Information on EC 4.2.1.19 - imidazoleglycerol-phosphate dehydratase

New: Word Map on EC 4.2.1.19
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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
LITERATURE
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
highly stereospecific, inversion of configuration at C3
-
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
Histidine metabolism
-
-
histidine metabolism
-
-
L-histidine biosynthesis
-
-
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
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
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
-
-
-
-
-
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
H9C4A4
-
-
-
?
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
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
show the reaction diagram
Candida humilis CBS 8195
H9C4A4
-
-
-
?
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
?
show the reaction diagram
-
-
-
-
-
additional information
?
-
P0CO22
sixth step in histidine biosynthesis
-
?
additional information
?
-
E9KPK6
enzyme activity is measured with 4-nitrophenyl phosphate as substrate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
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
H9C4A4
-
-
-
?
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
?
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
Candida humilis CBS 8195
H9C4A4
-
-
-
?
additional information
?
-
P0CO22
sixth step in histidine biosynthesis
-
?
METALS and IONS
ORGANISM
UNIPROT
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
Mn2+
-
contains two Mn2+ ions, 0.05 mM Mn2+ used in assay conditions
additional information
-
not activated by Mg2+, Ni2+, Cd2+, Fe2+, Co2+
additional information
-
not activated by Mg2+, Ni2+, Cd2+, Fe2+, Co2+, Fe3+
INHIBITORS
ORGANISM
UNIPROT
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
3-Amino-1,2,4-triazole
-
competitive
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
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
activation
cysteine
-
activation
mercaptoethylamine
-
activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
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
-
-
0.122
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
-
at pH 7.7 and 30C
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
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1000
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
-
at pH 7.7 and 30C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03
3-Amino-1,2,4-triazole
-
-
0.31
3-Amino-1,2,4-triazole
-
at pH 7.7 and 30C
0.008
phosphate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 7
-
-
7.5
-
wild-type enzyme
8
-
enzyme expressed in Escherichia coli
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 8
E9KPK6
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 60
E9KPK6
assay range
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Staphylococcus aureus (strain N315)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70000
-
trimeric enzyme in absence of Mn2+, gel filtration
5546
260000
-
bifunctional enzyme with EC 3.1.3.15, gel filtration
5531
290000
-
gel filtration
5534
300000
-
gel electrophoresis
5534
500000
-
polymeric enzyme in presence of Mn2+, gel filtration
5546
540000
-
gel filtration
5545
570000
-
gel filtration
728872
600000
-
gel filtration
5540
670000
-
gel electrophoresis
5540
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 22000, calculation from nucleotide sequence
?
-
x * 22466, calculation from nucleotide sequence
multimer
P0CO22
1 equivalent of Mn2+ per subunit induces the formation of 24-mers from the trimeric enzyme
polymer
-
x * 35000, SDS-PAGE
polymer
-
x * 46000, bifunctional enzyme with EC 3.1.3.15, SDS-PAGE
polymer
-
x * 23833, light scattering
polymer
-
24 * 21206, MALDI-TOF
polymer
-
x * 25000, subunits not linked by disulfide bridges, SDS-PAGE
tetradodecamer
-
-
trimer
P0CO22
1 equivalent of Mn2+ per subunit induces the formation of 24-mers from the trimeric enzyme
Crystallization/COMMENTARY
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
irreversible inactivation below
5531
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
54
-
60 min stable
5534
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Mg2+, Mn2+, glycerol, dithiothreitol do not stablilize
-
-80C, 20 mM triethanolamine-HCl buffer, pH 7.5, 100 mM 2-mercaptoethanol
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
photooxidation in presence of Rose Bengal
-
5534
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA affinity column chromatography and gel filtration
H9C4A4
Ni-NTA affinity column chromatography and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21
-
expressed in Saccharomyces cerevisiae strain BY4742
H9C4A4
expression in Saccharomyces cerevisiae
-
expressed in Mycobacterium smegmatis strain mc24517
-
expression in Escherichia coli
-
expression in Saccharomyces cerevisiae
-
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
E9KPK6