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Literature summary extracted from

  • Rostirolla, D.; Milech De Assuncao, T.; Bizarro, C.; Basso, L.; Santos, D.
    Biochemical characterization of Mycobacterium tuberculosis IMP dehydrogenase: kinetic mechanism, metal activation and evidence of a cooperative system (2014), RSC Adv., 4, 26271-26287.
No PubMed abstract available

Application

EC Number Application Comment Organism
1.1.1.205 drug development IMPDH from Mycobacterium tuberculosis (MtIMPDH) is a potential molecular target to inhibitor development Mycobacterium tuberculosis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.205 gene guaB2, recombinant expression in Escherichia coli strain C41(DE3) Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.205 APAD+ substrate inhibition, uncompetitive substrate inhibition versus IMP Mycobacterium tuberculosis
1.1.1.205 additional information several inhibitors compete with the flap for the vacant NADH site, thus preventing the hydrolysis of E-XMP* reaction intermediate Mycobacterium tuberculosis
1.1.1.205 NAD+ substrate inhibition Mycobacterium tuberculosis
1.1.1.205 NADH product inhibition, noncompetitive versus IMP, NAD+, and K+ Mycobacterium tuberculosis
1.1.1.205 XMP product inhibition, competitive versus IMP, noncompetitive versus NAD+ and K+ Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.205 additional information
-
additional information steady-state kinetics and kinetic analysis, detailed overview Mycobacterium tuberculosis
1.1.1.205 0.887
-
NAD+ recombinant enzyme, pH 8.5, 37°C Mycobacterium tuberculosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.205 K+ required, activates, the enzyme contains one K+ per subunit Mycobacterium tuberculosis
1.1.1.205 additional information the enzyme activity is dependent on the presence of a monovalent cation, preferaby K+. Neither Na+ nor Li+, which have lower ionic radii than K+, activate the MtIMPDH. Divalent cations, such as Mg2+ and Ca2+, do not activate the enzyme even at 200 mM Mycobacterium tuberculosis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.205 54775
-
-
Mycobacterium tuberculosis
1.1.1.205 220000
-
about, molecular weight determination by cross-linking experiments and 12% SDS-PAGE analysis, since the enzyme elutes as different species depending on its concentration, indicating the presence of different aggregated forms Mycobacterium tuberculosis

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 Mycobacterium tuberculosis
-
XMP + NADH + H+
-
?
1.1.1.205 IMP + NAD+ + H2O Mycobacterium tuberculosis H37Rv
-
XMP + NADH + H+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.205 Mycobacterium tuberculosis P9WKI7
-
-
1.1.1.205 Mycobacterium tuberculosis H37Rv P9WKI7
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.205 recombinant soluble enzyme 1.7fold from Escherichia coli strain C41(DE3) by affinity chromatography and gel filtration Mycobacterium tuberculosis

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.205 IMP + NAD+ + H2O = XMP + NADH + H+ a steady-state ordered Bi Bi kinetic mechanism in which IMP binds first followed by NAD+, and product release is ordered. Hydride transfer appears not to be rate-limiting. The pH-rate profile indicates one deprotonated group essential for catalysis Mycobacterium tuberculosis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.205 2
-
purified recombinant enzyme, pH 8.5, 37°C Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.205 IMP + APAD+ + H2O
-
Mycobacterium tuberculosis XMP + APADH + H+
-
?
1.1.1.205 IMP + APAD+ + H2O
-
Mycobacterium tuberculosis H37Rv XMP + APADH + H+
-
?
1.1.1.205 IMP + NAD+ + H2O
-
Mycobacterium tuberculosis XMP + NADH + H+
-
?
1.1.1.205 IMP + NAD+ + H2O
-
Mycobacterium tuberculosis H37Rv XMP + NADH + H+
-
?

Subunits

EC Number Subunits Comment Organism
1.1.1.205 More MtIMPDH predominates as a tetramer Mycobacterium tuberculosis
1.1.1.205 tetramer 4 * 54775, mass spectrometry, x * 55000, recombinnat enzyme, SDS-PAGE, 4 * 54700, about, sequence calculation Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
1.1.1.205 guaB2
-
Mycobacterium tuberculosis
1.1.1.205 IMP dehydrogenase
-
Mycobacterium tuberculosis
1.1.1.205 IMPDH
-
Mycobacterium tuberculosis
1.1.1.205 inosine 5'-monophosphate dehydrogenase
-
Mycobacterium tuberculosis
1.1.1.205 Rv3411c
-
Mycobacterium tuberculosis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.205 37
-
assay at Mycobacterium tuberculosis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.205 3.1
-
NAD+ recombinant enzyme, pH 8.5, 37°C Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.205 8 8.5
-
Mycobacterium tuberculosis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.1.205 7 10 activity range, profile overview Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.205 3-acetylpyridine adenine dinucleotide the NAD+ analog 3-acetylpyridine adenine dinucleotide (APAD+) is a substrate for MtIMPDH and the dependence of velocity on increasing concentrations of APAD+ (Fig. 4B) also displayed substrate inhibition Mycobacterium tuberculosis
1.1.1.205 NAD+ groups with pK values of 7.5 and 9.0 are important for NAD+ binding Mycobacterium tuberculosis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.1.1.205 additional information
-
additional information inhibition kinetic analysis, detailed overview Mycobacterium tuberculosis
1.1.1.205 6.3
-
NAD+ recombinant enzyme, pH 8.5, 37°C Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
1.1.1.205 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 Mycobacterium tuberculosis