Application | Comment | Organism |
---|---|---|
pharmacology | inhibition of AfM1PDH might be a useful target for therapy of Aspergillus fumigatus infections | Aspergillus fumigatus |
Cloned (Comment) | Organism |
---|---|
recombinant expression in Escherichia coli | Aspergillus fumigatus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | poor effects by ATP, ADP and AMP | Aspergillus fumigatus | |
NADH | - |
Aspergillus fumigatus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady-state kinetics and kinetic mechanism, binding of D-mannitol 1-phosphate and NAD+ is random, whereas D-fructose 6-phosphate binds only after NADH has bound to the enzyme. Hydride transfer is rate-determining for D-mannitol 1-phosphate oxidation by AfM1PDH. AfM1PDH behaves kinetically as a fructose 6-phosphate reductase, overview | Aspergillus fumigatus | |
0.014 | - |
NADH | pH 10.0, 25°C, recombinant enzyme | Aspergillus fumigatus | |
0.13 | - |
D-mannitol 1-phosphate | pH 7.1, 25°C, recombinant enzyme | Aspergillus fumigatus | |
0.8 | - |
NAD+ | pH 7.1, 25°C, recombinant enzyme | Aspergillus fumigatus | |
3.2 | - |
D-fructose 6-phosphate | pH 10.0, 25°C, recombinant enzyme | Aspergillus fumigatus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-mannitol 1-phosphate + NAD+ | Aspergillus fumigatus | AfM1PDH primarily functions as a D-fructose-6-phosphate reductase and is specific for its natural pair of substrates | D-fructose 6-phosphate + NADH + H+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus fumigatus | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
D-mannitol 1-phosphate + NAD+ = D-fructose 6-phosphate + NADH + H+ | the phosphate moiety in Man-ol1P and Fru6P is essential for substrate recognition and/or catalysis by Aspergillus fumigatus M1PDH. Binding of D-mannitol 1-phosphate and NAD+ is random, whereas D-fructose 6-phosphate binds only after NADH has bound to the enzyme. Hydride transfer is rate-determining for D-mannitol 1-phosphate oxidation by AfM1PDH. The enzyme behaves kinetically as a fructose 6-phosphate reductase | Aspergillus fumigatus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-mannitol 1-phosphate + NAD+ | AfM1PDH primarily functions as a D-fructose-6-phosphate reductase and is specific for its natural pair of substrates | Aspergillus fumigatus | D-fructose 6-phosphate + NADH + H+ | - |
r | |
additional information | M1PDH does not catalyze the oxidation of D-mannitol, D-sorbitol, D-ribitol, xylitol, D-xylose, L-xylose, D-glucose, D-mannose, L-arabinose, D-arabinose, D-galactose, L-fucose, and D-lyxose. The enzyme is also inactive above a level of 1% activity with D-fructose 6-phosphate for reduction of D-fructose, L-sorbose, D-xylulose, D-fructose 1,6-bisphosphate, D-glucose 6-phosphate, and D-glucose 1-phosphate | Aspergillus fumigatus | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
M1PDH | - |
Aspergillus fumigatus |
NADH-dependent mannitol-1-phosphate 5-dehydrogenase | - |
Aspergillus fumigatus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Aspergillus fumigatus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | 50 | half-life is 20 h at 40°C, the enzyme displays remarkable stability at 40°C and even at 50°C | Aspergillus fumigatus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
10.6 | - |
D-mannitol 1-phosphate | pH 7.1, 25°C, recombinant enzyme | Aspergillus fumigatus | |
132 | - |
D-fructose 6-phosphate | pH 10.0, 25°C, recombinant enzyme | Aspergillus fumigatus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.1 | - |
assay at, reduction reaction | Aspergillus fumigatus |
10 | - |
assay at, oxidation reaction | Aspergillus fumigatus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | NADP+ is a poor cofactor substrate | Aspergillus fumigatus | |
NAD+ | - |
Aspergillus fumigatus | |
NADH | - |
Aspergillus fumigatus |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.002 | - |
NADH | pH 10.0, 25°C, recombinant enzyme | Aspergillus fumigatus |
Organism | Comment | Expression |
---|---|---|
Aspergillus fumigatus | M1PDH becomes strongly upregulated during heat shock | up |
General Information | Comment | Organism |
---|---|---|
additional information | ATP, ADP and AMP do not affect the activity of AfM1PDH, suggesting the absence of flux control by cellular energy charge at the level of D-fructose 6-phosphate reduction | Aspergillus fumigatus |
physiological function | formation of mannitol is an essential component of the temperature stress response of Aspergillus fumigatus. Enhanced biosynthesis of d-mannitol via AfM1PDH-catalyzed conversion of fructose 6-phosphate might contribute extra robustness to Aspergillus fumigatus under high temperature conditions | Aspergillus fumigatus |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
41 | - |
D-fructose 6-phosphate | pH 10.0, 25°C, recombinant enzyme | Aspergillus fumigatus | |
80 | - |
D-mannitol 1-phosphate | pH 7.1, 25°C, recombinant enzyme | Aspergillus fumigatus |