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Literature summary for 1.1.1.205 extracted from

  • Buey, R.M.; Ledesma-Amaro, R.; Balsera, M.; de Pereda, J.M.; Revuelta, J.L.
    Increased riboflavin production by manipulation of inosine 5-monophosphate dehydrogenase in Ashbya gossypii (2015), Appl. Microbiol. Biotechnol., 99, 9577-9589.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene guaB, recombinant expresion of HIs8-tagged wild-type and mutant enzymes in Escherichia coli Eremothecium gossypii

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant mutant apoenzyme AgIMPDH-DELTABateman, vapor diffusion method, mixing 23 mg/ml protein 10 mM Tris-HCl, 100 mM KCl, 0.25 mM TCEP, pH 8.0, with an equal volume of mother liquor consisting of 0.1 M HEPES, pH 7.5, 40% PEG 300 v/v, and 0.2 M NaCl, for the enzyme mutant complex with IMP and NAD+ up to 5 mM XMP and 5 mM NAD+ are added to the protein solution, at room temperature, harvest of crystals of AgIMPDH-DELTABateman with a mixture of about 80% of the covalent intermediate E-XMP* and about 20% IMP bound to the active site, X-ray diffraction structure determination and analysis Eremothecium gossypii

Protein Variants

Protein Variants Comment Organism
additional information construction of the catalytically active AgIMPDH-DELTABateman enzyme mutant, that has a the deletion of the regulatory domain facilitating crystallization Eremothecium gossypii

Inhibitors

Inhibitors Comment Organism Structure
Mycophenolic acid
-
Eremothecium gossypii
NAD+ substrate inhibition Eremothecium gossypii
XMP product inhibition Eremothecium gossypii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten enzyme kinetics Eremothecium gossypii
0.0902
-
IMP recombinant wild-type enzyme, pH 8.0, 28°C Eremothecium gossypii
0.118
-
IMP recombinant AgIMPDH-DELTABateman mutant enzyme, pH 8.0, 28°C Eremothecium gossypii
0.28
-
NAD+ recombinant wild-type enzyme, pH 8.0, 28°C Eremothecium gossypii
0.387
-
NAD+ recombinant AgIMPDH-DELTABateman mutant enzyme, pH 8.0, 28°C Eremothecium gossypii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
IMP + NAD+ + H2O Eremothecium gossypii
-
XMP + NADH + H+
-
?
IMP + NAD+ + H2O Eremothecium gossypii ATCC 10895
-
XMP + NADH + H+
-
?

Organism

Organism UniProt Comment Textmining
Eremothecium gossypii Q756Z6 single gene
-
Eremothecium gossypii ATCC 10895 Q756Z6 single gene
-

Reaction

Reaction Comment Organism Reaction ID
IMP + NAD+ + H2O = XMP + NADH + H+ reaction in two steps via covalent interemediate state, the catalytic residue is Cys334 Eremothecium gossypii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
IMP + NAD+ + H2O
-
Eremothecium gossypii XMP + NADH + H+
-
?
IMP + NAD+ + H2O
-
Eremothecium gossypii ATCC 10895 XMP + NADH + H+
-
?

Subunits

Subunits Comment Organism
More the core of the catalytic domain comprises a (beta/alpha)8 barrel which represents the typical triose-phosphate isomerase fold (TIM barrel) Eremothecium gossypii
tetramer enzyme structure in solution Eremothecium gossypii

Synonyms

Synonyms Comment Organism
IMP dehydrogenase
-
Eremothecium gossypii
IMPDH
-
Eremothecium gossypii
inosine 5-monophosphate dehydrogenase
-
Eremothecium gossypii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
28
-
assay at Eremothecium gossypii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.46
-
IMP recombinant wild-type enzyme, pH 8.0, 28°C Eremothecium gossypii
3.06
-
IMP recombinant AgIMPDH-DELTABateman mutant enzyme, pH 8.0, 28°C Eremothecium gossypii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Eremothecium gossypii

Cofactor

Cofactor Comment Organism Structure
additional information the enzyme shows a clear preference for NAD+ over NADP+, since it loses more than 95% activity when using the latter as co-substrate Eremothecium gossypii
NAD+
-
Eremothecium gossypii

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0000321
-
Mycophenolic acid pH 8.0, 28°C, recombinant enzyme Eremothecium gossypii
0.2083
-
XMP pH 8.0, 28°C, recombinant enzyme Eremothecium gossypii
3.6
-
NAD+ recombinant wild-type enzyme, pH 8.0, 28°C Eremothecium gossypii
4.5
-
NAD+ recombinant AgIMPDH-DELTABateman mutant enzyme, pH 8.0, 28°C Eremothecium gossypii

General Information

General Information Comment Organism
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 Eremothecium gossypii
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 Eremothecium gossypii
additional information Ashbya gossypii is a natural riboflavin superproducer Eremothecium gossypii
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 Eremothecium gossypii