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Literature summary for 1.1.1.205 extracted from

  • Alexandre, T.; Raynal, B.; Rayna, B.; Munier-Lehmann, H.
    Two classes of bacterial IMPDHs according to their quaternary structures and catalytic properties (2015), PLoS ONE, 10, e0116578.
    View publication on PubMedView publication on EuropePMC

Activating Compound

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(Commentary)

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 [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

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 [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/ Products (Substrates)

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

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 (Commentary)

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 and Products (Substrate)

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

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

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 [°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 [°C]

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

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

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

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