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Information on EC 3.5.4.10 - IMP cyclohydrolase and Organism(s) Gallus gallus and UniProt Accession P31335

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Gallus gallus
UNIPROT: P31335 not found.
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The taxonomic range for the selected organisms is: Gallus gallus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
itga2, imp cyclohydrolase, impch, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/imp cyclohydrolase, inosine monophosphate cyclohydrolase, purh2, aicar transformylase/imp cyclohydrolase, inosinicase, mthpuro, af1811, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
inosine monophosphate cyclohydrolase
-
ATIC
-
-
-
-
IMP synthetase
-
-
-
-
IMPCHase
-
-
-
-
inosinate cyclohydrolase
-
-
-
-
inosine monophosphate cyclohydrolase
-
-
-
-
inosinicase
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
IMP 1,2-hydrolase (decyclizing)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9013-81-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
?
show the reaction diagram
-
de novo purine synthesis step 10
-
-
?
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
IMP + H2O
show the reaction diagram
trans-alpha,beta-diformamido-beta-(5'-phosphoribosylamino)acrylamide
IMP + H2O
show the reaction diagram
-
-
-
ir
additional information
?
-
bifunctional enzyme aminoimidazole-comprising the 4-carboxamide ribonucleotide transformylase, AICAR or Tfase, residues 200-593 and the IMPCH, ATIC, activities and catalyzes the final step in the de novo purine biosynthesis pathway that produces IMP, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
?
show the reaction diagram
-
de novo purine synthesis step 10
-
-
?
additional information
?
-
bifunctional enzyme aminoimidazole-comprising the 4-carboxamide ribonucleotide transformylase, AICAR or Tfase, residues 200-593 and the IMPCH, ATIC, activities and catalyzes the final step in the de novo purine biosynthesis pathway that produces IMP, overview
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2-dioxo-1,5-dihydroimidazo[4,5-c][1,2,6]thiadiazin-4(3H)-one
construction of 1,5-dihydroimidazo[4,5-c][1,2,6]thiadiazin-4(3H)-one 2,2-dioxide, the corresponding nucleoside, and the nucleoside monophosphate, as mimics of the tetrahedral intermediate in the cyclization reaction. All compounds are competitive inhibitors against IMPCH, but the simpler heterocycle has a completely different IMPCH binding mode, compared to the nucleosides, and is relocated to the phosphate binding pocket, the aromatic imidazole ring interacts with a helix dipole, inhibitor synthesis, binding structure, and mechanism of inhibition, overview
7-(3,4-dihydroxy-5-hydroxymethyltetrahydrofuran-2-yl)-2,2-dioxo-1,5-dihydroimidazo[4,5-c][1,2,6]thiadiazin-4(3H)-one
construction of 1,5-dihydroimidazo[4,5-c][1,2,6]thiadiazin-4(3H)-one 2,2-dioxide, the corresponding nucleoside, and the nucleoside monophosphate, as mimics of the tetrahedral intermediate in the cyclization reaction. All compounds are competitive inhibitors against IMPCH, but the simpler heterocycle has a completely different IMPCH binding mode, compared to the nucleosides, and is relocated to the phosphate binding pocket, the aromatic imidazole ring interacts with a helix dipole, inhibitor synthesis, binding structure, and mechanism of inhibition, overview
phosphoric acid mono-[3,4-dihydroxy-5-(2,2,4-trioxo-1,5-dihydroimidazo[4,5-c][1,2,6]thiadiazin-7-yl)tetrahydrofuran-2-yl]methyl ester
construction of 1,5-dihydroimidazo[4,5-c][1,2,6]thiadiazin-4(3H)-one 2,2-dioxide, the corresponding nucleoside, and the nucleoside monophosphate, as mimics of the tetrahedral intermediate in the cyclization reaction. All compounds are competitive inhibitors against IMPCH, but the simpler heterocycle has a completely different IMPCH binding mode, compared to the nucleosides, and is relocated to the phosphate binding pocket, the aromatic imidazole ring interacts with a helix dipole, inhibitor synthesis, binding structure, and mechanism of inhibition, overview
IMP
-
minor 5% IMP contaminant in the substrate found to have no effects on the inosinicase assay
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.13
1,5-dihydroimidazo[4,5-c][1,2,6]thiadiazin-4(3H)-one 2,2-dioxide
pH 7.4
0.23
7-(3,4-dihydroxy-5-hydroxymethyltetrahydrofuran-2-yl)-2,2-dioxo-1,5-dihydroimidazo[4,5-c][1,2,6]thiadiazin-4(3H)-one
about, pH 7.4
0.15
phosphoric acid mono-[3,4-dihydroxy-5-(2,2,4-trioxo-1,5-dihydroimidazo[4,5-c][1,2,6]thiadiazin-7-yl)tetrahydrofuran-2-yl]methyl ester
about, pH 7.4
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.09
-
at 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional protein, including EC 3.5.4.10 and EC 2.1.2.3
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PUR9_CHICK
593
0
64415
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
64422
-
2 * 64422, open reading frame, gel filtration
71000
-
2 * 71000, relative mobility in SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in complex with inhibitors, sitting drop vapor diffusion method, 22°C, 10 mg/ml protein, mixing of equal volumes of protein and reservoir solutions, the latter containing 20% w/v PEG 8000, 0.2 M imidazole, pH 7.2, 5 mM dithiothreitol, X-ray diffraction structure determination and analysis at 2.0-2.7 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
154-fold
-
expressed as glutathione-S-transferase fusion protein in Escherichia coli mutants
-
from liver homogenate
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
the enzyme is a potential target for antineoplastic intervention, design of IMPCH inhibitors, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Baggott, J.E.; Krumdieck, C.L.
trans-alpha, beta-Diformamido-beta-(5-phosphoribosylamino)acrylamide: a possible new intermediate in de novo purine biosynthesis
Biochemistry
18
3501-3506
1979
Gallus gallus, Rattus norvegicus
Manually annotated by BRENDA team
Ni, L.; Guan, K.; Zalkin, H.; Dixon, J.D.
De novo purine biosynthesis: cloning, sequencing and expression of a chicken PurH cDNA encoding 5-aminoimidazole-4-carboxamide-ribinucleotide transformylase-IMP cyclohydrolase
Gene
106
197-205
1981
Gallus gallus
Manually annotated by BRENDA team
Caperelli, C.A.; Benkovic, P.A.; Chettur, G.; Benkovic, S.J
Purification of a complex catalizing folate cofactor synthesis and transformylation in de novo purine biosynthesis
J. Biol. Chem.
255
1885-1890
1980
Gallus gallus
Manually annotated by BRENDA team
Mueller, W.T.; Benkovic, S.J.
On the purification and mechanism of action of 5-aminoimidazole-4-carboxamide-ribonucleotide transformylase from chicken liver
Biochemistry
20
337-344
1981
Gallus gallus
Manually annotated by BRENDA team
Xu, L.; Chong, Y.; Hwang, I.; DOnofrio, A.; Amore, K.; Beardsley, G.P.; Li, C.; Olson, A.J.; Boger, D.L.; Wilson, I.A.
Structure-based design, synthesis, evaluation, and crystal structures of transition state analogue inhibitors of inosine monophosphate cyclohydrolase
J. Biol. Chem.
282
13033-13046
2007
Gallus gallus (P31335)
Manually annotated by BRENDA team