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Enzyme Nomenclature
Information on EC 1.1.1.205 - IMP dehydrogenase
for references in articles please use BRENDA:EC1.1.1.205
Word Map on EC 1.1.1.205
- 1.1.1.205
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mycophenolic
- guanine
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immunosuppressive
- purine
- mofetil
- leukemia
- ribavirin
- tiazofurin
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antiviral
- renal
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rejection
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recipients
- xmp
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salvage
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cyclosporine
- hypoxanthine
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pharmacokinetic
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guanylate
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allograft
- xanthosine
- mizoribine
- phosphoribosyltransferase
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pharmacodynamic
- ribonucleotide
- tacrolimus
- dgtp
- benzamide
- tad
- dihydrofolate
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hypoxanthine-guanine
- pigmentosa
- riboside
- 6-mercaptopurine
- thiopurine
- parvum
- glucuronide
- adenylosuccinate
- azathioprine
- cryptosporidium
- calcineurin
- sirolimus
- 6-thioguanine
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antileukemic
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predose
- diagnostics
-
oncolytic
-
enteric-coated
- analysis
- hgprt
-
c-nucleoside
-
amido
- tritrichomonas
- drug development
- pharmacology
- medicine
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.1.1.205
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RECOMMENDED NAME
GeneOntology No.
IMP dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
IMP + NAD+ + H2O = XMP + NADH + H+
enzyme acts on the hydroxyl group of the hydrated derivative of the substrate, ordered bi-bi mechanism; IMP binds first, followed by NAD+, NADH dissociates from the ternary complex first, then XMP is released
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IMP + NAD+ + H2O = XMP + NADH + H+
IMP and K+ can bind randomly to the free enzyme, while NAD+ does not react unless K+ or both K+ and IMP are present on the enzyme; mechanism is partially random
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IMP + NAD+ + H2O = XMP + NADH + H+
enzyme acts on the hydroxyl group of the hydrated derivative of the substrate, ordered bi-bi mechanism
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IMP + NAD+ + H2O = XMP + NADH + H+
IMP binds first, XMP is released last; ordered sequential mechanism
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IMP + NAD+ + H2O = XMP + NADH + H+
ordered sequential mechanism; sequential addition of IMP, NAD+ and K+
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IMP + NAD+ + H2O = XMP + NADH + H+
substrate binding and catalytic reaction mechanism, Cys319 is the catalytic residue, NAD+ promotes the nucleophilic attack of Cys319 on IMP
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IMP + NAD+ + H2O = XMP + NADH + H+
covalent enzyme reaction intermediate, hydrolysis of enzyme-XMP is rate-limiting and requires the adoption of the closed conformation, Arg418 is involved in the reaction mechanism as catalytic base, Thr321 is involved in both hydride transfer and hydrolysis
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IMP + NAD+ + H2O = XMP + NADH + H+
Arg418 is involved in the reaction mechanism as catalytic base
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IMP + NAD+ + H2O = XMP + NADH + H+
reaction and kinetic mechanism, an Arg residue is involved in catalysis as general base
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IMP + NAD+ + H2O = XMP + NADH + H+
reaction and kinetic mechanism, an Arg residue is involved in catalysis as general base, Cys319-linked covalent enzyme intermediate E-XMP
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IMP + NAD+ + H2O = XMP + NADH + H+
reaction in two steps via covalent interemediate state, the catalytic residue is Cys334
IMP + NAD+ + H2O = XMP + NADH + H+
the IMPDH reaction involves two chemical transformations. First, the catalytic Cys attacks IMP, and hydride is transferred to NAD to form the covalent intermediate E-XMP*. In the second step, E-XMP* is hydrolyzed to produce XMP
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IMP + NAD+ + H2O = XMP + NADH + H+
the IMPDH reaction involves two chemical transformations. First, the catalytic Cys attacks IMP, and hydride is transferred to NAD to form the covalent intermediate E-XMP*. In the second step, E-XMP* is hydrolyzed to produce XMP
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IMP + NAD+ + H2O = XMP + NADH + H+
the IMPDH reaction involves two chemical transformations. First, the catalytic Cys attacks IMP, and hydride is transferred to NAD to form the covalent intermediate E-XMP*. In the second step, E-XMP* is hydrolyzed to produce XMP
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IMP + NAD+ + H2O = XMP + NADH + H+
the IMPDH reaction involves two chemical transformations. First, the catalytic Cys attacks IMP, and hydride is transferred to NAD to form the covalent intermediate E-XMP*. In the second step, E-XMP* is hydrolyzed to produce XMP
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IMP + NAD+ + H2O = XMP + NADH + H+
the enzymatic mechanism of IMPDH consists two steps, a dehydrogenase and a hydrolase reaction. Upon binding of IMP and NAD+ cofactor, a thioimidate enzyme-substrate adduct, E-XMP*, is formed via a covalent bond to the catalytic C341 with concurrent production of NADH. Hydride transfer occurs to the pro-S position with the cofactor in the anti-conformation. The cofactor is released and an active site mobile flap moves into the NAD+ site and facilitates E-XMP* hydrolysis with a conserved R443 acting as a general base. The enzyme has two distinct conformations, an open form for the dehydrogenase reaction and a closed form for E-XMP* hydrolysis
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IMP + NAD+ + H2O = XMP + NADH + H+
a steady-state ordered Bi Bi kinetic mechanism in which IMP binds first followed by NAD+, and product release is ordered. Hydride transfer appears not to be rate-limiting. The pH-rate profile indicates one deprotonated group essential for catalysis
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IMP + NAD+ + H2O = XMP + NADH + H+
reaction in two steps via covalent interemediate state, the catalytic residue is Cys334
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IMP + NAD+ + H2O = XMP + NADH + H+
a steady-state ordered Bi Bi kinetic mechanism in which IMP binds first followed by NAD+, and product release is ordered. Hydride transfer appears not to be rate-limiting. The pH-rate profile indicates one deprotonated group essential for catalysis; the enzymatic mechanism of IMPDH consists two steps, a dehydrogenase and a hydrolase reaction. Upon binding of IMP and NAD+ cofactor, a thioimidate enzyme-substrate adduct, E-XMP*, is formed via a covalent bond to the catalytic C341 with concurrent production of NADH. Hydride transfer occurs to the pro-S position with the cofactor in the anti-conformation. The cofactor is released and an active site mobile flap moves into the NAD+ site and facilitates E-XMP* hydrolysis with a conserved R443 acting as a general base. The enzyme has two distinct conformations, an open form for the dehydrogenase reaction and a closed form for E-XMP* hydrolysis
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IMP + NAD+ + H2O = XMP + NADH + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
IMP:NAD+ oxidoreductase
The enzyme acts on the hydroxy group of the hydrated derivative of the substrate.
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CAS REGISTRY NUMBER
COMMENTARY
9028-93-7
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
vero cell-line infected with vaccina virus and parainfluenza virus type 3 strain C243
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MMRL2651, subtype naturally resistant to inhibition by mycophenolic acid
UniProt
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serotype 2, SS2, strain ZY05719 is isolated from diseased pigs in Sichuan Province, China, in 2005
UniProt
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347911, 347919, 347929, 347934, 347939, 347941, 347961, 667473, 689055, 701583, 703193, 704629, 705494, 711735
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347905, 347912, 347916, 347918, 347931, 347960, 347961, 347962, 347965, 667966, 668295, 668351, 669800, 669807, 670881, 688258, 688266, 689095, 690045, 701583, 702243, 703271, 703272, 706090, 706815, 706817, 711518, 712578
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type 1 enzyme, retinal-specific isoforms IMPDH1(546) and IMPDH1(595) and canonical isoform IMPDH1(514)
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serotype 2, SS2, strain ZY05719 is isolated from diseased pigs in Sichuan Province, China, in 2005
UniProt
large splicing variant IMPDH; strains RH and RHDELTATHX, opportunistic apicomplexan parasite, two splicing variants, a short and a large one; short splicing variant IMPDH-S; strains RH and RHDELTATHX, opportunistiuc apicomplexan parasite, two splicing variants, a short and a large one
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
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comparison of enzyme activity and purine metabolite concentration in erythrocytes and plasma from a non-diving mammal (domestic pig) than from diving mammals (river otter and northern elephant seal). IMPDH activity in erythrocytes from domestic pig, Sus scrofa, is higher than that of erythrocytes from river otter, Lontra longicaudis annectens, and northern elephant seal, Mirounga angustirostris. IMPDH activities as well as HX, IMP, XMP and guanine (GDP and GTP), and adenine (AMP, ADP and ATP) nucleotides concentrations in plasma and erythrocytes from diving mammals are lower than those from a non-diving mammal
evolution
comparison of enzyme activity and purine metabolite concentration in erythrocytes and plasma from a non-diving mammal (domestic pig) than from diving mammals (river otter and northern elephant seal). IMPDH activity in erythrocytes from domestic pig, Sus scrofa, is higher than that of erythrocytes from river otter, Lontra longicaudis annectens, and northern elephant seal, Mirounga angustirostris. IMPDH activities as well as HX, IMP, XMP and guanine (GDP and GTP), and adenine (AMP, ADP and ATP) nucleotides concentrations in plasma and erythrocytes from diving mammals are lower than those from a non-diving mammal
evolution
Lontra longicaudis annectens
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comparison of enzyme activity and purine metabolite concentration in erythrocytes and plasma from a non-diving mammal (domestic pig) than from diving mammals (river otter and northern elephant seal). IMPDH activity in erythrocytes from domestic pig, Sus scrofa, is higher than that of erythrocytes from river otter, Lontra longicaudis annectens, and northern elephant seal, Mirounga angustirostris. IMPDH activities as well as HX, IMP, XMP and guanine (GDP and GTP), and adenine (AMP, ADP and ATP) nucleotides concentrations in plasma and erythrocytes from diving mammals are lower than those from a non-diving mammal
evolution
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classification of bacterial IMPDHs according to the regulation of their catalytic properties and their quaternary structures. Class I IMPDHs are cooperative enzymes for IMP, which are activated by MgATP2- and are octameric in all tested conditions. On the other hand, class II IMPDHs behave as Michaelis-Menten enzymes for both substrates and are tetramers in their apo state or in the presence of IMP, which are shifted to octamers in the presence of NAD+ or MgATP2-
evolution
classification of bacterial IMPDHs according to the regulation of their catalytic properties and their quaternary structures. Class I IMPDHs are cooperative enzymes for IMP, which are activated by MgATP2- and are octameric in all tested conditions. On the other hand, class II IMPDHs behave as Michaelis-Menten enzymes for both substrates and are tetramers in their apo state or in the presence of IMP, which are shifted to octamers in the presence of NAD+ or MgATP2-
evolution
C3EVF8
classification of bacterial IMPDHs according to the regulation of their catalytic properties and their quaternary structures. Class I IMPDHs are cooperative enzymes for IMP, which are activated by MgATP and are octameric in all tested conditions. On the other hand, class II IMPDHs behave as Michaelis-Menten enzymes for both substrates and are tetramers in their apo state or in the presence of IMP, which are shifted to octamers in the presence of NAD+ or MgATP
evolution
classification of bacterial IMPDHs according to the regulation of their catalytic properties and their quaternary structures. Class I IMPDHs are cooperative enzymes for IMP, which are activated by MgATP and are octameric in all tested conditions. On the other hand, class II IMPDHs behave as Michaelis-Menten enzymes for both substrates and are tetramers in their apo state or in the presence of IMP, which are shifted to octamers in the presence of NAD+ or MgATP
evolution
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classification of bacterial IMPDHs according to the regulation of their catalytic properties and their quaternary structures. Class I IMPDHs are cooperative enzymes for IMP, which are activated by MgATP2- and are octameric in all tested conditions. On the other hand, class II IMPDHs behave as Michaelis-Menten enzymes for both substrates and are tetramers in their apo state or in the presence of IMP, which are shifted to octamers in the presence of NAD+ or MgATP2-
evolution
classification of bacterial IMPDHs according to the regulation of their catalytic properties and their quaternary structures. Class I IMPDHs are cooperative enzymes for IMP, which are activated by MgATP2- and are octameric in all tested conditions. On the other hand, class II IMPDHs behave as Michaelis-Menten enzymes for both substrates and are tetramers in their apo state or in the presence of IMP, which are shifted to octamers in the presence of NAD+ or MgATP2-
evolution
classification of bacterial IMPDHs according to the regulation of their catalytic properties and their quaternary structures. Class I IMPDHs are cooperative enzymes for IMP, which are activated by MgATP2- and are octameric in all tested conditions. On the other hand, class II IMPDHs behave as Michaelis-Menten enzymes for both substrates and are tetramers in their apo state or in the presence of IMP, which are shifted to octamers in the presence of NAD+ or MgATP2-
evolution
classification of bacterial IMPDHs according to the regulation of their catalytic properties and their quaternary structures. Class I IMPDHs are cooperative enzymes for IMP, which are activated by MgATP2- and are octameric in all tested conditions. On the other hand, class II IMPDHs behave as Michaelis-Menten enzymes for both substrates and are tetramers in their apo state or in the presence of IMP, which are shifted to octamers in the presence of NAD+ or MgATP2-
evolution
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classification of bacterial IMPDHs according to the regulation of their catalytic properties and their quaternary structures. Class I IMPDHs are cooperative enzymes for IMP, which are activated by MgATP2- and are octameric in all tested conditions. On the other hand, class II IMPDHs behave as Michaelis-Menten enzymes for both substrates and are tetramers in their apo state or in the presence of IMP, which are shifted to octamers in the presence of NAD+ or MgATP2-
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evolution
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classification of bacterial IMPDHs according to the regulation of their catalytic properties and their quaternary structures. Class I IMPDHs are cooperative enzymes for IMP, which are activated by MgATP and are octameric in all tested conditions. On the other hand, class II IMPDHs behave as Michaelis-Menten enzymes for both substrates and are tetramers in their apo state or in the presence of IMP, which are shifted to octamers in the presence of NAD+ or MgATP
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evolution
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classification of bacterial IMPDHs according to the regulation of their catalytic properties and their quaternary structures. Class I IMPDHs are cooperative enzymes for IMP, which are activated by MgATP2- and are octameric in all tested conditions. On the other hand, class II IMPDHs behave as Michaelis-Menten enzymes for both substrates and are tetramers in their apo state or in the presence of IMP, which are shifted to octamers in the presence of NAD+ or MgATP2-
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evolution
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classification of bacterial IMPDHs according to the regulation of their catalytic properties and their quaternary structures. Class I IMPDHs are cooperative enzymes for IMP, which are activated by MgATP2- and are octameric in all tested conditions. On the other hand, class II IMPDHs behave as Michaelis-Menten enzymes for both substrates and are tetramers in their apo state or in the presence of IMP, which are shifted to octamers in the presence of NAD+ or MgATP2-
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evolution
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classification of bacterial IMPDHs according to the regulation of their catalytic properties and their quaternary structures. Class I IMPDHs are cooperative enzymes for IMP, which are activated by MgATP2- and are octameric in all tested conditions. On the other hand, class II IMPDHs behave as Michaelis-Menten enzymes for both substrates and are tetramers in their apo state or in the presence of IMP, which are shifted to octamers in the presence of NAD+ or MgATP2-
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malfunction
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a guanine-prototrophic Escherichia coli strain, MP101, is constructed with the cystathionine beta-synthase subdomain deleted from the chromosomal gene for IMPDH. The ATP content is substantially elevated in mutant strain MP101 whereas the GTP content is slighty reduced. The activities of IMPDH, adenylosuccinate synthetase and GMP reductase are 2 to 3fold lower in MP101 crude extracts compared with wild-type strain. Results of a comparative analysis of the purine nucleotide pools, fluxes and turnover rates in the mutant and wild-type strains, indicate that the cystathionine beta-synthase subdomain of IMPDH plays an important role in the regulation of purine nucleotide metabolism
malfunction
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mice that are homozygotic knockouts for the gene that encodes the type 2 isozyme die in early embryonic stages, despite presumptive expression of a functional type 1 isozyme and purine salvage enzymes
malfunction
overexpression of the IMPDH gene increases the metabolic flux through the guanine pathway and ultimately enhances 40% riboflavin production with respect to the wild-type. IMPDH disruption results in a 100fold increase of inosine excretion to the culture media
malfunction
IMPDH enzyme deletion leads to suppression of the glycolytic pathway enzymes triosephosphate isomerase (TPI) and glyceraldehyde phosphate dehydrogenase (GAPDH). The adhesion to host cells is the crucial step to cause infection for the pathogen, and reduction of adhesion of the IMPDH deletion mutant strain to some extent causes the attenuated virulence of the IMPDH deletion mutant strain in pigs, reduced adhesion ofthe mutant strain to PK15 and HEp-2 cells
malfunction
IMPDH inhibitors ribavirin and mycophenolic acid prevents cell growth and generates an apoptosis-like phenotype in sub-populations of L.eishmania amazonensis promastigotes. A subpopulation of parasites undergoes apoptosislike cell death in the nutrient poor environment of the vector gut
malfunction
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the inhibition of IMPDH leads to the depletion of the guanine nucleotide pool, which blocks proliferation
malfunction
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the inhibition of IMPDH leads to the depletion of the guanine nucleotide pool, which blocks proliferation
malfunction
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the inhibition of IMPDH leads to the depletion of the guanine nucleotide pool, which blocks proliferation
malfunction
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the inhibition of IMPDH leads to the depletion of the guanine nucleotide pool, which blocks proliferation
malfunction
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inhibition of IMPDH causes an overall reduction in guanine nucleotide pools and, as phosphoribosyl pyrophosphate (PRPP) synthetase and ribonucleotide reductase are allosterically regulated by these nucleotides, it may affect several metabolic pathways
malfunction
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overexpression of the IMPDH gene increases the metabolic flux through the guanine pathway and ultimately enhances 40% riboflavin production with respect to the wild-type. IMPDH disruption results in a 100fold increase of inosine excretion to the culture media
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malfunction
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inhibition of IMPDH causes an overall reduction in guanine nucleotide pools and, as phosphoribosyl pyrophosphate (PRPP) synthetase and ribonucleotide reductase are allosterically regulated by these nucleotides, it may affect several metabolic pathways
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malfunction
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IMPDH enzyme deletion leads to suppression of the glycolytic pathway enzymes triosephosphate isomerase (TPI) and glyceraldehyde phosphate dehydrogenase (GAPDH). The adhesion to host cells is the crucial step to cause infection for the pathogen, and reduction of adhesion of the IMPDH deletion mutant strain to some extent causes the attenuated virulence of the IMPDH deletion mutant strain in pigs, reduced adhesion ofthe mutant strain to PK15 and HEp-2 cells
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metabolism
isiform IMPDH2 undergoes time-dependent proteolysis with the protease-sensitive region mapping within the catalytic domain. Both IMPDH1 and IMPDH2 proteins show reduced proteolysis with pre-incubation of IMP. The presence of AMP results in significant protection of IMPDH2, via a mechanism involving conformational changes upon nucleotide binding to the Bateman domain without affecting catalytic activity; isoform IMPDH1 undergoes time-dependent proteolysis with the protease-sensitive region mapping within the catalytic domain. Both IMPDH1 and IMPDH2 proteins show reduced proteolysis with pre-incubation of IMP. The presence of ATP results in significant protection of IMPDH1, via a mechanism involving conformational changes upon nucleotide binding to the Bateman domain without affecting catalytic activity. Mutation R224P, responsible for retinitis pigmentosa, abolishes ATP binding and nucleotide protection and this correlates with an altered propensity to cluster
metabolism
the enzyme inosine-5'-monophosphate dehydrogenase (IMPDH) catalyzes the rate-limiting step in the guanine nucleotide de novo biosynthetic pathway and plays a key role in controlling the cellular nucleotide pools. The enzyme, UniProt ID AER117W, is the only one responsible for the IMPDH activity in Ashbya gossypiis
metabolism
IMPDH is a key enzyme in the purine nucleotide pathway
metabolism
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the enzyme catalyzes the first and rate-limiting step in guanine nucleotide biosynthesis
metabolism
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the enzyme catalyzes the first and rate-limiting step in guanine nucleotide biosynthesis
metabolism
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the enzyme catalyzes the first and rate-limiting step in guanine nucleotide biosynthesis
metabolism
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the enzyme catalyzes the first and rate-limiting step in guanine nucleotide biosynthesis
metabolism
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the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP
metabolism
the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP
metabolism
C3EVF8
the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP
metabolism
the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP
metabolism
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the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP
metabolism
the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP
metabolism
the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP
metabolism
the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP
metabolism
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the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP
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metabolism
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the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP
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metabolism
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the enzyme inosine-5'-monophosphate dehydrogenase (IMPDH) catalyzes the rate-limiting step in the guanine nucleotide de novo biosynthetic pathway and plays a key role in controlling the cellular nucleotide pools. The enzyme, UniProt ID AER117W, is the only one responsible for the IMPDH activity in Ashbya gossypiis
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metabolism
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the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP
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metabolism
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the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP
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metabolism
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the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP
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physiological function
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IMPDH activity is required for differentiation of preadipocytes into mature, lipid-laden adipocytes and maintenance of adipose tissue mass
physiological function
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mutations in the CBS subdomain of IMPDH1 account for 2-3% of autosomal dominant retinitis pigmentosa
physiological function
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the Bateman domain of IMPDH is a negative trans-regulator of adenylate nucleotide synthesis, whereby this role is independent of the catalytic function of IMPDH in the de novo GMP biosynthesis
physiological function
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is a key enzyme in the biosynthesis of purine nucleotides
physiological function
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is a key enzyme in the biosynthesis of purine nucleotides
physiological function
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is a key enzyme in the biosynthesis of purine nucleotides
physiological function
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is a key enzyme in the biosynthesis of purine nucleotides; is a key enzyme in the biosynthesis of purine nucleotides. Mutations in the type I gene cause the RP10 form of autosomal dominant retinitis pigmentosa
physiological function
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is a key enzyme in the biosynthesis of purine nucleotides
physiological function
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is a key enzyme in the biosynthesis of purine nucleotides. Loss of both alleles of the type 2 gene results in very early embryonic lethality. Type I enzymatic activity appears not to be essential for normal mouse development or fertility
physiological function
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is a key enzyme in the biosynthesis of purine nucleotides
physiological function
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is a key enzyme in the biosynthesis of purine nucleotides
physiological function
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is a key enzyme in the biosynthesis of purine nucleotides
physiological function
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is a key enzyme in the biosynthesis of purine nucleotides
physiological function
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is a key enzyme in the biosynthesis of purine nucleotides
physiological function
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presence of rs11706052 polymorphism reduces the antiproliferative effect of mycophenolic acid on lymphocytes by approximately 50% compared with the IMPDH2 wild-type form at therapeutic relevant concentrations of 10 microM/l and 25 microM/l
physiological function
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IMPDH is recruited to transcription complex through serine 2 phosphorylation of RNA polymerase II C-terminal domain. Subunit Imd2 genetically interacts with Ctk1 kinase. IMPDH is recruited to elongating RNA polymerase II only when serine 2 of the C-terminal domain is phosphorylated by Ctk1 kinase. Loss of Imd2 has little effect on the association of most elongation factors with RNA polymerase II. In cells lacking Imd2 or all the essential IMPDHs in the presence of minimal guanine, a defect in the association of Ctk1 kinase with the promoter region is seen
physiological function
heterologous expression of IMP dehydrogenase gene mpaF dramatically increases mycophenolic acid resistance in Aspergillus nidulans, which does not produce mycophenolic acid.The growth of an Aspergillus nidulans strain expressing mpaF is only marginally affected by mycophenolic acid at concentrations as high as 200 microg/ml
physiological function
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rate-limiting enzyme in the de novo purine biosynthetic pathway leading to the formation of guanine ribonucleotides
physiological function
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the key metabolic enzyme inosine-50-monophosphate dehydrogenase (IMPDH) occupies a central role in the de novo synthesis of guanosine nucleotides. The binding of Mg-ATP to Pseudomonas aeruginosa IMPDH and its crucial role in the regulation of the catalytic activity of the enzyme and its quaternary structure
physiological function
the enzyme inosine-5'-monophosphate dehydrogenase (IMPDH) catalyzes the rate-limiting step in the guanine nucleotide de novo biosynthetic pathway and plays a key role in controlling the cellular nucleotide pools. IMPDH is an important metabolic bottleneck in the guanine nucleotide synthesis. Guanine nucleotides are essential for cell viability
physiological function
a small percentage of Leishmania amazonensis undergoes programmed cell death (PCD) under heat shock, imitating host infection reaction, involving the enzyme IMPDH of the purine metabolism. Enzyme IMPDH is a key enzyme in the purine nucleotide pathway, and is related to cell growth and apoptosis
physiological function
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inosine monophosphate dehydrogenase (IMPDH), a key enzyme leading to GMP and GTP biosynthesis. Rod and ring (RR) formation from IMP dehydrogenase is regulated through the one-carbon metabolic pathway. RR formation is induced by IMPDH inhibitors as well as glutamine deprivation. Because RR assembly occurs when guanine nucleotide biosynthesis is inhibited, and because RRs rapidly disassemble after the addition of guanine nucleotide precursors, RR formation might be an adaptive homeostatic mechanism, allowing IMPDH to sense changes in the one-carbon folate pathway, detailed overview
physiological function
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the enzyme catalyzes a crucial step in the de novo synthesis of guanine nucleotides. It oxidizes inosine 5'-monophosphate (IMP) to xanthosine 5'-monophosphate (XMP) in a nicotinamide adenine dinucleotide (NAD+)-dependent manner. The enzyme has a critical position in the purine biosynthesis pathway
physiological function
IMPDH functional regulation, overview
physiological function
IMPDH functional regulation, overview
physiological function
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the enzyme IMPDH2 catalyzes the conversion of inosine 5'-monophosphate into xanthosine 5'-monophosphate with the concomitant reduction of NAD+ to NADH and controls flux into the guanine nucleotide pool
physiological function
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the enzyme inosine-5'-monophosphate dehydrogenase (IMPDH) catalyzes the rate-limiting step in the guanine nucleotide de novo biosynthetic pathway and plays a key role in controlling the cellular nucleotide pools. IMPDH is an important metabolic bottleneck in the guanine nucleotide synthesis. Guanine nucleotides are essential for cell viability
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physiological function
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rate-limiting enzyme in the de novo purine biosynthetic pathway leading to the formation of guanine ribonucleotides
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physiological function
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IMPDH functional regulation, overview
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physiological function
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the enzyme IMPDH2 catalyzes the conversion of inosine 5'-monophosphate into xanthosine 5'-monophosphate with the concomitant reduction of NAD+ to NADH and controls flux into the guanine nucleotide pool
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additional information
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three conserved loops seem to be key players in the allosteric regulation of enzyme activity as they connect the tetramer-tetramer interface with the active site and show significant modification upon substrate binding, mechanism for the allosteric regulation of IMPDH through the CBS motifs. Conerved residue Asp199 is involved in the recognition of the ribose moiety of ATP in IMPDHpa. Structure analysis of wild-type and mutant enzymes, overview
additional information
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substrate-binding siteinvolving Cys219 and Met302-Gly303, modelling, overview
additional information
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Ashbya gossypii is a natural riboflavin superproducer
additional information
Ashbya gossypii is a natural riboflavin superproducer
additional information
-
the enzyme has two essential but mutually exclusive conformations, an open conformation that accommodates both the substrate and cofactor during the dehydrogenase step, and a closed conformation where a mobile flap (referred to as the active site flap) moves into the cofactor-binding site for the hydrolysis of E-XMP*
additional information
-
the enzyme has two essential but mutually exclusive conformations, an open conformation that accommodates both the substrate and cofactor during the dehydrogenase step, and a closed conformation where a mobile flap (referred to as the active site flap) moves into the cofactor-binding site for the hydrolysis of E-XMP*
additional information
-
the enzyme has two essential but mutually exclusive conformations, an open conformation that accommodates both the substrate and cofactor during the dehydrogenase step, and a closed conformation where a mobile flap (referred to as the active site flap) moves into the cofactor-binding site for the hydrolysis of E-XMP*
additional information
-
the enzyme has two essential but mutually exclusive conformations, an open conformation that accommodates both the substrate and cofactor during the dehydrogenase step, and a closed conformation where a mobile flap (referred to as the active site flap) moves into the cofactor-binding site for the hydrolysis of E-XMP*
additional information
-
siRNA knockdown of serine hydroxymethyltransferase-2, SHMT2, or dihydrofolate reductase, DHFR, leads to increased rod and ring (RR) formation. IMPDH-containing RR structures can form in mammalian cells
additional information
-
IMPDH shares a two-domain organization composed of one catalytic domain, a (beta/alpha)8 barrel, and a smaller flanking domain, containing two CBS modules, forming together the Bateman domain, model for the quaternary structure modulation
additional information
IMPDH shares a two-domain organization composed of one catalytic domain, a (beta/alpha)8 barrel, and a smaller flanking domain, containing two CBS modules, forming together the so-called Bateman domain, model for the quaternary structure modulation
additional information
C3EVF8
IMPDH shares a two-domain organization composed of one catalytic domain, a (beta/alpha)8 barrel, and a smaller flanking domain, containing two CBS modules, forming together the so-called Bateman domain, model for the quaternary structure modulation
additional information
IMPDH shares a two-domain organization composed of one catalytic domain, a (beta/alpha)8 barrel, and a smaller flanking domain, containing two CBS modules, forming together the so-called Bateman domain, model for the quaternary structure modulation
additional information
-
IMPDH shares a two-domain organization composed of one catalytic domain, a (beta/alpha)8 barrel, and a smaller flanking domain, containing two CBS modules, forming together the so-called Bateman domain, model for the quaternary structure modulation
additional information
IMPDH shares a two-domain organization composed of one catalytic domain, a (beta/alpha)8 barrel, and a smaller flanking domain, containing two CBS modules, forming together the so-called Bateman domain, model for the quaternary structure modulation
additional information
IMPDH shares a two-domain organization composed of one catalytic domain, a (beta/alpha)8 barrel, and a smaller flanking domain, containing two CBS modules, forming together the Bateman domain, model for the quaternary structure modulation
additional information
IMPDH shares a two-domain organization composed of one catalytic domain, a (beta/alpha)8 barrel, and a smaller flanking domain, containing two CBS modules, forming together the so-called Bateman domain, model for the quaternary structure modulation
additional information
-
determination of XMP and NAD+ substrate binding structures, overview. Active site structures of wild-type apo-enzyme and of CBS domain-deleted enzyme mutant MtbIMPDH2DELTACBS in apoform
additional information
-
IMPDH shares a two-domain organization composed of one catalytic domain, a (beta/alpha)8 barrel, and a smaller flanking domain, containing two CBS modules, forming together the Bateman domain, model for the quaternary structure modulation
-
additional information
-
IMPDH shares a two-domain organization composed of one catalytic domain, a (beta/alpha)8 barrel, and a smaller flanking domain, containing two CBS modules, forming together the so-called Bateman domain, model for the quaternary structure modulation
-
additional information
-
substrate-binding siteinvolving Cys219 and Met302-Gly303, modelling, overview
-
additional information
-
Ashbya gossypii is a natural riboflavin superproducer
-
additional information
-
IMPDH shares a two-domain organization composed of one catalytic domain, a (beta/alpha)8 barrel, and a smaller flanking domain, containing two CBS modules, forming together the so-called Bateman domain, model for the quaternary structure modulation
-
additional information
-
IMPDH shares a two-domain organization composed of one catalytic domain, a (beta/alpha)8 barrel, and a smaller flanking domain, containing two CBS modules, forming together the so-called Bateman domain, model for the quaternary structure modulation
-
additional information
-
determination of XMP and NAD+ substrate binding structures, overview. Active site structures of wild-type apo-enzyme and of CBS domain-deleted enzyme mutant MtbIMPDH2DELTACBS in apoform
-
additional information
-
IMPDH shares a two-domain organization composed of one catalytic domain, a (beta/alpha)8 barrel, and a smaller flanking domain, containing two CBS modules, forming together the so-called Bateman domain, model for the quaternary structure modulation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
5'-amino-5'-deoxyinosine 5'-N-phosphate + NAD+ + H2O
5'-amino-5'-deoxyxanthosine 5'-N-phosphate + NADH
-
-
-
-
?
5'-mercapto-5'-deoxyinosine 5'-S-phosphate + NAD+ + H2O
5'-mercapto-5'-deoxyxanthosine 5'-phosphate + NADH
-
-
-
-
?
6-thioinosine 5'-phosphate + NAD+ + H2O
6-thioxanthosine 5'-phosphate + NADH
-
-
-
-
?
inosine + NAD+ + H2O
xanthosine + NADH
-
8% of the rate with inosine 5'-phosphate
-
-
?
inosine 5'-diphosphate + NAD+ + H2O
xanthosine 5'-diphosphate + NADH
-
-
-
-
?
inosine 5'-phosphate + 3-acetylpyridine adenine dinucleotide + H2O
xanthosine 5'-phosphate + reduced 3-acetylpyridine adenine dinucleotide
-
-
-
-
?
inosine 5'-phosphate + acetylpyridine adenine dinucleotide + H2O
xanthosine 5'-phosphate + reduced acetylpyridine adenine dinucleotide
inosine 5'-phosphorothioate + NAD+ + H2O
xanthosine 5'-phosphorothioate + NADH
-
-
-
-
?
inosine 5'-triphosphate + NAD+ + H2O
xanthosine 5'-triphosphate + NADH
-
-
-
-
?
IMP + NAD+ + H2O
XMP + NADH + H+
-
rate-limiting enzyme in the de novo purine biosynthetic pathway leading to the formation of guanine ribonucleotides
-
-
?
IMP + NAD+ + H2O
XMP + NADH + H+
-
rate-limiting enzyme in the de novo purine biosynthetic pathway leading to the formation of guanine ribonucleotides
-
-
?
IMP + NAD+ + H2O
XMP + NADH + H+
-
-
-
?
inosine 5'-diphosphate + NAD+ + H2O
xanthosine 5'-diphosphate + NADH + H+
-
-
-
?
inosine 5'-diphosphate + NAD+ + H2O
xanthosine 5'-diphosphate + NADH + H+
-
-
-
?
inosine 5'-diphosphate + NAD+ + H2O
xanthosine 5'-diphosphate + NADH + H+
-
-
-
-
?
inosine 5'-diphosphate + NAD+ + H2O
xanthosine 5'-diphosphate + NADH + H+
-
-
-
-
?
inosine 5'-diphosphate + NAD+ + H2O
xanthosine 5'-diphosphate + NADH + H+
-
xanthosine 5'-diphosphate is the only product
-
?
inosine 5'-phosphate + acetylpyridine adenine dinucleotide + H2O
xanthosine 5'-phosphate + reduced acetylpyridine adenine dinucleotide
-
-
-
-
?
inosine 5'-phosphate + acetylpyridine adenine dinucleotide + H2O
xanthosine 5'-phosphate + reduced acetylpyridine adenine dinucleotide
-
-
-
-
?
inosine 5'-phosphate + NAD+
xanthosine 5'-phosphate + NADH + H+
-
-
-
?
inosine 5'-phosphate + NAD+
xanthosine 5'-phosphate + NADH + H+
-
-
-
-
?
inosine 5'-phosphate + NAD+
xanthosine 5'-phosphate + NADH + H+
-
-
-
-
?
inosine 5'-phosphate + NAD+
xanthosine 5'-phosphate + NADH + H+
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
subdomain of the enzyme is not required for catalytic activity
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
r
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
the enzyme is important for the synthesis of guanine nucleotides
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
-
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
ir
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
rate-limiting step of the de novo guanine nucleotide biosynthesis
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
ir
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
rate-limiting step of the de novo guanine nucleotide biosynthesis
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
rate-limiting step of the de novo guanine nucleotide biosynthesis
-
-
ir
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
the enzyme performs the rate-limiting step in guanine nucleotide biosynthesis
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
-
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
ir
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
obligatory step in biosynthesis of nucleic acid guanine
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
enzyme is highly specific for both inosine 5'-phosphate and NAD+
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
Parainfluenza virus
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
Parainfluenza virus
-
rate-limiting step of the de novo guanine nucleotide biosynthesis, pathway overview
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
enzyme linked to proliferation and malignancy
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
rate-limiting step of the de novo guanine nucleotide biosynthesis
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
ir
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
the reaction is irreversible over the range of pH 5.5 to pH 8.8, step in guanylic acid biosynthesis
-
-
ir
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
the reaction is irreversible over the range of pH 5.5 to pH 8.8
-
-
ir
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
r
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
rate-limiting step of the de novo guanine nucleotide biosynthesis
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
rate-limiting step of the de novo guanine nucleotide biosynthesis, pathway overview
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
rate-limiting step of the de novo guanine nucleotide biosynthesis, pathway overview
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
IMP oxidation is the predominant metabolic route leading to ureide synthesis
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
IMPDH catalyzes a dehydrogenase reaction and a hydrolysis reaction, a redox step producing NADH and the covalent intermediate E-xanthosine 5'-monophosphate and a hydrolysis step that produces xanthosine 5'-monophosphate. The enzyme toggles between the open conformation required for the dehydrogenase reaction and the closed conformation of the hydrolase reaction by moving a mobile flap into the NAD site. The dehydrogenase and hydrolase reactions display significant differences in the host (Homo sapiens) and parasite (Cryptosporidium parvum) enzymes, in keeping with the phylogenetic and structural divergence of their active sites
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
IMPDH catalyzes a dehydrogenase reaction and a hydrolysis reaction, a redox step producing NADH and the covalent intermediate E-xanthosine 5'-monophosphate* and a hydrolysis step that produces xanthosine 5'-monophosphate. The enzyme toggles between the open conformation required for the dehydrogenase reaction and the closed conformation of the hydrolase reaction by moving a mobile flap into the NAD site. The dehydrogenase and hydrolase reactions display significant differences in the host (Homo sapiens) and parasite (Cryptosporidium parvum) enzymes, in keeping with the phylogenetic and structural divergence of their active sites
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
-
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
-
-
-
?
additional information
?
-
-
IMP-enzyme binding structure analysis, overview
-
-
-
additional information
?
-
-
IMP-enzyme binding structure analysis, overview
-
-
-
additional information
?
-
-
IMP-enzyme binding structure analysis, overview
-
-
-
additional information
?
-
-
the enzyme binds both RNA and DNA in vitro and in vivo
-
-
-
additional information
?
-
-
the CBS subdomain of IMPDH coordinately regulates the adenine and guanine nucleotide pool
-
-
-
additional information
?
-
-
enzyme inhibition by mycophenolic acid impairs maturation and function of dendritic cells due to low GTP levels and reduced expression of CD80, CD40, CD86, CD54, and CD83 in dendritic cells, accompanied by a decreased capacity to stimulate T-lymphocytes
-
-
-
additional information
?
-
enzyme mutations are involved in autosomal dominant retinitis pigmentosa, pathological mechanism, overview
-
-
-
additional information
?
-
-
increased activities of IMP DH and GMP synthase and in the elevated concentrations of guanylates in hepatomas and other tumor cells
-
-
-
additional information
?
-
-
inhibition of the enzyme in K562 cells sensitizes the before resistant cells to methotrexate
-
-
-
additional information
?
-
-
isozyme IMPDH-1 is essential for T lymphocyte development, enzyme inhibitor mycophenolic acid inhibits tumor-associated angiogenesis
-
-
-
additional information
?
-
-
the enzyme is rate-limiting in the de novo synthesis of guanine nucleotides
-
-
-
additional information
?
-
ssDNA and RNA binding of wild-type and mutant IMPDH1s
-
-
-
additional information
?
-
-
the enzyme binds both RNA and DNA in vitro and in vivo
-
-
-
additional information
?
-
-
the enzyme interacts with GTP which leads to formation of linear arrays, GTP reverses the enzyme aggregation by inhibitor mycophenolic acid
-
-
-
additional information
?
-
-
assay method optimization. XMP detection and quantification by anion exchange chromatography
-
-
-
additional information
?
-
-
increased activities of IMP DH and GMP synthase and in the elevated concentrations of guanylates in hepatomas and other tumor cells
-
-
-
additional information
?
-
the parasite damages fetuses in utero and threatens immunocompromized individuals
-
-
-
additional information
?
-
-
the parasite damages fetuses in utero and threatens immunocompromized individuals
-
-
-
additional information
?
-
-
the enzyme binds both RNA and DNA in vitro and in vivo
-
-
-
additional information
?
-
-
IMP- and XMP-enzyme binding structure analysis, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
IMP + NAD+ + H2O
XMP + NADH + H+
-
rate-limiting enzyme in the de novo purine biosynthetic pathway leading to the formation of guanine ribonucleotides
-
-
?
IMP + NAD+ + H2O
XMP + NADH + H+
-
rate-limiting enzyme in the de novo purine biosynthetic pathway leading to the formation of guanine ribonucleotides
-
-
?
IMP + NAD+ + H2O
XMP + NADH + H+
Q5ZUR9
-
-
-
?
inosine 5'-diphosphate + NAD+ + H2O
xanthosine 5'-diphosphate + NADH + H+
I3WTS0
-
-
-
?
inosine 5'-diphosphate + NAD+ + H2O
xanthosine 5'-diphosphate + NADH + H+
Q387Q3
-
xanthosine 5'-diphosphate is the only product
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
subdomain of the enzyme is not required for catalytic activity
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
Q59Q46
-
-
-
r
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
the enzyme is important for the synthesis of guanine nucleotides
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
rate-limiting step of the de novo guanine nucleotide biosynthesis
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
rate-limiting step of the de novo guanine nucleotide biosynthesis
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
rate-limiting step of the de novo guanine nucleotide biosynthesis
-
-
ir
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
P20839
the enzyme performs the rate-limiting step in guanine nucleotide biosynthesis
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
obligatory step in biosynthesis of nucleic acid guanine
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
Parainfluenza virus
-
rate-limiting step of the de novo guanine nucleotide biosynthesis, pathway overview
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
enzyme linked to proliferation and malignancy
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
rate-limiting step of the de novo guanine nucleotide biosynthesis
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
the reaction is irreversible over the range of pH 5.5 to pH 8.8, step in guanylic acid biosynthesis
-
-
ir
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
Q4VRV8
-
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
-
-
-
r
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
rate-limiting step of the de novo guanine nucleotide biosynthesis
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
rate-limiting step of the de novo guanine nucleotide biosynthesis, pathway overview
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
rate-limiting step of the de novo guanine nucleotide biosynthesis, pathway overview
-
-
?
inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH
-
IMP oxidation is the predominant metabolic route leading to ureide synthesis
-
-
?
additional information
?
-
-
enzyme inhibition by mycophenolic acid impairs maturation and function of dendritic cells due to low GTP levels and reduced expression of CD80, CD40, CD86, CD54, and CD83 in dendritic cells, accompanied by a decreased capacity to stimulate T-lymphocytes
-
-
-
additional information
?
-
P20839
enzyme mutations are involved in autosomal dominant retinitis pigmentosa, pathological mechanism, overview
-
-
-
additional information
?
-
-
increased activities of IMP DH and GMP synthase and in the elevated concentrations of guanylates in hepatomas and other tumor cells
-
-
-
additional information
?
-
-
inhibition of the enzyme in K562 cells sensitizes the before resistant cells to methotrexate
-
-
-
additional information
?
-
-
isozyme IMPDH-1 is essential for T lymphocyte development, enzyme inhibitor mycophenolic acid inhibits tumor-associated angiogenesis
-
-
-
additional information
?
-
-
the enzyme is rate-limiting in the de novo synthesis of guanine nucleotides
-
-
-
additional information
?
-
-
increased activities of IMP DH and GMP synthase and in the elevated concentrations of guanylates in hepatomas and other tumor cells
-
-
-
additional information
?
-
Q4VRV8
the parasite damages fetuses in utero and threatens immunocompromized individuals
-
-
-
additional information
?
-
-
the parasite damages fetuses in utero and threatens immunocompromized individuals
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-acetylpyridine adenine dinucleotide
-
the NAD+ analog 3-acetylpyridine adenine dinucleotide (APAD+) is a substrate for MtIMPDH and the dependence of velocity on increasing concentrations of APAD+ (Fig. 4B) also displayed substrate inhibition
NAD+
-
B-sided stereospecificity: 2-3H of IMP is transferred to pro-S position of carbon atom C-4 of the nicotinamide ring in NAD+
NAD+
-
B-sided stereospecificity: 2-3H of IMP is transferred to pro-S position of carbon atom C-4 of the nicotinamide ring in NAD+
NAD+
-
; preferred cofactor, NADP+ shows poor activity, less that 10% compared to NAD+
NAD+
-
NAD+ promotes the nucleophilic attack of Cys319 on IMP, the NAD+ site may be an exploitable target for the design of antimicrobial drugs
NAD+
-
-
NAD+
-
-
NAD+
-
comparison between the NAD+ binding sites of human IMPDHs and Mycobacterium tuberculosis IMPDH; comparison between the NAD+ binding sites of human IMPDHs and Mycobacterium tuberculosis IMPDH
NAD+
-
comparison between the NAD+ binding-sites of human IMPDHs and Mycobacterium tuberculosis IMPDH
NAD+
-
-
347905, 347912, 347916, 347918, 347931, 667473, 667508, 667921, 667935, 667937, 667965, 667980, 668351, 670881, 701583, 702243, 703271, 706815, 706817, 740794, 740808
NAD+
-
dependent on, binding structure to CBS domain-deleted enzyme mutant of MtbIMPDH2DELTACBS
NAD+
-
groups with pK values of 7.5 and 9.0 are important for NAD+ binding
additional information
-
involvement of three conserved water molecules (W(L), W(M), and W(C)) in the recognition of catalytic residues (R 322, D 364, and N 303) to cofactor
-
additional information
-
the enzyme shows a clear preference for NAD+ over NADP+, since it loses more than 95% activity when using the latter as co-substrate
-
additional information
the enzyme shows a clear preference for NAD+ over NADP+, since it loses more than 95% activity when using the latter as co-substrate
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cs+
K+
MgATP2-
Na+
NaCl
-
activity at 2 M NaCl is more than 4fold higher than that in the absence of salt
NH4+
Rb+
Tl+
additional information
K+
-
enhances inosine 5'-phosphate bound at a stoichiometry of four sites per tetramer and the affinity of the type 2 isozyme by 2fold
K+
-
strong activation, the K+ site is observed at the subunit interface, the activation is linked to NAD+
K+
-
activates, Km: 1.6 mM, the activation is competitively inhibited by Mg2+; activation; K+ activation is inhibited by Mg2+
MgATP2-
has a positive effector of IMPDHpa acting on the maximal rate and on the affinity for IMP. The positive effector binds onto the two CBS modules, with consequences on the global shape
MgATP2-
-
MgATP2- has no effect on the catalytic activity of class II IMPDHsa, but has a role in the modulation of the quaternary structure of class II IMPDHs
MgATP2-
MgATP2- has a drastic impact on the kinetic properties of class I IMPDHs. It increases the thermostability of the enzyme, is a positive effector for the cooperative class I IMPDH IMPDHpp
MgATP2-
a positive effector for the cooperative class I IMPDH IMPDHnm
MgATP2-
-
allosteric regulation of Pseudomonas aeruginosa IMPDH by MgATP2-
MgATP2-
MgATP2- has no effect on the catalytic activity of class II IMPDHsa, but has a role in the modulation of the quaternary structure of class II IMPDHs
additional information
MgATP has no significant effect on the catalytic activity of IMPDHbt
additional information
-
inosine 5'-phosphate binding is not altered by K+
additional information
-
the enzyme activity is dependent on the presence of a monovalent cation, preferaby K+. Neither Na+ nor Li+, which have lower ionic radii than K+, activate the MtIMPDH. Divalent cations, such as Mg2+ and Ca2+, do not activate the enzyme even at 200 mM
additional information
-
influence of various metal ions on enzyme activity
additional information
-
100-800 mM K+ does not affect the R418A mutant activity
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,2R,3R,5S)-2,3,5-trihydroxy-5-(propylcarbamoyl)cyclohexyl (4E)-6-[4-(acetyloxy)-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl]-4-methylhex-4-enoate
-
;
(2-[acetyl[(2E)-4-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-2-methylbut-2-en-1-yl]amino]ethyl)phosphonic acid
-
isozyme IMPDH II IC50: 785 nM
(2-[formyl[(2E)-4-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-2-methylbut-2-en-1-yl]amino]ethyl)phosphonic acid
-
isozyme IMPDH II IC50: 749 nM
(2-[[(2E)-4-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-2-methylbut-2-en-1-yl](methyl)amino]ethyl)phosphonic acid
-
isozyme IMPDH II IC50: above 0.001 mM
(2-[[(2E)-4-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-2-methylbut-2-en-1-yl](methylsulfonyl)amino]ethyl)phosphonic acid
-
isozyme IMPDH II IC50: 498 nM
(2-[[(2E)-4-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-2-methylbut-2-en-1-yl](sulfamoyl)amino]ethyl)phosphonic acid
-
isozyme IMPDH II IC50: 93 nM
(2-[[(2E)-4-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-2-methylbut-2-en-1-yl]amino]ethyl)phosphonic acid
-
isozyme IMPDH II IC50: 499 nM
(2-[[(2E)-4-(6-ethyl-4-hydroxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-2-methylbut-2-en-1-yl](methyl)amino]ethyl)phosphonic acid
-
isozyme IMPDH II IC50: 132 nM
(2-[[(2E)-4-(6-ethyl-4-hydroxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-2-methylbut-2-en-1-yl](methylsulfonyl)amino]ethyl)phosphonic acid
-
isozyme IMPDH II IC50: 68 nM
(2-[[(2E)-4-(6-ethyl-4-hydroxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-2-methylbut-2-en-1-yl](sulfamoyl)amino]ethyl)phosphonic acid
-
isozyme IMPDH II IC50: 24 nM
(2-[[(2E)-4-(6-ethyl-4-hydroxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-2-methylbut-2-en-1-yl]amino]ethyl)phosphonic acid
-
isozyme IMPDH II IC50: 13 nM
(2E)-3-furan-2-yl-N-[4-(4-methyl-1,3-oxazol-5-yl)phenyl]prop-2-enamide
-
isozyme IMPDH II IC50: 0.002 mM
(2E)-3-{3-[N''-cyano-N'-(4-cyano-3-methoxyphenyl)carbamimidamido]phenyl}prop-2-enoic acid
-
-
(2E)-4-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-2-methylbut-2-enal
-
;
(2E)-4-[4-(acetyloxy)-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl]-2-methylbut-2-enoic acid
-
;
(2E)-4-{6-methoxy-7-methyl-3-oxo-4-[2-(trimethylsilyl)ethoxy]-1,3-dihydro-2-benzofuran-5-yl}-2-methylbut-2-enal
-
;
(2E)-N-hydroxy-3-[3-({[3-methoxy-4-(1,3-oxazol-5-yl)phenyl]carbamoyl}amino)phenyl]prop-2-enamide
-
;
(2E)-N-hydroxy-3-[4-({[3-methoxy-4-(1,3-oxazol-5-yl)phenyl]carbamoyl}amino)phenyl]prop-2-enamide
-
;
(2R)-1-cyanobutan-2-yl [(1S)-1-(3-{[(2,3-dihydro-1-benzofuran-7-yl)carbamoyl]amino}phenyl)ethyl]carbamate
-
-
(2R)-1-cyanobutan-2-yl [(1S)-1-(3-{[(2-acetyl-1-methyl-2,3-dihydro-1H-benzimidazol-4-yl)carbamoyl]amino}phenyl)ethyl]carbamate
-
-
(2R)-1-cyanobutan-2-yl [(1S)-1-(3-{[(2-methoxyquinoxalin-5-yl)carbamoyl]amino}phenyl)ethyl]carbamate
-
-
(2R)-1-cyanobutan-2-yl [(1S)-1-(3-{[(2-methyl-4-oxo-3,4-dihydro-2H-1-benzopyran-6-yl)carbamoyl]amino}phenyl)ethyl]carbamate
-
-
(2R)-1-cyanobutan-2-yl [(1S)-1-(3-{[(2H-1,3-benzodioxol-5-yl)carbamoyl]amino}phenyl)ethyl]carbamate
-
-
(2R)-1-cyanobutan-2-yl [(1S)-1-(3-{[(3,4-dimethoxybenzene-1-sulfonyl)carbamoyl]amino}phenyl)ethyl]carbamate
-
-
(2R)-1-cyanobutan-2-yl [(1S)-1-(3-{[(3-methoxy-4-methylphenyl)carbamoyl]amino}phenyl)ethyl]carbamate
-
-
(2R)-1-cyanobutan-2-yl [(1S)-1-(3-{[(3-methoxyquinoxalin-5-yl)carbamoyl]amino}phenyl)ethyl]carbamate
-
-
(2R)-1-cyanobutan-2-yl [(1S)-1-(3-{[(4-cyano-3-methoxyphenyl)carbamoyl]amino}phenyl)ethyl]carbamate
-
i.e. VX-4997
(2R)-1-cyanobutan-2-yl [(1S)-1-(3-{[(4-methyl-2,3-dihydro-1-benzofuran-6-yl)carbamoyl]amino}phenyl)ethyl]carbamate
-
-
(2R)-1-cyanobutan-2-yl [(1S)-1-(3-{[(4-oxo-3,4-dihydro-2H-1-benzopyran-6-yl)carbamoyl]amino}phenyl)ethyl]carbamate
-
-
(2R)-1-cyanobutan-2-yl [(1S)-1-(3-{[(5,6-dihydro-1,4-dioxin-2-yl)carbamoyl]amino}phenyl)ethyl]carbamate
-
-
(2R)-1-cyanobutan-2-yl [(1S)-1-(3-{[(6,7-dimethoxynaphthalen-1-yl)carbamoyl]amino}phenyl)ethyl]carbamate
-
-
(2R)-1-cyanobutan-2-yl [(1S)-1-(3-{[(E)-1-(3,4-dimethoxyanilino)-2-nitroethenyl]amino}phenyl)ethyl]carbamate
-
-
(2R)-1-cyanobutan-2-yl [(1S)-1-(3-{[(E)-1-(4-cyano-3-methoxyanilino)-2-nitroethenyl]amino}phenyl)ethyl]carbamate
-
-
(2R)-1-cyanobutan-2-yl [(1S)-1-(3-{[4-(4-cyano-3-methoxyphenyl)piperazine-1-carbonyl]amino}phenyl)ethyl]carbamate
-
-
(2R)-1-cyanobutan-2-yl [(1S)-1-(3-{[5-(4-cyano-3-methoxyphenyl)-1H-benzimidazol-2-yl]amino}phenyl)ethyl]carbamate
-
-
(2R)-1-cyanobutan-2-yl [(1S)-1-(3-{[6-(4-cyano-3-methoxyphenyl)pyrazine-2-carbonyl]amino}phenyl)ethyl]carbamate
-
-
(2R)-1-cyanobutan-2-yl [(1S)-1-{3-[2-(3,4-dimethoxyphenoxy)acetamido]phenyl}ethyl]carbamate
-
-
(2R)-1-cyanobutan-2-yl [(1S)-1-{3-[2-(4-cyano-3-methoxyphenoxy)acetamido]phenyl}ethyl]carbamate
-
-
(2R)-1-cyanobutan-2-yl [(1S)-1-{3-[3-(4-cyano-3-methoxyphenyl)-2,4-dioxoimidazolidin-1-yl]phenyl}ethyl]carbamate
-
-
(2R)-1-cyanobutan-2-yl [(1S)-1-{3-[N'-(3,4-dimethoxyphenyl)carbamimidamido]phenyl}ethyl]carbamate
-
-
(2R)-1-cyanobutan-2-yl {(1S)-1-[3-({[3-methoxy-4-(1,3-oxazol-5-yl)phenyl]carbamoyl}amino)phenyl]ethyl}carbamate
-
-
(2R)-1-cyanobutan-2-yl {(1S)-1-[3-({[3-methoxy-4-(morpholin-4-yl)phenyl]carbamoyl}amino)phenyl]ethyl}carbamate
-
-
(2R)-1-cyanobutan-2-yl {(1S)-1-[3-({[3-methoxy-4-(oxan-4-yl)phenyl]carbamoyl}amino)phenyl]ethyl}carbamate
-
-
(2R)-1-cyanobutan-2-yl {(1S)-1-[3-({[4-(3,6-dihydro-2H-pyran-4-yl)-3-methoxyphenyl]carbamoyl}amino)phenyl]ethyl}carbamate
-
-
(2R)-1-cyanobutan-2-yl-[(1S)-1-(3-{[(3,4-dimethoxyphenyl)carbamoyl]amino}phenyl)-ethyl] carbamate
-
-
(2R)-2-phenyl-N-[2-(pyridin-4-yl)-1,3-benzoxazol-5-yl]propanamide
-
-
(2S)-1-cyanobutan-2-yl [(1R)-1-(3-{[(3,4-dimethoxyphenyl)carbamothioyl]amino}phenyl)ethyl]carbamate
-
-
(2S)-1-cyanobutan-2-yl [(1R)-1-(3-{[(4-cyano-3-methoxyphenyl)carbamothioyl]amino}phenyl)ethyl]carbamate
-
-
(2S)-1-cyanobutan-2-yl [(1R)-1-{3-[N''-cyano-N'-(4-cyano-3,5-dimethoxyphenyl)carbamimidamido]phenyl}ethyl]carbamate
-
-
(2S)-1-cyanobutan-2-yl [(1R)-1-{3-[N'-(3,4,5-trimethoxyphenyl)carbamimidamido]phenyl}ethyl]carbamate
-
-
(2S)-1-cyanobutan-2-yl [(1R)-1-{3-[N'-(4-cyano-3,5-dimethoxyphenyl)carbamimidamido]phenyl}ethyl]carbamate
-
-
(2S)-2-(2,3-dichlorophenoxy)-N-[2-(pyridin-4-yl)-1,3-benzoxazol-5-yl]propanamide
-
-
(2S)-2-(2,3-dichlorophenoxy)-N-[2-(pyridin-4-yl)-1,3-benzoxazol-6-yl]propanamide
-
-
(2S)-2-(2,3-dimethoxyphenoxy)-N-[2-(pyridin-4-yl)-1,3-benzoxazol-5-yl]propanamide
-
-
(2S)-2-(2-chloro-3-nitrophenoxy)-N-[2-(pyridin-4-yl)-1,3-benzoxazol-5-yl]propanamide
-
-
(2S)-2-(2-chlorophenoxy)-N-[2-(pyridin-4-yl)-1,3-benzoxazol-5-yl]propanamide
-
-
(2S)-2-[(1-naphthyl)amino]-N-[2-(pyridin-4-yl)-1,3-benzoxazol-5-yl]propanamide
-
competitive versus NAD+
(2S)-2-[(3,4-dichlorophenyl)amino]-N-[2-(pyridin-4-yl)-1,3-benzoxazol-5-yl]propanamide
-
competitive versus NAD+, displays excellent IMPDH inhibitory activity and moderate stability in mouse liver microsomes
(3aR,4R,6S,7aR)-6-hydroxy-2,2-dimethyl-6-(propylcarbamoyl)hexahydro-2H-1,3-benzodioxol-4-yl (4E)-6-[4-(acetyloxy)-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl]-4-methylhex-4-enoate
-
;
(3aR,4R,7S,8aR)-7-hydroxy-2,2-dimethyltetrahydro-2H-4,7-methano[1,3]dioxolo[4,5-c]oxepin-6(4H)-one
-
;
(3aR,5R,7R,7aS)-5,7-dihydroxy-2,2-dimethyl-N-propylhexahydro-2H-1,3-benzodioxole-5-carboxamide
-
;
(3S)-oxolan-3-yl {[3-({[3-methoxy-4-(1,3-oxazol-5-yl)phenyl]carbamoyl}amino)phenyl]methyl}carbamate
(3S,4E)-6-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-3,4-dimethylhex-4-enoic acid
-
;
(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)acetaldehyde
-
;
(4E)-6-(4,6-dihydroxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-4-methylhex-4-enoic acid
derivative of mycophenolic acid. IC50 value for K562 cells proliferation 8.2 microM; derivative of mycophenolic acid. IC50 value for K562 cells proliferation 8.2 microM
(4E)-6-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-4-methyl-N-(1,3,4-thiadiazol-2-yl)hex-4-enamide}
-
(4E)-6-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-4-methyl-N-(1,3-thiazol-2-yl)hex-4-enamide}
-
(4E)-6-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-4-methyl-N-(1H-1,2,4-triazol-5-yl)hex-4-enamide
-
;
(4E)-6-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-4-methyl-N-(1H-1,2,4-triazol-5-yl)hex-4-enamide}
-
(4E)-6-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-4-methyl-N-(1H-tetrazol-5-yl)hex-4-enamide}
-
(4E)-6-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-4-methyl-N-(4H-1,2,4-triazol-4-yl)hex-4-enamide}
-
(4E)-6-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-4-methyl-N-(pyridin-2-yl)hex-4-enamide}
-
(4E)-6-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-4-methyl-N-{[(1-nitro-4a,9a-dihydroacridin-9-yl)amino]methyl}hex-4-enamide
-
;
(4E)-6-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-4-methyl-N-{[(4-nitro-9-oxo-4a,9,9a,10-tetrahydroacridin-1-yl)amino]methyl}hex-4-enamide
-
;
(4E)-6-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-4-methylhex-4-enal
-
;
(4E)-6-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-4-methylhex-4-enamide
-
;
(4E)-6-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-4-methylhex-4-enethioic S-acid}
-
(4E)-6-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-4-methylhex-4-enoic acid
-
;
(4E)-6-[4-(acetyloxy)-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl]-4-methylhex-4-enoic acid
derivative of mycophenolic acid. IC50 value for K562 cells proliferation 0.59 microM; derivative of mycophenolic acid. IC50 value for K562 cells proliferation 0.59 microM
(4E)-N-hydroxy-6-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-4-methylhex-4-enamide
(4E)-N-hydroxy-6-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-4-methylhex-4-enamide}
-
(5E)-N-hydroxy-7-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-5-methylhept-5-enamide
-
comparison with inhibition of histone deacetylase and K562 cell proliferation
([[(2E)-4-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-2-methylbut-2-en-1-yl]oxy]methyl)phosphonic acid
-
isozyme IMPDH II IC50: 246 nM
([[(2E)-4-(6-ethyl-4-hydroxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-2-methylbut-2-en-1-yl]oxy]methyl)phosphonic acid
-
isozyme IMPDH II IC50: 23 nM
({hydroxy[2-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)ethoxy]phosphoryl}methyl)phosphonic acid
-
;
1-(2,2-dimethylpropanoyl)-7'-methoxy-3'-methyl-6'-(1,3-oxazol-5-yl)-1'H-spiro[pyrrolidine-3,2'-quinazolin]-4'(3'H)-one
-
IC50: 0.094 mM, isozyme IMPDH II
1-(2-[3-[(1E)-N-hydroxyethanimidoyl]phenyl]propan-2-yl)-3-quinolin-7-ylurea
-
displays high potency against Cryptosporidium parvum IMPDH, more than 1000fold selectivity versus human IMPDH type 2 and good stability in mouse liver microsomes
1-(3-methylphenyl)-3-[4-(1,3-oxazol-5-yl)phenyl]urea
-
isozyme IMPDH II IC50: 640 nM
1-(4-chloro-5-nitrocyclohexa-1,5-dien-1-yl)-3-(2-[3-[(1E)-N-hydroxyethanimidoyl]phenyl]propan-2-yl)urea
-
displays high potency against Cryptosporidium parvum IMPDH, more than 1000fold selectivity versus human IMPDH type 2 and good stability in mouse liver microsomes
1-tert-butyl 5-methyl (3R,5R)-7'-methoxy-3'-methyl-6'-(1,3-oxazol-5-yl)-4'-oxo-3',4'-dihydro-1H,1'H-spiro[pyrrolidine-3,2'-quinazoline]-1,5-dicarboxylate
-
IC50: 35 nM, isozyme IMPDH II
1-tert-butyl 5-methyl (3R,5S)-7'-methoxy-3'-methyl-6'-(1,3-oxazol-5-yl)-4'-oxo-3',4'-dihydro-1H,1'H-spiro[pyrrolidine-3,2'-quinazoline]-1,5-dicarboxylate
-
IC50: 948 nM, isozyme IMPDH II
1-tert-butyl 5-methyl (3S,5R)-7'-methoxy-3'-methyl-6'-(1,3-oxazol-5-yl)-4'-oxo-3',4'-dihydro-1H,1'H-spiro[pyrrolidine-3,2'-quinazoline]-1,5-dicarboxylate
-
IC50: 35 nM, isozyme IMPDH II
1-tert-butyl 5-methyl (3S,5S)-7'-methoxy-3'-methyl-6'-(1,3-oxazol-5-yl)-4'-oxo-3',4'-dihydro-1H,1'H-spiro[pyrrolidine-3,2'-quinazoline]-1,5-dicarboxylate
-
26% inhibition at 10 micromol, isozyme IMPDH II
1-[2-[3-(prop-1-en-2-yl)phenyl]propan-2-yl]-3-quinolin-7-ylurea
-
displays high potency against Cryptosporidium parvum IMPDH, more than 1000fold selectivity versus human IMPDH type 2 and good stability in mouse liver microsomes
1-[3-chloro-4-(1,3-oxazol-5-yl)phenyl]-3-(3-methylphenyl)urea
-
isozyme IMPDH II IC50: 43 nM
1-[3-methoxy-4-(1,3-oxazol-5-yl)phenyl]-3-(3-methylphenyl)urea
-
isozyme IMPDH II IC50: 19 nM
1-[4-(4-methyl-1,3-oxazol-5-yl)phenyl]-3-(3-methylphenyl)urea
-
isozyme IMPDH II IC50: 500 nM
1-{5-O-[hydroxy({hydroxy[2-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)ethoxy]phosphoryl}methyl)phosphoryl]-beta-D-ribofuranosyl}-1H-benzimidazol-4-amine
-
;
14,16-dihydroxy-3,8-dimethyl-3,4,5,6,9,10-hexahydro-1H-2-benzoxacyclotetradecine-1,7(8H)-dione
inhibition of leukemia K562 cells proliferation, IC50 of 71.3 microM
2'-methylthiazole-4-carboxamide adenine dinucleotide
-
noncompetitive inhibition, less cytotoxic against K562 tumor cells
2-(1,3-oxazol-5-yl)-5-[(5-phenyl-1,3-oxazol-2-yl)amino]phenol
-
isozyme IMPDH II IC50: 0.0016 mM
2-(1-benzothiophen-3-yl)-6-methoxy-5-(1,3-oxazol-2-yl)-1H-indole-3-carbaldehyde
-
-
2-(1-benzothiophen-3-yl)-6-methoxy-5-(1,3-oxazol-5-yl)-1H-indole-3-carbaldehyde
-
;
2-(2,4-dichlorophenoxy)-N-[2-(pyridin-2-yl)-1,3-benzoxazol-5-yl]propanamide
-
-
2-(2-chlorophenoxy)-N-[2-(pyridin-4-yl)-1,3-benzoxazol-5-yl]propanamide
-
-
2-(4-methoxyphenoxy)-N-[2-(pyridin-4-yl)-1,3-benzoxazol-5-yl]propanamide
-
-
2-(dimethylamino)-7-methoxy-6-(1,3-oxazol-5-yl)quinolin-4(1H)-one
-
isozyme IMPDH II IC50: 200 nM
2-(methyl{2-[(2lambda~5~-triaza-1,2-dien-2-yl)acetyl]phenyl}amino)-2-oxoethyl acetate
-
;
2-benzyl-7-methoxy-6-(1,3-oxazol-5-yl)quinolin-4(1H)-one
-
isozyme IMPDH II IC50: 180 nM
2-beta-D-ribofuranosylthiazole-4-carboxamide 5'-phosphate
-
RTC monophosphate
2-chloro-5-[[(2-[3-[(1Z)-N-hydroxyethanimidoyl]phenyl]propan-2-yl)carbamoyl]amino]-N,N-dimethylbenzamide
-
-
2-chloro-5-[[(2-[3-[(1Z)-N-hydroxyethanimidoyl]phenyl]propan-2-yl)carbamoyl]amino]benzamide
-
-
2-chloro-N,N-diethyl-5-[[(2-[3-[(1Z)-N-hydroxyethanimidoyl]phenyl]propan-2-yl)carbamoyl]amino]benzamide
-
-
2-chloro-N,N-dimethyl-5-[([2-[3-(prop-1-en-2-yl)phenyl]propan-2-yl]carbamoyl)amino]benzamide
-
noncompetitive inhibitor, that has similar affinity to both E-IMP and E-XMP, enzyme binding structure analysis, overview
2-chloro-N-methyl-5-[[[1-methyl-1-[3-(1-methylethenyl)phenyl]ethyl]amino]carbonyl]aminobenzamide
-
2-cyano-1-[3-methoxy-4-(1,3-oxazol-5-yl)phenyl]-3-phenylguanidine
-
isozyme IMPDH II IC50: 240 nM
2-ethyl-5'-O-[hydroxy({hydroxy[2-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)ethoxy]phosphoryl}methyl)phosphoryl]adenosine
-
;
2-ethyl-9-[5-O-[hydroxy(2-[hydroxy[2-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)ethoxy]phosphoryl]ethyl)phosphoryl]-beta-L-ribofuranosyl]-9H-purin-6-amine
inhibition of leukemia K562 cells proliferation, IC50 of 4.0 microM; inhibition of leukemia K562 cells proliferation, IC50 of 4.0 microM
2-furan-3-yl-7-methoxy-6-(1,3-oxazol-5-yl)quinolin-4(1H)-one
-
isozyme IMPDH II IC50: 32 nM
2-hydroxy-N-[2-(2-[[3-methoxy-4-(1,3-oxazol-4-yl)phenyl]amino]-1,3-oxazol-5-yl)phenyl]-N-methylacetamide
-
isozyme IMPDH II IC50: 41 nM
2-tert-butyl-7-methoxy-6-(1,3-oxazol-5-yl)quinolin-4(1H)-one
-
isozyme IMPDH II IC50: 0.01 mM
2-[(2-{2-[3-methoxy-4-(1,3-oxazol-5-yl)anilino]-1,3-oxazol-5-yl}phenyl)(methyl)amino]-2-oxoethyl acetate
-
;
2-[(3,4-dichlorophenyl)amino]-N-[2-(pyridin-4-yl)-1,3-benzoxazol-5-yl]propanamide
-
racemic variant, competitive versus NAD+. Compound displays good antiparasitic activity in a Toxoplasma gondii strain that relies on Cryptosporidium parvum IMPDH, EC50 20 nM. No toxicity is observed against four mammalian cells lines
2-[(3-ethyl-4-oxo-3,4-dihydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]-N-(4-methoxyphenyl)acetamide
2-[2-(Z)-fluorovinyl]-inosine 5'-phosphate
-
is a time-dependent inactivator
2-[methyl[2-(2-[[3-(1,3-oxazol-5-yl)-1H-indol-6-yl]amino]-1,3-oxazol-5-yl)phenyl]amino]-2-oxoethyl acetate
-
;
3'-methylthiazole-4-carboxamide adenine dinucleotide
-
noncompetitive inhibition, less cytotoxic against K562 tumor cells
3'-[N''-cyano-N'-(4-cyano-3-methoxyphenyl)carbamimidamido][1,1'-biphenyl]-3-carboxylic acid
-
-
3-(2-{2-[3-methoxy-4-(1,3-oxazol-5-yl)anilino]-1,3-oxazol-5-yl}phenyl)-1-(morpholin-4-yl)butan-2-one
-
i.e. BMS-337197
3-cyanoindole-based inhibitors
-
synthesis and initial structure–activity relationships of 3-cyanoindole-based inhibitors with isozyme IMPDH II, IC50: 33-420 nM, comparison to other inhibitor structural classes, overview
-
3-hydroxy-N-methyl-N-[2-(2-[[3-methyl-4-(1,3-oxazol-5-yl)phenyl]amino]-1,3-oxazol-5-yl)phenyl]propanamide
-
isozyme IMPDH II IC50: 100 nM
3-hydroxy-N-[2-(2-[[3-methoxy-4-(1,3-oxazol-5-yl)phenyl]amino]-1,3-oxazol-5-yl)phenyl]-N-methylpropanamide
-
isozyme IMPDH II IC50: 21 nM
3-phenyl quinolone derivatives
-
several, isozyme IMPDH II IC50: 5-160 nM, overview
-
3-{3-[N''-cyano-N'-(4-cyano-3-methoxyphenyl)carbamimidamido]phenyl}propanoic acid
-
-