Activating Compound | Comment | Organism | Structure |
---|---|---|---|
MgATP2- | a positive effector for the cooperative class I IMPDH IMPDHnm | Neisseria meningitidis | |
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 | Bacillus anthracis | |
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 | Legionella pneumophila subsp. pneumophila | |
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 | Klebsiella pneumoniae | |
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 | Staphylococcus aureus | |
additional information | MgATP has no significant effect on the catalytic activity of IMPDHbt. The ATP analogue ATP-gamma-AmNS does not bind to enzyme IMPDHbt | Burkholderia thailandensis |
Cloned (Comment) | Organism |
---|---|
gene A1S_3321, sequence comparisons, functional recombinant overexpression of the His-tagged soluble enzyme in Escherichia coli strain BL21(DE3)/pDIA17, the enzyme forms a turbid solution, regardless of the protein concentration or buffer composition | Acinetobacter baumannii |
gene guaB, sequence comparisons, functional recombinant overexpression of the His-tagged soluble enzyme in Escherichia coli strain BL21(DE3)/pDIA17 | Klebsiella pneumoniae |
gene guaB, sequence comparisons, functional recombinant overexpression of the His-tagged soluble enzyme in Escherichia coli strain BL21(DE3)/pDIA17 | Bacillus thuringiensis |
gene guaB, sequence comparisons, functional recombinant overexpression of the His-tagged soluble enzyme in Escherichia coli strain BL21(DE3)/pDIA17 | Legionella pneumophila subsp. pneumophila |
gene guaB, sequence comparisons, functional recombinant overexpression of the His-tagged soluble enzyme in Escherichia coli strain BL21(DE3)/pDIA17 | Neisseria meningitidis |
gene guaB, sequence comparisons, functional recombinant overexpression of the His-tagged soluble enzyme in Escherichia coli strain BL21(DE3)/pDIA17 | Staphylococcus aureus |
gene guaB, sequence comparisons, functional recombinant overexpression of the His-tagged soluble enzyme in Escherichia coli strain BL21(DE3)/pDIA17 | Burkholderia thailandensis |
gene guaB, sequence comparisons, functional recombinant overexpression of the soluble His-tagged enzyme in Escherichia coli strain BL21(DE3)/pDIA17 | Bacillus anthracis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics | Klebsiella pneumoniae | |
additional information | - |
additional information | Michaelis-Menten kinetics | Bacillus anthracis | |
additional information | - |
additional information | Michaelis-Menten kinetics | Staphylococcus aureus | |
additional information | - |
additional information | Michaelis-Menten kinetics | Burkholderia thailandensis | |
additional information | - |
additional information | enzyme IMPDHnm exhibits cooperative kinetics for IMP with MgATP2- as the positive effector | Neisseria meningitidis | |
additional information | - |
additional information | enzyme IMPDHpp exhibits cooperative kinetics for IMP with MgATP2- as the positive effector | Legionella pneumophila subsp. pneumophila | |
0.039 | - |
IMP | pH 10.0, 30°C, recombinant enzyme, with MgATP2- | Legionella pneumophila subsp. pneumophila | |
0.039 | - |
IMP | pH 8.0, 30°C, recombinant enzyme, with MgATP | Burkholderia thailandensis | |
0.05 | - |
IMP | pH 8.0, 30°C, recombinant enzyme, with MgATP2- | Neisseria meningitidis | |
0.052 | - |
IMP | pH 10.0, 30°C, recombinant enzyme, without MgATP2- | Legionella pneumophila subsp. pneumophila | |
0.052 | - |
IMP | pH 8.0, 30°C, recombinant enzyme, without MgATP | Burkholderia thailandensis | |
0.053 | - |
IMP | pH 8.0, 30°C, recombinant enzyme, with MgATP2- | Klebsiella pneumoniae | |
0.058 | - |
IMP | pH 8.0, 30°C, recombinant enzyme, without MgATP2- | Klebsiella pneumoniae | |
0.12 | - |
IMP | pH 8.0, 30°C, recombinant enzyme, without MgATP2- | Bacillus anthracis | |
0.148 | - |
IMP | pH 8.0, 30°C, recombinant enzyme, with MgATP2- | Bacillus anthracis | |
0.196 | - |
IMP | pH 8.0, 30°C, recombinant enzyme, without MgATP2- | Staphylococcus aureus | |
0.197 | - |
IMP | pH 8.0, 30°C, recombinant enzyme, with MgATP2- | Staphylococcus aureus | |
0.269 | - |
NAD+ | pH 8.0, 30°C, recombinant enzyme, without MgATP2- | Neisseria meningitidis | |
0.315 | - |
IMP | pH 8.0, 30°C, recombinant enzyme, without MgATP2- | Neisseria meningitidis | |
0.355 | - |
NAD+ | pH 8.0, 30°C, recombinant enzyme, without MgATP | Burkholderia thailandensis | |
0.418 | - |
NAD+ | pH 8.0, 30°C, recombinant enzyme, with MgATP | Burkholderia thailandensis | |
0.477 | - |
NAD+ | pH 8.0, 30°C, recombinant enzyme, with MgATP2- | Neisseria meningitidis | |
0.998 | - |
NAD+ | pH 10.0, 30°C, recombinant enzyme, without MgATP2- | Legionella pneumophila subsp. pneumophila | |
1.122 | - |
NAD+ | pH 8.0, 30°C, recombinant enzyme, with MgATP2- | Klebsiella pneumoniae | |
1.175 | - |
NAD+ | pH 8.0, 30°C, recombinant enzyme, without MgATP2- | Klebsiella pneumoniae | |
1.762 | - |
NAD+ | pH 10.0, 30°C, recombinant enzyme, with MgATP2- | Legionella pneumophila subsp. pneumophila | |
1.762 | - |
NAD+ | pH 8.0, 30°C, recombinant enzyme, with MgATP2- | Staphylococcus aureus | |
1.994 | - |
NAD+ | pH 8.0, 30°C, recombinant enzyme, with MgATP2- | Bacillus anthracis | |
2.209 | - |
NAD+ | pH 8.0, 30°C, recombinant enzyme, without MgATP2- | Bacillus anthracis | |
2.35 | - |
NAD+ | pH 8.0, 30°C, recombinant enzyme, without MgATP2- | Staphylococcus aureus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
K+ | required at 20-150 mM | Legionella pneumophila subsp. pneumophila | |
MgATP2- | a positive effector for the cooperative class I IMPDH IMPDHnm | Neisseria meningitidis | |
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 | Bacillus anthracis | |
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 | Legionella pneumophila subsp. pneumophila | |
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 | Klebsiella pneumoniae | |
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 | Staphylococcus aureus | |
additional information | MgATP has no significant effect on the catalytic activity of IMPDHbt | Burkholderia thailandensis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
218000 | - |
recombinant enzyme, gel filtration and analytical ultracentrifugation | Burkholderia thailandensis |
218000 | - |
recombinant tetrameric enzyme, gel filtration and analytical ultracentrifugation | Klebsiella pneumoniae |
218000 | - |
recombinant tetrameric enzyme, gel filtration and analytical ultracentrifugation | Staphylococcus aureus |
440000 | - |
recombinant enzyme, gel filtration and analytical ultracentrifugation | Legionella pneumophila subsp. pneumophila |
440000 | - |
recombinant enzyme, gel filtration and analytical ultracentrifugation | Neisseria meningitidis |
440000 | - |
recombinant octameric enzyme, gel filtration and analytical ultracentrifugation | Klebsiella pneumoniae |
440000 | - |
recombinant octameric enzyme, gel filtration and analytical ultracentrifugation | Staphylococcus aureus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
IMP + NAD+ + H2O | Klebsiella pneumoniae | - |
XMP + NADH + H+ | - |
? | |
IMP + NAD+ + H2O | Bacillus thuringiensis | - |
XMP + NADH + H+ | - |
? | |
IMP + NAD+ + H2O | Acinetobacter baumannii | - |
XMP + NADH + H+ | - |
? | |
IMP + NAD+ + H2O | Bacillus anthracis | - |
XMP + NADH + H+ | - |
? | |
IMP + NAD+ + H2O | Legionella pneumophila subsp. pneumophila | - |
XMP + NADH + H+ | - |
? | |
IMP + NAD+ + H2O | Neisseria meningitidis | - |
XMP + NADH + H+ | - |
? | |
IMP + NAD+ + H2O | Staphylococcus aureus | - |
XMP + NADH + H+ | - |
? | |
IMP + NAD+ + H2O | Burkholderia thailandensis | - |
XMP + NADH + H+ | - |
? | |
IMP + NAD+ + H2O | Staphylococcus aureus N315 | - |
XMP + NADH + H+ | - |
? | |
IMP + NAD+ + H2O | Bacillus thuringiensis BGSC 4AJ1 | - |
XMP + NADH + H+ | - |
? | |
IMP + NAD+ + H2O | Legionella pneumophila subsp. pneumophila Philadelphia 1 | - |
XMP + NADH + H+ | - |
? | |
IMP + NAD+ + H2O | Acinetobacter baumannii 5377 | - |
XMP + NADH + H+ | - |
? | |
IMP + NAD+ + H2O | Klebsiella pneumoniae 52145 | - |
XMP + NADH + H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Acinetobacter baumannii | - |
- |
- |
Acinetobacter baumannii 5377 | - |
- |
- |
Bacillus anthracis | Q81W29 | gene GBAA_0008 | - |
Bacillus thuringiensis | - |
serovar monterrey | - |
Bacillus thuringiensis BGSC 4AJ1 | - |
serovar monterrey | - |
Burkholderia thailandensis | Q2SWW9 | - |
- |
Klebsiella pneumoniae | - |
- |
- |
Klebsiella pneumoniae 52145 | - |
- |
- |
Legionella pneumophila subsp. pneumophila | Q5ZUR9 | - |
- |
Legionella pneumophila subsp. pneumophila Philadelphia 1 | Q5ZUR9 | - |
- |
Neisseria meningitidis | A1KU15 | - |
- |
Staphylococcus aureus | P99106 | - |
- |
Staphylococcus aureus N315 | P99106 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant soluble His-tagged enzyme from Escherichia coli strain BL21(DE3)/pDIA17 by nickel affinity chromatography and gel filtration | Klebsiella pneumoniae |
recombinant soluble His-tagged enzyme from Escherichia coli strain BL21(DE3)/pDIA17 by nickel affinity chromatography and gel filtration | Bacillus thuringiensis |
recombinant soluble His-tagged enzyme from Escherichia coli strain BL21(DE3)/pDIA17 by nickel affinity chromatography and gel filtration | Bacillus anthracis |
recombinant soluble His-tagged enzyme from Escherichia coli strain BL21(DE3)/pDIA17 by nickel affinity chromatography and gel filtration | Legionella pneumophila subsp. pneumophila |
recombinant soluble His-tagged enzyme from Escherichia coli strain BL21(DE3)/pDIA17 by nickel affinity chromatography and gel filtration | Neisseria meningitidis |
recombinant soluble His-tagged enzyme from Escherichia coli strain BL21(DE3)/pDIA17 by nickel affinity chromatography and gel filtration | Staphylococcus aureus |
recombinant soluble His-tagged enzyme from Escherichia coli strain BL21(DE3)/pDIA17 by nickel affinity chromatography and gel filtration | Burkholderia thailandensis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
IMP + NAD+ + H2O | - |
Klebsiella pneumoniae | XMP + NADH + H+ | - |
? | |
IMP + NAD+ + H2O | - |
Bacillus thuringiensis | XMP + NADH + H+ | - |
? | |
IMP + NAD+ + H2O | - |
Acinetobacter baumannii | XMP + NADH + H+ | - |
? | |
IMP + NAD+ + H2O | - |
Bacillus anthracis | XMP + NADH + H+ | - |
? | |
IMP + NAD+ + H2O | - |
Legionella pneumophila subsp. pneumophila | XMP + NADH + H+ | - |
? | |
IMP + NAD+ + H2O | - |
Neisseria meningitidis | XMP + NADH + H+ | - |
? | |
IMP + NAD+ + H2O | - |
Staphylococcus aureus | XMP + NADH + H+ | - |
? | |
IMP + NAD+ + H2O | - |
Burkholderia thailandensis | XMP + NADH + H+ | - |
? | |
IMP + NAD+ + H2O | - |
Staphylococcus aureus N315 | XMP + NADH + H+ | - |
? | |
IMP + NAD+ + H2O | - |
Bacillus thuringiensis BGSC 4AJ1 | XMP + NADH + H+ | - |
? | |
IMP + NAD+ + H2O | - |
Legionella pneumophila subsp. pneumophila Philadelphia 1 | XMP + NADH + H+ | - |
? | |
IMP + NAD+ + H2O | - |
Acinetobacter baumannii 5377 | XMP + NADH + H+ | - |
? | |
IMP + NAD+ + H2O | - |
Klebsiella pneumoniae 52145 | XMP + NADH + H+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | 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 | Klebsiella pneumoniae |
More | 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 | Bacillus thuringiensis |
More | 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 | Bacillus anthracis |
More | 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 | Legionella pneumophila subsp. pneumophila |
More | 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 | Neisseria meningitidis |
More | 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 | Staphylococcus aureus |
More | 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 | Burkholderia thailandensis |
octamer | - |
Legionella pneumophila subsp. pneumophila |
octamer | - |
Neisseria meningitidis |
octamer | IMPDHba is predominantly octameric. In the presence of IMP, class II IMPDHs remain tetrameric | Acinetobacter baumannii |
octamer | the quaternary structure of the second class IMPDHbt oscillates between tetramer and octamer. IMPDHba is predominantly octameric. In the presence of IMP, class II IMPDHs remain tetrameric, while in the presence of NAD, IMPDHbt is predominantly octameric | Burkholderia thailandensis |
tetramer | in the presence of IMP, class II IMPDHs remain tetrameric | Bacillus thuringiensis |
tetramer or octamer | in the case of IMPDHkp, several peaks are detected, which correspond to tetrameric species and higher oligomeric forms, multiples of tetramers, under equilibrium | Klebsiella pneumoniae |
tetramer or octamer | in the presence of NAD+, IMPDHba is predominantly octameric | Bacillus anthracis |
tetramer or octamer | the quaternary structure of the second class IMPDHsa oscillates between tetramer and octamer. Enzyme IMPDHsa is tetrameric in the apo state. In the presence of IMP, class II IMPDHs remain tetrameric | Staphylococcus aureus |
Synonyms | Comment | Organism |
---|---|---|
A1S_3321 | - |
Acinetobacter baumannii |
BTH_I2056 | - |
Burkholderia thailandensis |
class I IMPDH | - |
Legionella pneumophila subsp. pneumophila |
class I IMPDH | - |
Neisseria meningitidis |
class II IMPDH | - |
Klebsiella pneumoniae |
class II IMPDH | - |
Bacillus thuringiensis |
class II IMPDH | - |
Acinetobacter baumannii |
class II IMPDH | - |
Bacillus anthracis |
class II IMPDH | - |
Staphylococcus aureus |
class II IMPDH | - |
Burkholderia thailandensis |
DR63_268 | - |
Burkholderia thailandensis |
GBAA_0008 | - |
Bacillus anthracis |
guaB | - |
Klebsiella pneumoniae |
guaB | - |
Bacillus thuringiensis |
guaB | - |
Acinetobacter baumannii |
guaB | - |
Bacillus anthracis |
guaB | - |
Legionella pneumophila subsp. pneumophila |
guaB | - |
Neisseria meningitidis |
guaB | - |
Staphylococcus aureus |
guaB | - |
Burkholderia thailandensis |
IMPDH | - |
Klebsiella pneumoniae |
IMPDH | - |
Bacillus thuringiensis |
IMPDH | - |
Acinetobacter baumannii |
IMPDH | - |
Bacillus anthracis |
IMPDH | - |
Legionella pneumophila subsp. pneumophila |
IMPDH | - |
Neisseria meningitidis |
IMPDH | - |
Staphylococcus aureus |
IMPDH | - |
Burkholderia thailandensis |
IMPDHab | - |
Acinetobacter baumannii |
IMPDHba | - |
Bacillus anthracis |
IMPDHbt | - |
Burkholderia thailandensis |
IMPDHkp | - |
Klebsiella pneumoniae |
IMPDHlpp | - |
Legionella pneumophila subsp. pneumophila |
IMPDHnm | - |
Neisseria meningitidis |
inosine-5'-monophosphate dehydrogenase | - |
Klebsiella pneumoniae |
inosine-5'-monophosphate dehydrogenase | - |
Bacillus thuringiensis |
inosine-5'-monophosphate dehydrogenase | - |
Acinetobacter baumannii |
inosine-5'-monophosphate dehydrogenase | - |
Bacillus anthracis |
inosine-5'-monophosphate dehydrogenase | - |
Legionella pneumophila subsp. pneumophila |
inosine-5'-monophosphate dehydrogenase | - |
Neisseria meningitidis |
inosine-5'-monophosphate dehydrogenase | - |
Staphylococcus aureus |
inosine-5'-monophosphate dehydrogenase | - |
Burkholderia thailandensis |
lpg1723 | - |
Legionella pneumophila subsp. pneumophila |
NMC1103 | - |
Neisseria meningitidis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Klebsiella pneumoniae |
30 | - |
assay at | Bacillus thuringiensis |
30 | - |
assay at | Acinetobacter baumannii |
30 | - |
assay at | Bacillus anthracis |
30 | - |
assay at | Legionella pneumophila subsp. pneumophila |
30 | - |
assay at | Neisseria meningitidis |
30 | - |
assay at | Staphylococcus aureus |
30 | - |
assay at | Burkholderia thailandensis |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
49 | 67 | purified recombinant enzyme, 1 mg/mL protein in 50 mM K2HPO4, pH 9.0, 50 mM KCl, 10 min, loss of 50% activity. Addition of MgATP2- results in a significant increase of Tm value for IMPDHlpp to 67°C | Legionella pneumophila subsp. pneumophila |
71 | 78 | purified recombinant enzyme, 1 mg/mL protein in 50 mM Na2CO3, pH 9.5, KCl 100 mM, 10 min, loss of 50% activity. Addition of MgATP results in a significant increase of Tm value for IMPDHbt to 78°C | Burkholderia thailandensis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
- |
Bacillus thuringiensis |
8 | - |
- |
Acinetobacter baumannii |
8 | - |
- |
Neisseria meningitidis |
8 | - |
- |
Burkholderia thailandensis |
8.5 | - |
- |
Klebsiella pneumoniae |
9 | - |
- |
Bacillus anthracis |
9.2 | - |
- |
Staphylococcus aureus |
10 | - |
- |
Legionella pneumophila subsp. pneumophila |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Klebsiella pneumoniae | |
NAD+ | - |
Bacillus thuringiensis | |
NAD+ | - |
Acinetobacter baumannii | |
NAD+ | - |
Bacillus anthracis | |
NAD+ | - |
Legionella pneumophila subsp. pneumophila | |
NAD+ | - |
Neisseria meningitidis | |
NAD+ | - |
Staphylococcus aureus | |
NAD+ | - |
Burkholderia thailandensis |
General Information | Comment | Organism |
---|---|---|
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 | Bacillus thuringiensis |
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 | Burkholderia thailandensis |
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- | Klebsiella pneumoniae |
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- | Acinetobacter baumannii |
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- | Bacillus anthracis |
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- | Legionella pneumophila subsp. pneumophila |
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- | Neisseria meningitidis |
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- | Staphylococcus aureus |
metabolism | the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP | Klebsiella pneumoniae |
metabolism | the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP | Bacillus thuringiensis |
metabolism | the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP | Acinetobacter baumannii |
metabolism | the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP | Bacillus anthracis |
metabolism | the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP | Legionella pneumophila subsp. pneumophila |
metabolism | the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP | Neisseria meningitidis |
metabolism | the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP | Staphylococcus aureus |
metabolism | the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP | Burkholderia thailandensis |
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 | Acinetobacter baumannii |
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 | Neisseria meningitidis |
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 | Klebsiella pneumoniae |
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 | Bacillus thuringiensis |
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 | Bacillus anthracis |
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 | Legionella pneumophila subsp. pneumophila |
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 | Staphylococcus aureus |
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 | Burkholderia thailandensis |
physiological function | IMPDH functional regulation, overview | Klebsiella pneumoniae |
physiological function | IMPDH functional regulation, overview | Bacillus thuringiensis |
physiological function | IMPDH functional regulation, overview | Acinetobacter baumannii |
physiological function | IMPDH functional regulation, overview | Bacillus anthracis |
physiological function | IMPDH functional regulation, overview | Legionella pneumophila subsp. pneumophila |
physiological function | IMPDH functional regulation, overview | Neisseria meningitidis |
physiological function | IMPDH functional regulation, overview | Staphylococcus aureus |
physiological function | IMPDH functional regulation, overview | Burkholderia thailandensis |