,4-triazole
-
Ki: 0.0026 mM
3-Amino-1,2,4-triazole
-
Ki: 0.12 mM
phosphate
-
Ki: 0.008 mM
[3-Hydroxy-2-(1H-[1,2,4]triazol-3-yl)-butyl]-phosphonic acid
-
IRL 1803
[3-Hydroxy-2-(1H-[1,2,4]triazol-3-yl)-cyclohexyl]-phosphonic acid
-
IRL 1856
[3-Hydroxy-2-(1H-[1,2,4]triazol-3-yl)-propyl]-phosphonic acid
-
IRL 1695
additional information
-
not inhibited by histidinol phosphate, histidinol, histidine
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
activation
cysteine
-
activation
mercaptoethylamine
-
activation
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.049
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
-
-
0.083
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
-
-
0.1
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
-
-
0.2
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
-
wild-type enzyme
0.24
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
-
-
0.3
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
-
expressed in E. coli
0.4
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
-
-
0.54
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.03
-
3-Amino-1,2,4-triazole
-
-
0.008
-
phosphate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.195
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
wild-type enzyme
8
-
-
enzyme expressed in Escherichia coli
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
8
E9KPK5
assay range
6.8
8
-
wild-type enzyme, less than 50% of maximal activity above and below
7.2
8.2
-
enzyme expressed in E. coli, less than 50% of maximal activity above and below
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10
60
E9KPK5
assay range
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
70000
-
-
trimeric enzyme in absence of Mn2+, gel filtration
260000
-
-
bifunctional enzyme with EC 3.1.3.15, gel filtration
290000
-
-
gel filtration
300000
-
-
gel electrophoresis
500000
-
-
polymeric enzyme in presence of Mn2+, gel filtration
540000
-
-
gel filtration
600000
-
-
gel filtration
670000
-
-
gel electrophoresis
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 22466, calculation from nucleotide sequence
?
-
x * 22000, calculation from nucleotide sequence
multimer
P0CO22
1 equivalent of Mn2+ per subunit induces the formation of 24-mers from the trimeric enzyme
polymer
-
x * 46000, bifunctional enzyme with EC 3.1.3.15, SDS-PAGE
polymer
-
x * 35000, SDS-PAGE
polymer
-
x * 25000, subunits not linked by disulfide bridges, SDS-PAGE
polymer
-
24 * 21206, MALDI-TOF
polymer
-
x * 23833, light scattering
trimer
P0CO22
1 equivalent of Mn2+ per subunit induces the formation of 24-mers from the trimeric enzyme
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystallized in presence of Mn, unit-cell parameters: a = b = 157.9 A, c = 480 A, alpha = beta = 90°, gamma = 120°, with either 16 or 24 subunits in the asymmetric unit, space group R3, 3.0 A resolution
-
crystals belong to space group R3 with cell parameters a = 157.9 A, b = 157.9 A, c = 480 A, alpha = beta = 90°, gamma = 120°. Structure of manganese assembled, active form of the enzyme at 3.0 A resolution
-
trimeric form without Mn2+, hanging drop vapor diffusion method
P0CO22
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
-
irreversible inactivation below
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
54
-
-
60 min stable
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Mg2+, Mn2+, glycerol, dithiothreitol do not stablilize
-
-80°C, 20 mM triethanolamine-HCl buffer, pH 7.5, 100 mM 2-mercaptoethanol
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
photooxidation in presence of Rose Bengal
-
5534
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli BL21
-
expression in Saccharomyces cerevisiae
-
expression in Saccharomyces cerevisiae
-
expression in Escherichia coli
-
DNA and amino acid sequence determination and analysis, phylogenetic analysis, subcloning in Escherichia coli, functional complementation of a pho5? mutation, affecting a repressible acid phosphatase, and a his3? mutation in Saccharomyces cerevisiae, expression in Saccharomyces cerevisiae strain ML20Cstrain DSY-5
E9KPK5