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Enzyme Nomenclature
Information on EC 1.1.1.17 - mannitol-1-phosphate 5-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.17
Word Map on EC 1.1.1.17
- 1.1.1.17
- fructose-6-phosphate
-
mannitol-specific
- mannitol-1-phosphatase
- tenella
-
phosphoenolpyruvate-dependent
-
1-phosphatase
- synthesis
- pharmacology
- agriculture
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.1.1.17
-
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RECOMMENDED NAME
GeneOntology No.
mannitol-1-phosphate 5-dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-mannitol 1-phosphate + NAD+ = D-fructose 6-phosphate + NADH + H+
-
-
-
-
D-mannitol 1-phosphate + NAD+ = D-fructose 6-phosphate + NADH + H+
the hydride transfer is strongly rate-determining for the overall enzymatic reaction
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
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
intramolecular phosphate transfer
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
D-mannitol-1-phosphate:NAD+ 5-oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
9028-24-4
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
hyperexpression of enzyme upon growth on mannitol as sole carbon source
-
-
Ectocarpus siliculosus Ec32 / CCAP 1310/4
Mdp1 is disrupted by insertion mutagenesis, and the resulting mpd1 strain lacks all detectable NAD+-linked mannitol 1-phosphate dehydrogenase activity
Uniprot
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
-
deletion of gene mtlD results in a complete loss of salt-dependent mannitol biosynthesis
metabolism
physiological function
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 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
sequence analysis suggests that algal and apicomplexa M1PDHs represent a distinct type of mannitol-1-phosphate dehydrogenase in the PSLDR family; sequence analysis suggests that algal and apicomplexa M1PDHs represent a distinct type of mannitol-1-phosphate dehydrogenase in the PSLDR family; 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
-
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; the enzyme catalyzes the first step of the synthesis of mannitol, i.e. reduction of the photo-assimilate fructose-6-phosphate, mannitol cycle, overview; 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
-
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
Ectocarpus siliculosus Ec32 / CCAP 1310/4
-
the enzyme catalyzes the first step of the synthesis of mannitol, i.e. reduction of the photo-assimilate fructose-6-phosphate, mannitol cycle, overview; the enzyme catalyzes the first step of the synthesis of mannitol, i.e. reduction of the photo-assimilate fructose-6-phosphate, mannitol cycle, overview; the enzyme catalyzes the first step of the synthesis of mannitol, i.e. reduction of the photo-assimilate fructose-6-phosphate, mannitol cycle, 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
-
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
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 + 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-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
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+
-
-
-
-
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+
-
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+
the enzyme shows higher activity in the reduction reaction
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
Ectocarpus siliculosus Ec32 / CCAP 1310/4
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
Ectocarpus siliculosus Ec32 / CCAP 1310/4
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+
-
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
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
?
-
D7G793;
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
?
-
D7G793;
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
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-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
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+
Q4X1A4
-
-
-
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+
-
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+
C7FDI4
-
-
-
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+
D7FMJ8, D7G793, D8LI09
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
D7FMJ8, D7G793, D8LI09
the enzyme shows higher activity in the reduction reaction
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
Ectocarpus siliculosus Ec32 / CCAP 1310/4
D7FMJ8, D7G793, D8LI09
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+
Q6FBP5
-
-
-
r
D-mannitol 1-phosphate + NADP+
D-fructose 6-phosphate + NADPH + H+
Q6FBP5
-
-
-
r
additional information
?
-
Q6FBP5
MtlD is a bifunctional enzyme of mannitol biosynthesis that combines mannitol-1-phosphate dehydrogenase and phosphatase activities in a single polypeptide chain
-
-
-
additional information
?
-
Q6FBP5
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
?
-
D7FMJ8
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
?
-
D7G793
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
?
-
D8LI09
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
?
-
Q0U6E8
mannitol 1-phosphate metabolism is required for sporulation in planta of the wheat pathogen Stagonospora nodorum
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
the NAD+-binding consensus sequence GxGxxGxGxxG is localized within the highly conserved N-terminal portion of MtlD corresponding to the amino acid residues 9-19
NADH
-
maximal specific activity with NADH is 15fold lower compared to NADPH
additional information
isozyme EsM1PDH1 highly prefers NADH/NAD+ to NADP+/NADPH; isozyme EsM1PDH1 highly prefers NADH/NAD+ to NADP+/NADPH; isozyme EsM1PDH1 highly prefers NADH/NAD+ to NADP+/NADPH
-
additional information
D7G793;
isozyme EsM1PDH1 highly prefers NADH/NAD+ to NADP+/NADPH; isozyme EsM1PDH1 highly prefers NADH/NAD+ to NADP+/NADPH; isozyme EsM1PDH1 highly prefers NADH/NAD+ to NADP+/NADPH
-
additional information
isozyme EsM1PDH1 highly prefers NADH/NAD+ to NADP+/NADPH; isozyme EsM1PDH1 highly prefers NADH/NAD+ to NADP+/NADPH; isozyme EsM1PDH1 highly prefers NADH/NAD+ to NADP+/NADPH
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
NaCl
additional information
-
5 and 10 mM concentrations of MgSO4, MnSO4, FeCl3, ZnCl2, CoCl2, and LiCl have no effect on the nezyme activity
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-hydroxymercuribenzoate
strong inhibition; strong inhibition; strong inhibition
adenosine diphosphoribose
-
competitive inhibition with respect to NADH, noncompetitive inhibition with respect to D-fructose 6-phosphate
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
diethyldithiocarbamate
-
95% inactivation, prevented by presence of 2-mercaptoethanol
N-ethylmaleimide
-
1 mM, 80% inhibition of reduction and oxidation reaction
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
D-fructose 6-phosphate
-
competitive inhibition with respect to D-mannitol 1-phosphate
D-fructose 6-phosphate
-
56% inhibition of mannitol 1-phosphate oxidation
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
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
D7G793;
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.19
D-fructose 6-phosphate
recombinant enzyme, pH 7.0, 30°C; recombinant enzyme, pH 7.0, 30°C; recombinant enzyme, pH 7.0, 30°C
0.38
D-mannitol 1-phosphate
recombinant enzyme, pH 9.0, 30°C; recombinant enzyme, pH 9.0, 30°C; recombinant enzyme, pH 9.0, 30°C
0.02
NAD+
recombinant enzyme, pH 9.0, 30°C; recombinant enzyme, pH 9.0, 30°C; recombinant enzyme, pH 9.0, 30°C
16
NADH
recombinant enzyme, pH 7.0, 30°C; recombinant enzyme, pH 7.0, 30°C; recombinant enzyme, pH 7.0, 30°C
additional information
additional information
kinetic isotope effects, overview
-
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
-
additional information
additional information
Michaelis-Menten kinetics; Michaelis-Menten kinetics; Michaelis-Menten kinetics
-
additional information
additional information
D7G793;
Michaelis-Menten kinetics; Michaelis-Menten kinetics; Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics; Michaelis-Menten kinetics; Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
170
D-fructose 6-phosphate
recombinant enzyme, pH 7.0, 30°C; recombinant enzyme, pH 7.0, 30°C; recombinant enzyme, pH 7.0, 30°C
29
D-mannitol 1-phosphate
recombinant enzyme, pH 9.0, 30°C; recombinant enzyme, pH 9.0, 30°C; recombinant enzyme, pH 9.0, 30°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.33
D-fructose 6-phosphate
-
able to inhibit the forward reaction to 100%, competitive inhibition with respect to mannitol 1-phosphate, noncompetitive inhibition with respect to NAD+
2
ADP
-
competitive inhibition with respect to NADH, noncompetitive inhibition with respect to fructose 6-phosphate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.002
algal extract, pH 6.3, 30°C, in presence of NaCl; algal extract, pH 6.3, 30°C, in presence of NaCl; algal extract, pH 6.3, 30°C, in presence of NaCl
0.014
recombinant enzyme, D-mannitol 1-phosphate oxidation, pH 9.0, 30°C; recombinant enzyme, D-mannitol 1-phosphate oxidation, pH 9.0, 30°C; recombinant enzyme, D-mannitol 1-phosphate oxidation, pH 9.0, 30°C
0.016
purified recombinant enzyme, D-mannitol 1-phosphate oxidation, pH 9.0, 30°C; purified recombinant enzyme, D-mannitol 1-phosphate oxidation, pH 9.0, 30°C; purified recombinant enzyme, D-mannitol 1-phosphate oxidation, pH 9.0, 30°C
0.026
recombinant enzyme, D-fructose 6-phosphate reduction, pH 7.0, 30°C; recombinant enzyme, D-fructose 6-phosphate reduction, pH 7.0, 30°C; recombinant enzyme, D-fructose 6-phosphate reduction, pH 7.0, 30°C
0.046
purified recombinant enzyme, D-fructose 6-phosphate reduction, pH 7.0, 30°C; purified recombinant enzyme, D-fructose 6-phosphate reduction, pH 7.0, 30°C; purified recombinant enzyme, D-fructose 6-phosphate reduction, pH 7.0, 30°C
2.8
-
premature conidiospores, pH not specified in the publication, temperature not specified in the publication
3.32
-
recombinant enzyme, crude extract, pH 7.5, 30°C, fructose 6-phosphate reduction
18.6
-
mature conidiospores, pH not specified in the publication, temperature not specified in the publication
68.3
-
non-sporulating mycelium, pH not specified in the publication, temperature not specified in the publication
453.9
-
sporulating mycelium, pH not specified in the publication, temperature not specified in the publication
additional information
additional information
-
1 unit defined as change of 0.01 in optical density at 340 nm during 30-90 second interval; 860 U/mg protein
additional information
-
1 unit defined as change of 0.01 in optical density at 340 nm during 30-90 second interval; 240 U/mg protein
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.3
reduction reaction; reduction reaction; reduction reaction
7.1
7.5
9.5
7
D-fructose 6-phosphate reduction; D-fructose 6-phosphate reduction; D-fructose 6-phosphate reduction
9
oxidation reaction; oxidation reaction; oxidation reaction
9
D-mannitol 1-phosphate oxidation; D-mannitol 1-phosphate oxidation; D-mannitol 1-phosphate oxidation
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
-
for the oxidative and reductive direction of the reactions under conditions where substrate is limiting (kcat/K) or saturating (kcat)
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 50
35% of maximum activity at 5-10°C, less than 5% at 50°C; 35% of maximum activity at 5-10°C, less than 5% at 50°C; 35% of maximum activity at 5-10°C, less than 5% at 50°C
10 - 40
-
70% of maximal activity at 15°C or 35°C, and 50% at 10°C or 40°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
reductase activity affected by the presence of nitrate during growth
additional information
-
poor expression of MpdA in conidiospores, expression anaylsis
additional information
-
gene mtlD is constitutively expressed even when no mannitol wis present in the growth medium
additional information
-
gene mtlD is constitutively expressed even when no mannitol wis present in the growth medium
-
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
A7X522
Staphylococcus aureus (strain Mu3 / ATCC 700698);
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
42000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
?
x * 47000, isozyme EsM1PHD3; x * 58000, isozyme EsM1PHD1; x * 60000, isozyme EsM1PHD2
?
x * 42000, recombinant His-tagged EsM1PDH1 isozyme, SDS-PAGE; x * 42000, recombinant His-tagged EsM1PDH1 isozyme, SDS-PAGE; x * 42000, recombinant His-tagged EsM1PDH1 isozyme, SDS-PAGE
?
Ectocarpus siliculosus Ec32 / CCAP 1310/4
-
x * 47000, isozyme EsM1PHD3; x * 58000, isozyme EsM1PHD1; x * 60000, isozyme EsM1PHD2
-
additional information
structure-based sequence comparisons, overview; structure-based sequence comparisons, overview; structure-based sequence comparisons, overview
additional information
D7G793;
structure-based sequence comparisons, overview; structure-based sequence comparisons, overview; structure-based sequence comparisons, overview
additional information
structure-based sequence comparisons, overview; structure-based sequence comparisons, overview; structure-based sequence comparisons, overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
40 - 50
-
half-life is 20 h at 40°C, the enzyme displays remarkable stability at 40°C and even at 50°C
60
30
-
half-life: 2 h, decreasing stability in the presence of zinc ions
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 0.05 M Tris-HCl, pH 7.5, presence of 2-mercaptoethanol, long term storage without loss of activity
-
4°C, 0.05 M Tris-HCl, pH 7.6, 0.05 M NaCl, 5 mM 2-mercaptoethanol, stable for weeks
-
4°C, purified native enzyme, the enzyme retains high activity during storage for two weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme 2.1fold from Escherichia coli by affinity chromatography
recombinant His-tagged EsM1PDH1 from Escherichia coli by nickel affinity chromatography and gel filtration; recombinant His-tagged EsM1PDH1 from Escherichia coli by nickel affinity chromatography and gel filtration; recombinant His-tagged EsM1PDH1 from Escherichia coli by nickel affinity chromatography and gel filtration
recombinant His6-tagged nezyme from Escherichia coli strain SG13009 by nickel affinity chromatography
-
to homogeneity, chromatography techniques
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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 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 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 mtld1, encoded in the mannitol operon, sequence comparison, real-time PCR expression analysis, expression as His6-tagged protein in Escherichia coli strain SG13009
-
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
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
induction of the enzyme in cell culture by isopropyl 1-thio-beta-D-galactopyranoside
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
construction of a disruption mutant, that shows elevated levels of trehalose, but is viable, and the conidia germinate normally, the mutant is less pathogenic in infected tobacco plants compared to the wild-type fungus, overview
additional information
-
construction of a disruption mutant, that shows elevated levels of trehalose, but is viable, and the conidia germinate normally, the mutant is less pathogenic in infected tobacco plants compared to the wild-type fungus, overview
-
additional information
-
gene disruption mutant, reduced growth on glucitol, no growth on mannitol as sole carbon source
additional information
-
mannitol accumulation in mtlD transgenics is expected to confer a range of biotic and abiotic-stress tolerance, phenotypes, overview
additional information
-
C-terminal truncation, lacking 162 amino acids of the C-terminus, 10% in vivo activity compared to the wild-type form
additional information
-
the enzyme competes with two sorbitol-6-phosphate dehydrogenase for D-fructose 6-phosphate, a mutant strain deficient for both L- and D-lactate dehydrogenase activities shows two highly active sorbitol-6-phosphate dehydrogenase genes srlD1 and srlD2, that are constitutively expressed at a high level in this mutant, the mannitol production of the mutant strain is reduced compared to the wild-type, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
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. Metabolic engineering of osmoprotectant synthesis pathways can be used to improve stress tolerance in horticultural crops
pharmacology
-
inhibition of AfM1PDH might be a useful target for therapy of Aspergillus fumigatus infections
synthesis
synthesis
-
strategy for mannitol production in Lactococcus, most promising is overexpression of enzyme in a lactate-dehydrogenase deficient strain
synthesis
hydrogen transfer from formate to D-fructose 6-phosphate, mediated by NAD(H) and catalyzed by a coupled enzyme system of purified Candida boidinii formate dehydrogenase and AfM1PDH, is used for the preparative synthesis of D-mannitol 1-phosphate or, by applying an analogous procedure using deuterio formate, the 5-[2H] derivative thereof, overview
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.17)
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