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Literature summary 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

EC Number Activating Compound Comment Organism Structure
1.1.1.205 MgATP2- a positive effector for the cooperative class I IMPDH IMPDHnm Neisseria meningitidis
1.1.1.205 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
1.1.1.205 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
1.1.1.205 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
1.1.1.205 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
1.1.1.205 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)

EC Number Cloned (Comment) Organism
1.1.1.205 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
1.1.1.205 gene guaB, sequence comparisons, functional recombinant overexpression of the His-tagged soluble enzyme in Escherichia coli strain BL21(DE3)/pDIA17 Klebsiella pneumoniae
1.1.1.205 gene guaB, sequence comparisons, functional recombinant overexpression of the His-tagged soluble enzyme in Escherichia coli strain BL21(DE3)/pDIA17 Bacillus thuringiensis
1.1.1.205 gene guaB, sequence comparisons, functional recombinant overexpression of the His-tagged soluble enzyme in Escherichia coli strain BL21(DE3)/pDIA17 Legionella pneumophila subsp. pneumophila
1.1.1.205 gene guaB, sequence comparisons, functional recombinant overexpression of the His-tagged soluble enzyme in Escherichia coli strain BL21(DE3)/pDIA17 Neisseria meningitidis
1.1.1.205 gene guaB, sequence comparisons, functional recombinant overexpression of the His-tagged soluble enzyme in Escherichia coli strain BL21(DE3)/pDIA17 Staphylococcus aureus
1.1.1.205 gene guaB, sequence comparisons, functional recombinant overexpression of the His-tagged soluble enzyme in Escherichia coli strain BL21(DE3)/pDIA17 Burkholderia thailandensis
1.1.1.205 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.205 additional information
-
 additional information Michaelis-Menten kinetics Klebsiella pneumoniae
1.1.1.205 additional information
-
 additional information Michaelis-Menten kinetics Bacillus anthracis
1.1.1.205 additional information
-
 additional information Michaelis-Menten kinetics Staphylococcus aureus
1.1.1.205 additional information
-
 additional information Michaelis-Menten kinetics Burkholderia thailandensis
1.1.1.205 additional information
-
 additional information enzyme IMPDHnm exhibits cooperative kinetics for IMP with MgATP2- as the positive effector Neisseria meningitidis
1.1.1.205 additional information
-
 additional information enzyme IMPDHpp exhibits cooperative kinetics for IMP with MgATP2- as the positive effector Legionella pneumophila subsp. pneumophila
1.1.1.205 0.039
-
 IMP pH 10.0, 30°C, recombinant enzyme, with MgATP2- Legionella pneumophila subsp. pneumophila
1.1.1.205 0.039
-
 IMP pH 8.0, 30°C, recombinant enzyme, with MgATP Burkholderia thailandensis
1.1.1.205 0.05
-
 IMP pH 8.0, 30°C, recombinant enzyme, with MgATP2- Neisseria meningitidis
1.1.1.205 0.052
-
 IMP pH 10.0, 30°C, recombinant enzyme, without MgATP2- Legionella pneumophila subsp. pneumophila
1.1.1.205 0.052
-
 IMP pH 8.0, 30°C, recombinant enzyme, without MgATP Burkholderia thailandensis
1.1.1.205 0.053
-
 IMP pH 8.0, 30°C, recombinant enzyme, with MgATP2- Klebsiella pneumoniae
1.1.1.205 0.058
-
 IMP pH 8.0, 30°C, recombinant enzyme, without MgATP2- Klebsiella pneumoniae
1.1.1.205 0.12
-
 IMP pH 8.0, 30°C, recombinant enzyme, without MgATP2- Bacillus anthracis
1.1.1.205 0.148
-
 IMP pH 8.0, 30°C, recombinant enzyme, with MgATP2- Bacillus anthracis
1.1.1.205 0.196
-
 IMP pH 8.0, 30°C, recombinant enzyme, without MgATP2- Staphylococcus aureus
1.1.1.205 0.197
-
 IMP pH 8.0, 30°C, recombinant enzyme, with MgATP2- Staphylococcus aureus
1.1.1.205 0.269
-
 NAD+ pH 8.0, 30°C, recombinant enzyme, without MgATP2- Neisseria meningitidis
1.1.1.205 0.315
-
 IMP pH 8.0, 30°C, recombinant enzyme, without MgATP2- Neisseria meningitidis
1.1.1.205 0.355
-
 NAD+ pH 8.0, 30°C, recombinant enzyme, without MgATP Burkholderia thailandensis
1.1.1.205 0.418
-
 NAD+ pH 8.0, 30°C, recombinant enzyme, with MgATP Burkholderia thailandensis
1.1.1.205 0.477
-
 NAD+ pH 8.0, 30°C, recombinant enzyme, with MgATP2- Neisseria meningitidis
1.1.1.205 0.998
-
 NAD+ pH 10.0, 30°C, recombinant enzyme, without MgATP2- Legionella pneumophila subsp. pneumophila
1.1.1.205 1.122
-
 NAD+ pH 8.0, 30°C, recombinant enzyme, with MgATP2- Klebsiella pneumoniae
1.1.1.205 1.175
-
 NAD+ pH 8.0, 30°C, recombinant enzyme, without MgATP2- Klebsiella pneumoniae
1.1.1.205 1.762
-
 NAD+ pH 10.0, 30°C, recombinant enzyme, with MgATP2- Legionella pneumophila subsp. pneumophila
1.1.1.205 1.762
-
 NAD+ pH 8.0, 30°C, recombinant enzyme, with MgATP2- Staphylococcus aureus
1.1.1.205 1.994
-
 NAD+ pH 8.0, 30°C, recombinant enzyme, with MgATP2- Bacillus anthracis
1.1.1.205 2.209
-
 NAD+ pH 8.0, 30°C, recombinant enzyme, without MgATP2- Bacillus anthracis
1.1.1.205 2.35
-
 NAD+ pH 8.0, 30°C, recombinant enzyme, without MgATP2- Staphylococcus aureus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.205 K+ required at 20-150 mM Legionella pneumophila subsp. pneumophila
1.1.1.205 MgATP2- a positive effector for the cooperative class I IMPDH IMPDHnm Neisseria meningitidis
1.1.1.205 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
1.1.1.205 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
1.1.1.205 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
1.1.1.205 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
1.1.1.205 additional information MgATP has no significant effect on the catalytic activity of IMPDHbt Burkholderia thailandensis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.205 218000
-
 recombinant enzyme, gel filtration and analytical ultracentrifugation Burkholderia thailandensis
1.1.1.205 218000
-
 recombinant tetrameric enzyme, gel filtration and analytical ultracentrifugation Klebsiella pneumoniae
1.1.1.205 218000
-
 recombinant tetrameric enzyme, gel filtration and analytical ultracentrifugation Staphylococcus aureus
1.1.1.205 440000
-
 recombinant enzyme, gel filtration and analytical ultracentrifugation Legionella pneumophila subsp. pneumophila
1.1.1.205 440000
-
 recombinant enzyme, gel filtration and analytical ultracentrifugation Neisseria meningitidis
1.1.1.205 440000
-
 recombinant octameric enzyme, gel filtration and analytical ultracentrifugation Klebsiella pneumoniae
1.1.1.205 440000
-
 recombinant octameric enzyme, gel filtration and analytical ultracentrifugation Staphylococcus aureus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.205 IMP + NAD+ + H2O Klebsiella pneumoniae
-
 XMP + NADH + H+
-
 ?
1.1.1.205 IMP + NAD+ + H2O Bacillus thuringiensis
-
 XMP + NADH + H+
-
 ?
1.1.1.205 IMP + NAD+ + H2O Acinetobacter baumannii
-
 XMP + NADH + H+
-
 ?
1.1.1.205 IMP + NAD+ + H2O Bacillus anthracis
-
 XMP + NADH + H+
-
 ?
1.1.1.205 IMP + NAD+ + H2O Legionella pneumophila subsp. pneumophila
-
 XMP + NADH + H+
-
 ?
1.1.1.205 IMP + NAD+ + H2O Neisseria meningitidis
-
 XMP + NADH + H+
-
 ?
1.1.1.205 IMP + NAD+ + H2O Staphylococcus aureus
-
 XMP + NADH + H+
-
 ?
1.1.1.205 IMP + NAD+ + H2O Burkholderia thailandensis
-
 XMP + NADH + H+
-
 ?
1.1.1.205 IMP + NAD+ + H2O Staphylococcus aureus N315
-
 XMP + NADH + H+
-
 ?
1.1.1.205 IMP + NAD+ + H2O Bacillus thuringiensis BGSC 4AJ1
-
 XMP + NADH + H+
-
 ?
1.1.1.205 IMP + NAD+ + H2O Legionella pneumophila subsp. pneumophila Philadelphia 1
-
 XMP + NADH + H+
-
 ?
1.1.1.205 IMP + NAD+ + H2O Acinetobacter baumannii 5377
-
 XMP + NADH + H+
-
 ?
1.1.1.205 IMP + NAD+ + H2O Klebsiella pneumoniae 52145
-
 XMP + NADH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.205 Acinetobacter baumannii
-
-
-
1.1.1.205 Acinetobacter baumannii 5377
-
-
-
1.1.1.205 Bacillus anthracis Q81W29 gene GBAA_0008
-
1.1.1.205 Bacillus thuringiensis
-
 serovar monterrey
-
1.1.1.205 Bacillus thuringiensis BGSC 4AJ1
-
 serovar monterrey
-
1.1.1.205 Burkholderia thailandensis Q2SWW9
-
-
1.1.1.205 Klebsiella pneumoniae
-
-
-
1.1.1.205 Klebsiella pneumoniae 52145
-
-
-
1.1.1.205 Legionella pneumophila subsp. pneumophila Q5ZUR9
-
-
1.1.1.205 Legionella pneumophila subsp. pneumophila Philadelphia 1 Q5ZUR9
-
-
1.1.1.205 Neisseria meningitidis A1KU15
-
-
1.1.1.205 Staphylococcus aureus P99106
-
-
1.1.1.205 Staphylococcus aureus N315 P99106
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.205 recombinant soluble His-tagged enzyme from Escherichia coli strain BL21(DE3)/pDIA17 by nickel affinity chromatography and gel filtration Klebsiella pneumoniae
1.1.1.205 recombinant soluble His-tagged enzyme from Escherichia coli strain BL21(DE3)/pDIA17 by nickel affinity chromatography and gel filtration Bacillus thuringiensis
1.1.1.205 recombinant soluble His-tagged enzyme from Escherichia coli strain BL21(DE3)/pDIA17 by nickel affinity chromatography and gel filtration Bacillus anthracis
1.1.1.205 recombinant soluble His-tagged enzyme from Escherichia coli strain BL21(DE3)/pDIA17 by nickel affinity chromatography and gel filtration Legionella pneumophila subsp. pneumophila
1.1.1.205 recombinant soluble His-tagged enzyme from Escherichia coli strain BL21(DE3)/pDIA17 by nickel affinity chromatography and gel filtration Neisseria meningitidis
1.1.1.205 recombinant soluble His-tagged enzyme from Escherichia coli strain BL21(DE3)/pDIA17 by nickel affinity chromatography and gel filtration Staphylococcus aureus
1.1.1.205 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.205 IMP + NAD+ + H2O
-
 Klebsiella pneumoniae XMP + NADH + H+
-
 ?
1.1.1.205 IMP + NAD+ + H2O
-
 Bacillus thuringiensis XMP + NADH + H+
-
 ?
1.1.1.205 IMP + NAD+ + H2O
-
 Acinetobacter baumannii XMP + NADH + H+
-
 ?
1.1.1.205 IMP + NAD+ + H2O
-
 Bacillus anthracis XMP + NADH + H+
-
 ?
1.1.1.205 IMP + NAD+ + H2O
-
 Legionella pneumophila subsp. pneumophila XMP + NADH + H+
-
 ?
1.1.1.205 IMP + NAD+ + H2O
-
 Neisseria meningitidis XMP + NADH + H+
-
 ?
1.1.1.205 IMP + NAD+ + H2O
-
 Staphylococcus aureus XMP + NADH + H+
-
 ?
1.1.1.205 IMP + NAD+ + H2O
-
 Burkholderia thailandensis XMP + NADH + H+
-
 ?
1.1.1.205 IMP + NAD+ + H2O
-
 Staphylococcus aureus N315 XMP + NADH + H+
-
 ?
1.1.1.205 IMP + NAD+ + H2O
-
 Bacillus thuringiensis BGSC 4AJ1 XMP + NADH + H+
-
 ?
1.1.1.205 IMP + NAD+ + H2O
-
 Legionella pneumophila subsp. pneumophila Philadelphia 1 XMP + NADH + H+
-
 ?
1.1.1.205 IMP + NAD+ + H2O
-
 Acinetobacter baumannii 5377 XMP + NADH + H+
-
 ?
1.1.1.205 IMP + NAD+ + H2O
-
 Klebsiella pneumoniae 52145 XMP + NADH + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.205 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
1.1.1.205 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
1.1.1.205 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
1.1.1.205 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
1.1.1.205 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
1.1.1.205 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
1.1.1.205 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
1.1.1.205 octamer
-
 Legionella pneumophila subsp. pneumophila
1.1.1.205 octamer
-
 Neisseria meningitidis
1.1.1.205 octamer IMPDHba is predominantly octameric. In the presence of IMP, class II IMPDHs remain tetrameric Acinetobacter baumannii
1.1.1.205 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
1.1.1.205 tetramer in the presence of IMP, class II IMPDHs remain tetrameric Bacillus thuringiensis
1.1.1.205 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
1.1.1.205 tetramer or octamer in the presence of NAD+, IMPDHba is predominantly octameric Bacillus anthracis
1.1.1.205 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

EC Number Synonyms Comment Organism
1.1.1.205 A1S_3321
-
 Acinetobacter baumannii
1.1.1.205 BTH_I2056
-
 Burkholderia thailandensis
1.1.1.205 class I IMPDH
-
 Legionella pneumophila subsp. pneumophila
1.1.1.205 class I IMPDH
-
 Neisseria meningitidis
1.1.1.205 class II IMPDH
-
 Klebsiella pneumoniae
1.1.1.205 class II IMPDH
-
 Bacillus thuringiensis
1.1.1.205 class II IMPDH
-
 Acinetobacter baumannii
1.1.1.205 class II IMPDH
-
 Bacillus anthracis
1.1.1.205 class II IMPDH
-
 Staphylococcus aureus
1.1.1.205 class II IMPDH
-
 Burkholderia thailandensis
1.1.1.205 DR63_268
-
 Burkholderia thailandensis
1.1.1.205 GBAA_0008
-
 Bacillus anthracis
1.1.1.205 guaB
-
 Klebsiella pneumoniae
1.1.1.205 guaB
-
 Bacillus thuringiensis
1.1.1.205 guaB
-
 Acinetobacter baumannii
1.1.1.205 guaB
-
 Bacillus anthracis
1.1.1.205 guaB
-
 Legionella pneumophila subsp. pneumophila
1.1.1.205 guaB
-
 Neisseria meningitidis
1.1.1.205 guaB
-
 Staphylococcus aureus
1.1.1.205 guaB
-
 Burkholderia thailandensis
1.1.1.205 IMPDH
-
 Klebsiella pneumoniae
1.1.1.205 IMPDH
-
 Bacillus thuringiensis
1.1.1.205 IMPDH
-
 Acinetobacter baumannii
1.1.1.205 IMPDH
-
 Bacillus anthracis
1.1.1.205 IMPDH
-
 Legionella pneumophila subsp. pneumophila
1.1.1.205 IMPDH
-
 Neisseria meningitidis
1.1.1.205 IMPDH
-
 Staphylococcus aureus
1.1.1.205 IMPDH
-
 Burkholderia thailandensis
1.1.1.205 IMPDHab
-
 Acinetobacter baumannii
1.1.1.205 IMPDHba
-
 Bacillus anthracis
1.1.1.205 IMPDHbt
-
 Burkholderia thailandensis
1.1.1.205 IMPDHkp
-
 Klebsiella pneumoniae
1.1.1.205 IMPDHlpp
-
 Legionella pneumophila subsp. pneumophila
1.1.1.205 IMPDHnm
-
 Neisseria meningitidis
1.1.1.205 inosine-5'-monophosphate dehydrogenase
-
 Klebsiella pneumoniae
1.1.1.205 inosine-5'-monophosphate dehydrogenase
-
 Bacillus thuringiensis
1.1.1.205 inosine-5'-monophosphate dehydrogenase
-
 Acinetobacter baumannii
1.1.1.205 inosine-5'-monophosphate dehydrogenase
-
 Bacillus anthracis
1.1.1.205 inosine-5'-monophosphate dehydrogenase
-
 Legionella pneumophila subsp. pneumophila
1.1.1.205 inosine-5'-monophosphate dehydrogenase
-
 Neisseria meningitidis
1.1.1.205 inosine-5'-monophosphate dehydrogenase
-
 Staphylococcus aureus
1.1.1.205 inosine-5'-monophosphate dehydrogenase
-
 Burkholderia thailandensis
1.1.1.205 lpg1723
-
 Legionella pneumophila subsp. pneumophila
1.1.1.205 NMC1103
-
 Neisseria meningitidis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.205 30
-
 assay at Klebsiella pneumoniae
1.1.1.205 30
-
 assay at Bacillus thuringiensis
1.1.1.205 30
-
 assay at Acinetobacter baumannii
1.1.1.205 30
-
 assay at Bacillus anthracis
1.1.1.205 30
-
 assay at Legionella pneumophila subsp. pneumophila
1.1.1.205 30
-
 assay at Neisseria meningitidis
1.1.1.205 30
-
 assay at Staphylococcus aureus
1.1.1.205 30
-
 assay at Burkholderia thailandensis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.205 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
1.1.1.205 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

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.205 8
-
-
 Bacillus thuringiensis
1.1.1.205 8
-
-
 Acinetobacter baumannii
1.1.1.205 8
-
-
 Neisseria meningitidis
1.1.1.205 8
-
-
 Burkholderia thailandensis
1.1.1.205 8.5
-
-
 Klebsiella pneumoniae
1.1.1.205 9
-
-
 Bacillus anthracis
1.1.1.205 9.2
-
-
 Staphylococcus aureus
1.1.1.205 10
-
-
 Legionella pneumophila subsp. pneumophila

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.205 NAD+
-
 Klebsiella pneumoniae
1.1.1.205 NAD+
-
 Bacillus thuringiensis
1.1.1.205 NAD+
-
 Acinetobacter baumannii
1.1.1.205 NAD+
-
 Bacillus anthracis
1.1.1.205 NAD+
-
 Legionella pneumophila subsp. pneumophila
1.1.1.205 NAD+
-
 Neisseria meningitidis
1.1.1.205 NAD+
-
 Staphylococcus aureus
1.1.1.205 NAD+
-
 Burkholderia thailandensis

General Information

EC Number General Information Comment Organism
1.1.1.205 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
1.1.1.205 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
1.1.1.205 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
1.1.1.205 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
1.1.1.205 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
1.1.1.205 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
1.1.1.205 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
1.1.1.205 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
1.1.1.205 metabolism the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP Klebsiella pneumoniae
1.1.1.205 metabolism the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP Bacillus thuringiensis
1.1.1.205 metabolism the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP Acinetobacter baumannii
1.1.1.205 metabolism the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP Bacillus anthracis
1.1.1.205 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
1.1.1.205 metabolism the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP Neisseria meningitidis
1.1.1.205 metabolism the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP Staphylococcus aureus
1.1.1.205 metabolism the enzyme occupies a key position in purine nucleotide metabolism catalyzing the rate-limiting NAD-dependent oxidation of IMP to XMP Burkholderia thailandensis
1.1.1.205 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
1.1.1.205 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
1.1.1.205 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
1.1.1.205 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
1.1.1.205 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
1.1.1.205 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
1.1.1.205 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
1.1.1.205 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
1.1.1.205 physiological function IMPDH functional regulation, overview Klebsiella pneumoniae
1.1.1.205 physiological function IMPDH functional regulation, overview Bacillus thuringiensis
1.1.1.205 physiological function IMPDH functional regulation, overview Acinetobacter baumannii
1.1.1.205 physiological function IMPDH functional regulation, overview Bacillus anthracis
1.1.1.205 physiological function IMPDH functional regulation, overview Legionella pneumophila subsp. pneumophila
1.1.1.205 physiological function IMPDH functional regulation, overview Neisseria meningitidis
1.1.1.205 physiological function IMPDH functional regulation, overview Staphylococcus aureus
1.1.1.205 physiological function IMPDH functional regulation, overview Burkholderia thailandensis