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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
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
Q81W29
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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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
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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
-
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
-
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
-
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
-
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
-
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
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
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
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
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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
defects in inosine monophosphate dehydrogenase-1 lead to insufficient biosyntheses of purine nucleotides and are believed to cause retinitis pigmentosa in eyes
malfunction
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enzyme depletion is bactericidal in vitro and ex vivo
malfunction
enzyme dysfunction leads to retinitis pigmentosa
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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malfunction
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enzyme depletion is bactericidal in vitro and ex vivo
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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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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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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
metabolism
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
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
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
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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
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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
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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
Q81W29
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
the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP
metabolism
rate-limiting enzyme for guanosine triphosphate synthesis
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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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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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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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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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
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
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
mutations in the CBS subdomain of IMPDH1 account for 2-3% of autosomal dominant retinitis pigmentosa
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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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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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
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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IMPDH functional regulation, overview
physiological function
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IMPDH functional regulation, overview
physiological function
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IMPDH functional regulation, overview
physiological function
Q81W29
IMPDH functional regulation, overview
physiological function
IMPDH functional regulation, overview
physiological function
IMPDH functional regulation, overview
physiological function
IMPDH functional regulation, overview
physiological function
IMPDH functional regulation, overview
physiological function
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
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
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
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
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
increased isoform IMPDH2 enhances RNA polymerase I and III transcription directly linking GTP metabolism to both anabolic capacity as well as nucleolar enlargement historically observed as associated with cancer. Isoform IMPDH2 has the essential function in embryogenesis that cannot be compensated by isoform IMPDH1
physiological function
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the enzyme is essential for Mycobacterium tuberculosis to establish an infection in mice
physiological function
the enzyme selectively inhibits cell and tumor growth of ASCL1Low small cell lung cancer cells
physiological function
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IMPDH functional regulation, overview
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physiological function
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IMPDH functional regulation, overview
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physiological function
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IMPDH functional regulation, overview
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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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the enzyme is essential for Mycobacterium tuberculosis to establish an infection in mice
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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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physiological function
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IMPDH functional regulation, overview
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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 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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additional information
Ashbya gossypii is a natural riboflavin superproducer
additional information
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Ashbya gossypii is a natural riboflavin superproducer
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
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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
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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 Bateman domain, model for the quaternary structure modulation
additional information
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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
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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
Q81W29
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
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
substrate-binding siteinvolving Cys219 and Met302-Gly303, modelling, overview
additional information
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substrate-binding siteinvolving Cys219 and Met302-Gly303, modelling, overview
additional information
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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
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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
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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
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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
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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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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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
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additional information
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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
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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
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additional information
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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
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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
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