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D-arabitol 1-phosphate + NAD+
D-xylulose 5-phosphate + NADH + H+
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADPH + H+
D-mannitol 1-phosphate + NADP+
D-fructose-6-phosphate + NADH
D-mannitol-1-phosphate + NAD+
-
-
-
-
r
D-mannitol 1-phosphate + 3-acetylpyridine-NAD+
D-fructose 6-phosphate + ?
-
7% of the activity compared to NAD+
-
?
D-mannitol 1-phosphate + acetylpyridine adenine dinucleotide
D-fructose 6-phosphate + ?
-
50% of the activity compared to NAD+
-
?
D-mannitol 1-phosphate + dichlorophenolindophenol
D-fructose 6-phosphate + reduced dichlorophenolindophenol
-
higher activity than for NAD+
-
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NADP+
D-fructose 6-phosphate + NADPH + H+
D-mannitol 1-phosphate + nicotinamide 6-(2-hydoxyethylamino) purine dinucleotide
D-fructose 6-phosphate + ?
-
75% of the activity compared to NAD+
-
?
D-mannitol 1-phosphate + nicotinamide hypoxanthine dinucleotide
D-fructose 6-phosphate + ?
-
84% of the activity compared to NAD+
-
?
D-mannitol-1-phosphate + NAD+
D-fructose-6-phosphate + NADH
-
-
-
-
r
D-sorbitol 6-phosphate + NAD+
D-glucose 6-phosphate + NADH + H+
-
38.8% of the activity compared to D-mannitol 1-phosphate
-
r
ethanol + NAD+
acetaldehyde + NADH
-
56% of the activity compared to D-mannitol 1-phosphate
-
r
hexitol phosphate + NAD+
? + NADH
additional information
?
-
D-arabitol 1-phosphate + NAD+
D-xylulose 5-phosphate + NADH + H+
-
-
-
r
D-arabitol 1-phosphate + NAD+
D-xylulose 5-phosphate + NADH + H+
-
-
-
r
D-arabitol 1-phosphate + NAD+
D-xylulose 5-phosphate + NADH + H+
-
-
-
r
D-arabitol 1-phosphate + NAD+
D-xylulose 5-phosphate + NADH + H+
-
-
-
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
-
-
-
?
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
-
-
-
?
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
-
-
-
-
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
-
-
-
-
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
-
-
-
r
D-fructose 6-phosphate + NADPH + H+
D-mannitol 1-phosphate + NADP+
-
-
-
?
D-fructose 6-phosphate + NADPH + H+
D-mannitol 1-phosphate + NADP+
-
-
-
?
D-fructose 6-phosphate + NADPH + H+
D-mannitol 1-phosphate + NADP+
-
-
-
-
r
D-fructose 6-phosphate + NADPH + H+
D-mannitol 1-phosphate + NADP+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
the enzyme is involved in mannitol biosynthesis, which is required for plant pathogenicity by Alternaria alternata, overview
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
the enzyme is involved in mannitol biosynthesis, which is required for plant pathogenicity by Alternaria alternata, overview
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
M1PDH is stereospecific for transferring the hydrogen to NAD+, in situ proton NMR studies of enzymatic oxidation of D-5-[2H]-mannitol 1-phosphate, overview
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
AfM1PDH primarily functions as a D-fructose-6-phosphate reductase and is specific for its natural pair of substrates
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
highly specific for both substrates
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
random bi-bi kinetic with two dead-end complexes
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
the enzyme shows higher activity in the reduction reaction
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
the enzyme shows higher activity in the reduction reaction
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
part of the phosphoenolpyruvate phosphotransferase system
-
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
highly specific for both substrates
-
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
highly specific for both substrates
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
favours reverse reaction
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
highly specific for both substrates
-
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
the enzyme competes with two sorbitol-6-phosphate dehydrogenase for D-fructose 6-phosphate, metabolic flux in engineered organisms, overview
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
highly specific for both substrates
-
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
part of the phosphoenolpyruvate phosphotransferase system
-
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
-
r
D-mannitol 1-phosphate + NADP+
D-fructose 6-phosphate + NADPH + H+
-
-
-
r
D-mannitol 1-phosphate + NADP+
D-fructose 6-phosphate + NADPH + H+
-
-
-
r
hexitol phosphate + NAD+
? + NADH
-
-
-
?
hexitol phosphate + NAD+
? + NADH
-
-
-
?
additional information
?
-
MtlD is a bifunctional enzyme of mannitol biosynthesis that combines mannitol-1-phosphate dehydrogenase and phosphatase activities in a single polypeptide chain
-
-
?
additional information
?
-
MtlD is a bifunctional enzyme of mannitol biosynthesis that combines mannitol-1-phosphate dehydrogenase and phosphatase activities in a single polypeptide chain
-
-
?
additional information
?
-
-
important role for Lys213 in the catalytic mechanism of M1PDH
-
-
?
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
-
-
?
additional information
?
-
-
required for assimilation of mannitol and glucitol
-
-
?
additional information
?
-
-
high specificity for substrates fructose-6-phosphate/NADH and mannitol-1-phosphate/NAD+, no substrate: fructose-1-phosphate, fructose-1,6-bisphosphate, glucose-1-phosphate, NADPH, NADP+
-
-
?
additional information
?
-
mannitol is present in large amounts in brown algae, where its synthesis involved two steps: a mannitol-1-phosphate dehydrogenase (M1PDH) catalyzes a reversible reaction between fructose-6-phosphate (F6P) and mannitol-1-phosphate (M1P) (EC 1.1.1.17), and a mannitol-1-phosphatase hydrolyzes M1P to mannitol (EC 3.1.3.22)
-
-
?
additional information
?
-
mannitol is present in large amounts in brown algae, where its synthesis involved two steps: a mannitol-1-phosphate dehydrogenase (M1PDH) catalyzes a reversible reaction between fructose-6-phosphate (F6P) and mannitol-1-phosphate (M1P) (EC 1.1.1.17), and a mannitol-1-phosphatase hydrolyzes M1P to mannitol (EC 3.1.3.22)
-
-
?
additional information
?
-
mannitol is present in large amounts in brown algae, where its synthesis involved two steps: a mannitol-1-phosphate dehydrogenase (M1PDH) catalyzes a reversible reaction between fructose-6-phosphate (F6P) and mannitol-1-phosphate (M1P) (EC 1.1.1.17), and a mannitol-1-phosphatase hydrolyzes M1P to mannitol (EC 3.1.3.22)
-
-
?
additional information
?
-
EsM1PDH1cat isozyme is specific for D-fructose 6-phosphate and D-mannitol 1-phosphate
-
-
?
additional information
?
-
EsM1PDH1cat isozyme is specific for D-fructose 6-phosphate and D-mannitol 1-phosphate
-
-
?
additional information
?
-
EsM1PDH1cat isozyme is specific for D-fructose 6-phosphate and D-mannitol 1-phosphate
-
-
?
additional information
?
-
no activity with D-glucose 6-phosphate, sorbitol 6-phosphate, D-fructose 1-phosphate
-
-
?
additional information
?
-
-
no activity with D-glucose 6-phosphate, sorbitol 6-phosphate, D-fructose 1-phosphate
-
-
?
additional information
?
-
-
Petunia hybrida (Hook) Vilm. cv. Mitchell is transformed with an Escherichia coli gene encoding mannitol 1-phosphate dehydrogenase. The high-mannitol containing lines are more tolerant of chilling stress than the low mannitol containing transgenic lines and wild-type. In the higher mannitol lines only 0.04% to 0.06% of the total osmotic potential generated from all solutes can be attributed to mannitol, thus its action is more like that of an osmoprotectant rather than an osmoregulator
-
-
?
additional information
?
-
mannitol 1-phosphate metabolism is required for sporulation in planta of the wheat pathogen Stagonospora nodorum
-
-
?
additional information
?
-
-
mannitol 1-phosphate metabolism is required for sporulation in planta of the wheat pathogen Stagonospora nodorum
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-arabitol 1-phosphate + NAD+
D-xylulose 5-phosphate + NADH + H+
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
-
-
-
-
r
D-fructose 6-phosphate + NADPH + H+
D-mannitol 1-phosphate + NADP+
-
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NADP+
D-fructose 6-phosphate + NADPH + H+
D-sorbitol 6-phosphate + NAD+
D-glucose 6-phosphate + NADH + H+
-
38.8% of the activity compared to D-mannitol 1-phosphate
-
r
ethanol + NAD+
acetaldehyde + NADH
-
56% of the activity compared to D-mannitol 1-phosphate
-
r
hexitol phosphate + NAD+
? + NADH
additional information
?
-
D-arabitol 1-phosphate + NAD+
D-xylulose 5-phosphate + NADH + H+
-
-
-
r
D-arabitol 1-phosphate + NAD+
D-xylulose 5-phosphate + NADH + H+
-
-
-
r
D-arabitol 1-phosphate + NAD+
D-xylulose 5-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
the enzyme is involved in mannitol biosynthesis, which is required for plant pathogenicity by Alternaria alternata, overview
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
the enzyme is involved in mannitol biosynthesis, which is required for plant pathogenicity by Alternaria alternata, overview
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
AfM1PDH primarily functions as a D-fructose-6-phosphate reductase and is specific for its natural pair of substrates
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
highly specific for both substrates
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
random bi-bi kinetic with two dead-end complexes
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
the enzyme shows higher activity in the reduction reaction
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
the enzyme shows higher activity in the reduction reaction
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
part of the phosphoenolpyruvate phosphotransferase system
-
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
highly specific for both substrates
-
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
highly specific for both substrates
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
favours reverse reaction
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
highly specific for both substrates
-
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
the enzyme competes with two sorbitol-6-phosphate dehydrogenase for D-fructose 6-phosphate, metabolic flux in engineered organisms, overview
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
highly specific for both substrates
-
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
part of the phosphoenolpyruvate phosphotransferase system
-
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
-
r
D-mannitol 1-phosphate + NADP+
D-fructose 6-phosphate + NADPH + H+
-
-
-
r
D-mannitol 1-phosphate + NADP+
D-fructose 6-phosphate + NADPH + H+
-
-
-
r
hexitol phosphate + NAD+
? + NADH
-
-
-
?
hexitol phosphate + NAD+
? + NADH
-
-
-
?
additional information
?
-
MtlD is a bifunctional enzyme of mannitol biosynthesis that combines mannitol-1-phosphate dehydrogenase and phosphatase activities in a single polypeptide chain
-
-
?
additional information
?
-
MtlD is a bifunctional enzyme of mannitol biosynthesis that combines mannitol-1-phosphate dehydrogenase and phosphatase activities in a single polypeptide chain
-
-
?
additional information
?
-
-
required for assimilation of mannitol and glucitol
-
-
?
additional information
?
-
mannitol is present in large amounts in brown algae, where its synthesis involved two steps: a mannitol-1-phosphate dehydrogenase (M1PDH) catalyzes a reversible reaction between fructose-6-phosphate (F6P) and mannitol-1-phosphate (M1P) (EC 1.1.1.17), and a mannitol-1-phosphatase hydrolyzes M1P to mannitol (EC 3.1.3.22)
-
-
?
additional information
?
-
mannitol is present in large amounts in brown algae, where its synthesis involved two steps: a mannitol-1-phosphate dehydrogenase (M1PDH) catalyzes a reversible reaction between fructose-6-phosphate (F6P) and mannitol-1-phosphate (M1P) (EC 1.1.1.17), and a mannitol-1-phosphatase hydrolyzes M1P to mannitol (EC 3.1.3.22)
-
-
?
additional information
?
-
mannitol is present in large amounts in brown algae, where its synthesis involved two steps: a mannitol-1-phosphate dehydrogenase (M1PDH) catalyzes a reversible reaction between fructose-6-phosphate (F6P) and mannitol-1-phosphate (M1P) (EC 1.1.1.17), and a mannitol-1-phosphatase hydrolyzes M1P to mannitol (EC 3.1.3.22)
-
-
?
additional information
?
-
-
Petunia hybrida (Hook) Vilm. cv. Mitchell is transformed with an Escherichia coli gene encoding mannitol 1-phosphate dehydrogenase. The high-mannitol containing lines are more tolerant of chilling stress than the low mannitol containing transgenic lines and wild-type. In the higher mannitol lines only 0.04% to 0.06% of the total osmotic potential generated from all solutes can be attributed to mannitol, thus its action is more like that of an osmoprotectant rather than an osmoregulator
-
-
?
additional information
?
-
mannitol 1-phosphate metabolism is required for sporulation in planta of the wheat pathogen Stagonospora nodorum
-
-
?
additional information
?
-
-
mannitol 1-phosphate metabolism is required for sporulation in planta of the wheat pathogen Stagonospora nodorum
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,10-phenanthroline
-
weak inhibition
2,2'-bipyridyl
-
weak inhibition
4,7-phenanthroline
-
weak inhibition
4-hydroxymercuribenzoate
strong inhibition; strong inhibition; strong inhibition
5,5'-dithiobis-(2-nitrobenzoate)
-
complete inactivation at 0.24 mM
adenosine
-
48% inhibition of fructose 6-phosphate reduction
adenosine diphosphoribose
-
competitive inhibition with respect to NADH, noncompetitive inhibition with respect to D-fructose 6-phosphate
Ca2+
35.9% inhibition at 10 mM of the reverse reaction
cytidine
-
17% inhibition of fructose 6-phosphate reduction
D-fructose 1,6-diphosphate
-
12% inhibition of mannitol 1-phosphate oxidation
D-glucose 6-phosphate
-
competitive inhibition with respect to D-fructose 6-phosphate, noncompetitive inhibition with respect to NADH
D-mannitol 1-phosphate
-
competitive inhibition with respect to D-fructose 6-phosphate, noncompetitive inhibition with respect to NADH
diethyldicarbonate
-
60% inhibition at 1 mM
diethyldithiocarbamate
-
95% inactivation, prevented by presence of 2-mercaptoethanol
dihydrocelastrol
competitive inhibitor, presence of dihydrocelastrol effectively reduces bacterial cell viability during host infection
DTT
46.0% inhibition at 10 mM of the reverse reaction
fructose-6-phosphate
-
substrate inhibition above 0.5 mM
GTP
-
11% inhibition of mannitol 1-phosphate oxidation
guanosine
-
10% inhibition of fructose 6-phosphate reduction
KCl
at 1.5 M, 52% of maximum activity obtained with NaCl
Li+
24.4% inhibition at 50 mM of the reverse reaction
Mg2+
31.2% inhibition at 10 mM of the reverse reaction
Mn2+
31.3% inhibition at 50 mM of the reverse reaction
N-ethylmaleimide
-
1 mM, 80% inhibition of reduction and oxidation reaction
NaCl
activity is strictly salt dependent, with highest stimulation at 600 mM NaCl and 24% of maximum activity at 1.5 M
NAD+
-
competitive inhibition with respect to NADH, noncompetitive inhibition with respect to D-fructose 6-phosphate
p-hydroxymercuribenzoate
-
0.5 mM, complete inhibition of reduction and oxidation reaction, 2-mercaptoethanol protects
phosphoenolpyruvate
-
14% inhibition of mannitol 1-phosphate oxidation
SDS
80.1% inhibition at 1 mM of the reverse reaction
thymidine
-
8% inhibition of fructose 6-phosphate reduction
uridine
-
16% inhibition of fructose 6-phosphate reduction
ADP
-
competitive inhibition
ADP
-
20% inhibition of mannitol 1-phosphate oxidation
ATP
-
competitive inhibition
ATP
-
53% inhibition of mannitol 1-phosphate oxidation
Cd2+
-
competitive inhibition
Cd2+
-
cooperative binding
Co2+
-
competitive inhibition
Co2+
-
cooperative binding
Cu2+
-
irreversible inactivation
Cu2+
-
irreversible inactivation
Cu2+
32.8% inhibition at 2 mM of the reverse reaction
D-fructose 6-phosphate
-
competitive inhibition with respect to D-mannitol 1-phosphate
D-fructose 6-phosphate
-
56% inhibition of mannitol 1-phosphate oxidation
Hg2+
-
irreversible inactivation
Hg2+
-
irreversible inactivation
NADH
-
-
NADH
-
competitive inhibition with respect to NAD+
Ni2+
-
competitive inhibition
Ni2+
-
cooperative binding
Zn2+
-
competitive with respect to D-fructose 6-phosphate, noncompetitive inhibition with respect to NADH
Zn2+
-
cooperative binding of Zn2+, competitive type if KCl concentration is greater 100 mM, sigmoidal type at lower salt concentrations
Zn2+
44.7% inhibition at 2 mM of the reverse reaction
additional information
-
poor effects by ATP, ADP and AMP
-
additional information
no or poor inhibition of the reverse reaction by EDTA and 2-mercaptoethanol
-
additional information
-
no or poor inhibition of the reverse reaction by EDTA and 2-mercaptoethanol
-
additional information
no inhibition by EDTA; no inhibition by EDTA; no inhibition by EDTA
-
additional information
no inhibition by EDTA; no inhibition by EDTA; no inhibition by EDTA
-
additional information
no inhibition by EDTA; no inhibition by EDTA; no inhibition by EDTA
-
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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
evolution
-
the enzyme belongs to the medium chain dehydrogenases
evolution
sequence analysis suggests that algal and apicomplexa M1PDHs represent a distinct type of mannitol-1-phosphate dehydrogenase in the PSLDR family
evolution
the C-terminus of MtlD from Acinetobacter baylyi is similar to dehydrogenase domains found in other dehydrogenases with a glycine-rich conserved domain (Rossmann-fold) starting at position 247 for cosubstrate binding (GIHGFGAIGGG). The N-terminal domain of MtlD is similar to members of the HAD (haloacid dehalogenase) superfamily
evolution
-
the C-terminus of MtlD from Acinetobacter baylyi is similar to dehydrogenase domains found in other dehydrogenases with a glycine-rich conserved domain (Rossmann-fold) starting at position 247 for cosubstrate binding (GIHGFGAIGGG). The N-terminal domain of MtlD is similar to members of the HAD (haloacid dehalogenase) superfamily
-
malfunction
-
deletion of gene mtlD results in a complete loss of salt-dependent mannitol biosynthesis
malfunction
the Corynebacterium glutamicum arabitol-negative DELTAmtlD deletion mutant can be complemented by heterologous expression of Bacillus methanolicus strain MGA3 operon atlABCD or gene atlD
metabolism
-
the enzyme is involved in the mannitol cycle in the fungus
metabolism
-
mannitol-1-phosphate dehydrogenase mediates the first step of two-step pathway for osmo-induced synthesis of mannitol, regulated by salinity on the transcriptional as well as on the activity level, overview
metabolism
the enzyme catalyzes the first step of the synthesis of mannitol, i.e. reduction of the photo-assimilate fructose-6-phosphate, mannitol cycle, overview
metabolism
mannitol-1-phosphate dehydrogenase MtlD is essential for mannitol biosynthesis and catalyses the first step in mannitol biosynthesis, the reduction of fructose-6-phosphate to the intermediate mannitol-1-phosphate
metabolism
the enzyme is involved in the arabitol catabolism and the pentose phosphate pathway, model of the pathways for arabitol catabolism in bacteria, overview
metabolism
-
the enzyme catalyzes the first step of the synthesis of mannitol, i.e. reduction of the photo-assimilate fructose-6-phosphate, mannitol cycle, overview
-
metabolism
-
the enzyme is involved in the arabitol catabolism and the pentose phosphate pathway, model of the pathways for arabitol catabolism in bacteria, overview
-
metabolism
-
mannitol-1-phosphate dehydrogenase MtlD is essential for mannitol biosynthesis and catalyses the first step in mannitol biosynthesis, the reduction of fructose-6-phosphate to the intermediate mannitol-1-phosphate
-
metabolism
-
the enzyme is involved in the arabitol catabolism and the pentose phosphate pathway, model of the pathways for arabitol catabolism in bacteria, overview
-
physiological function
crucial role of BbMPD in the mannitol biosynthesis of Beauveria bassiana
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
physiological function
the nutritionally versatile soil bacterium Acinetobacter baylyi ADP1 copes with salt stress by the accumulation of compatible solutes. The bacterium synthesizes the sugar alcohol mannitol de novo in response to osmotic stress. THe enzyme is essential for mannitol 1-phosphate biosynthesis, and it also possesses a unique sequence among known mannitol-1-phosphate dehydrogenases with a haloacid dehalogenase (HAD)-like phosphatase domain at the N-terminus. This domain has phosphatase activity
physiological function
after deletion of the mtlD gene, cells no longer accumulate mannitol and growth is completely impaired at high salt concentrations
physiological function
Corynebacterium glutamicum is a natural D-arabitol utilizer that requires arabitol-utilizing mannitol-1-phosphate 5-dehydrogenase MtlD for arabitol catabolism
physiological function
M1PDH is essential to endure pH, high salt concentration, and oxidative stress and is required for preventing osmotic burst by regulating pressure potential imposed by mannitol. In a mouse infection model, M1PDH is essential for bacterial survival during infection
physiological function
MpdA deletion leads to ascosporogenesis failure and results in small cleistothecia with no functional ascospores. MpdA modulates the expression of key development- and meiosis-regulatory genes during sexual development. The MpdA deletion increases hyphal branching and decreases conidial heat resistance. Mannitol production in conidia shows no difference, whereas it is decreased in mycelia and sexual cultures
physiological function
when the mannitol-1-phosphate 5-dehydrogenase gene MtlD is targeted by CRISPRi, mtlD RNA levels, and MtlD specific activities in crude extracts are decreased to about 50 %, which results in reduced biomass formation from mannitol
physiological function
-
MpdA deletion leads to ascosporogenesis failure and results in small cleistothecia with no functional ascospores. MpdA modulates the expression of key development- and meiosis-regulatory genes during sexual development. The MpdA deletion increases hyphal branching and decreases conidial heat resistance. Mannitol production in conidia shows no difference, whereas it is decreased in mycelia and sexual cultures
-
physiological function
-
M1PDH is essential to endure pH, high salt concentration, and oxidative stress and is required for preventing osmotic burst by regulating pressure potential imposed by mannitol. In a mouse infection model, M1PDH is essential for bacterial survival during infection
-
physiological function
-
the nutritionally versatile soil bacterium Acinetobacter baylyi ADP1 copes with salt stress by the accumulation of compatible solutes. The bacterium synthesizes the sugar alcohol mannitol de novo in response to osmotic stress. THe enzyme is essential for mannitol 1-phosphate biosynthesis, and it also possesses a unique sequence among known mannitol-1-phosphate dehydrogenases with a haloacid dehalogenase (HAD)-like phosphatase domain at the N-terminus. This domain has phosphatase activity
-
physiological function
-
after deletion of the mtlD gene, cells no longer accumulate mannitol and growth is completely impaired at high salt concentrations
-
physiological function
-
when the mannitol-1-phosphate 5-dehydrogenase gene MtlD is targeted by CRISPRi, mtlD RNA levels, and MtlD specific activities in crude extracts are decreased to about 50 %, which results in reduced biomass formation from mannitol
-
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enhanced tolerance to salt stress in transgenic loblolly pine simultaneously expressing two genes encoding mannitol-1-phosphate dehydrogenase and glucitol-6-phosphate dehydrogenase
-
expression in Escherichia coli
expression in transgenic Oryza sativa plants, basmati indica rice, using the Agrobacterium tumefaciens transfection and DNA integration method, leading to increased tolerance to salinity and drought in the transgenic plants compared to wild-type plants by accumulation of mannitol, overview
-
gene BbMPD, DNA and amino acid sequence determination and analysis, phylogenetic tree
gene EsM1PDH2 is located at Esi0020_0181, DNA and amino acid sequence determination and analysis, sequence comparison, real-time-PCR expression analysis, expression in Escherichia coli strain BL21(DE3)
gene EsM1PDH3 is located at Esi0080_0017, DNA and amino acid sequence determination and analysis, sequence comparison, real-time-PCR expression analysis, expression in Escherichia coli strain BL21(DE3)
gene EsM1PHD1 is located at Esi0017_0062, DNA and amino acid sequence determination and analysis, sequence comparison, real-time-PCR expression analysis, expression in Escherichia coli strain BL21(DE3)
gene MPDH1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, expression analysis
gene MPDH1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, expression analysis, recombinant expression of His-tagged EsM1PDH1 in Escherichia coli
gene MPDH2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, expression analysis
gene mtlD or ACIAD1672, DNA and amino acid sequence determination and analysis, real-time-PCR expression analysis, expression of His-tagged enzyme
-
gene mtlD, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
gene mtlD, recombinant expression in Beta vulgaris under control of a stress-inducible rd29A promoter, the transgenic plants are more resistant against stress caused by infections of fungi, e.g. Alternaria alternata, Botrytis cinerea, and Cercospora beticola. Expression profiling by semi-quantitative reverse transcription -PCR analysis shows different levels of cold-inducible expression of mtlD in independent T1 transformants in leafs and whole plants. AAccumulation of mannitol in T1 transgenic lines. Phenotypes, overview
gene mtlD, recombinant expression of the enzyme under control of constitutive promoter CaMV35S in Arachis hypogaea cv. GG 20 via transfection and introduction with Agrobacterium tumefaciens strain LBA 4404, genetic transformation and regeneration of peanut from deembryonated cotyledons. All transgenic plants show accumulation of mannitol. Under water-deficit stress, different transgenic lines have significantly different levels of mannitol suggesting multiple mechanisms controlling the activity of the enzyme encoded by the transgene and the level of gene expression
gene mtlD, transcriptional organization of the gene cluster, quantitative RT-PCR enzyme expression analysis
gene mtld1, encoded in the mannitol operon, sequence comparison, real-time PCR expression analysis, expression as His6-tagged protein in Escherichia coli strain SG13009
-
heterologous expression in Escherichia coli JM109
-
high level overexpression in Escherichia coli strain JM109
overexpression in Escherichia coli
-
overexpression of enzyme in Lactococcus lactis, small amounts of mannitol are formed in growing cells of lactate dehydrogenase deficient or phosphofructokinase-reduced strains, while resting cells of lactate-dehydrogenase deficient strain convert 25% of glucose into mannitol
-
Petunia hybrida (Hook) Vilm. cv. Mitchell is transformed with an Escherichia coli gene encoding mannitol 1-phosphate dehydrogenase. The high-mannitol containing lines are more tolerant of chilling stress than the low mannitol containing transgenic lines and wild-type. In the higher mannitol lines only 0.04% to 0.06% of the total osmotic potential generated from all solutes can be attributed to mannitol, thus its action is more like that of an osmoprotectant rather than an osmoregulator
-
recombinant expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
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Evidence for and characterization of a mannitol cycle in Eimeria tenella
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39
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-
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70
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-
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Parastagonospora nodorum (Q0U6E8), Parastagonospora nodorum
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Enhanced tolerance to salt stress in transgenic loblolly pine simultaneously expressing two genes encoding mannitol-1-phosphate dehydrogenase and glucitol-6-phosphate dehydrogenase
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brenda
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Overexpression of bacterial mtlD gene in peanut improves drought tolerance through accumulation of mannitol
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Escherichia coli (P09424)
-
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Salt induction and activation of MtlD, the key enzyme in the synthesis of the compatible solute mannitol in Acinetobacter baumannii
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Aspergillus nidulans (Q5B0F5), Aspergillus nidulans, Aspergillus nidulans ATCC 38163 (Q5B0F5)
brenda
Lopez, M.G.; Irla, M.; Brito, L.F.; Wendisch, V.F.
Characterization of D-arabitol as newly discovered carbon source of Bacillus methanolicus
Front. Microbiol.
10
1725
2019
Corynebacterium glutamicum (A0A0U4Y4V3), Bacillus methanolicus (I3E3X0), Bacillus methanolicus ATCC 53907 (I3E3X0), Bacillus methanolicus MGA3 (I3E3X0)
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Nguyen, T.; Kim, T.; Ta, H.; Yeo, W.; Choi, J.; Mizar, P.; Lee, S.; Bae, T.; Chaurasia, A.; Kim, K.
Targeting mannitol metabolism as an alternative antimicrobial strategy based on the structure-function study of mannitol-1-phosphate dehydrogenase in Staphylococcus aureus
mBio
10
e02660
2019
Staphylococcus aureus (A8YYC5), Staphylococcus aureus, Staphylococcus aureus USA300 (A8YYC5)
brenda