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Information on EC 1.1.1.17 - mannitol-1-phosphate 5-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.17
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.17 mannitol-1-phosphate 5-dehydrogenase
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 1.1.1.17
- fructose-6-phosphate
- mannitol-1-phosphatase
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mannitol-specific
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phosphoenolpyruvate-dependent
- ectocarpus
- arabitol
-
1-phosphatase
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mannitol-producing
- synthesis
- agriculture
- analysis
- pharmacology
showSynonyms
mannitol-1-phosphate dehydrogenase, mannitol 1-phosphate dehydrogenase, m1pdh, d-mannitol-1-phosphate dehydrogenase, mannitol 1-phosphate 5-dehydrogenase, bbmpd, esm1pdh1, mannitol-1-phosphate 5-dehydrogenase, esm1pdh2, mtl-1-p dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AbMtlD
bifunctional mannitol-1-phosphate dehydrogenase/phosphatase
BMMGA3_01075
BMMGA3_RS01080
D-mannitol-1-phosphate dehydrogenase
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dehydrogenase, mannitol 1-phosphate
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fructose 6-phosphate reductase
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HAD hydrolase, family IA, variant 3
hexose reductase
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HMPREF0010_00722
M1PDH
M1PDH1
M1PDH2
M1PDH3
mannitol 1-phosphate 5-dehydrogenase
mannitol 1-phosphate dehydrogenase
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-
-
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mannitol-1-phosphate dehydrogenase
MpdA
MPDH
Mtl-1-P dehydrogenase
MtlD
additional information
bifunctional mannitol-1-phosphate dehydrogenase/phosphatase
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bifunctional mannitol-1-phosphate dehydrogenase/phosphatase
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bifunctional mannitol-1-phosphate dehydrogenase/phosphatase
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bifunctional mannitol-1-phosphate dehydrogenase/phosphatase
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-
bifunctional mannitol-1-phosphate dehydrogenase/phosphatase
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-
bifunctional mannitol-1-phosphate dehydrogenase/phosphatase
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-
bifunctional mannitol-1-phosphate dehydrogenase/phosphatase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-mannitol 1-phosphate + NAD+ = D-fructose 6-phosphate + NADH + H+
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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
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oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
MetaCyc
mannitol cycle, mannitol degradation I
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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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-fructose-6-phosphate + NADH
D-mannitol-1-phosphate + NAD+
-
Substrates: -
Products: -
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r
D-mannitol 1-phosphate + 3-acetylpyridine-NAD+
D-fructose 6-phosphate + ?
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Substrates: 7% of the activity compared to NAD+
Products: -
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?
D-mannitol 1-phosphate + acetylpyridine adenine dinucleotide
D-fructose 6-phosphate + ?
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Substrates: 50% of the activity compared to NAD+
Products: -
Products: -
?
D-mannitol 1-phosphate + dichlorophenolindophenol
D-fructose 6-phosphate + reduced dichlorophenolindophenol
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Substrates: higher activity than for NAD+
Products: -
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?
D-mannitol 1-phosphate + nicotinamide 6-(2-hydoxyethylamino) purine dinucleotide
D-fructose 6-phosphate + ?
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Substrates: 75% of the activity compared to NAD+
Products: -
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?
D-mannitol 1-phosphate + nicotinamide hypoxanthine dinucleotide
D-fructose 6-phosphate + ?
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Substrates: 84% of the activity compared to NAD+
Products: -
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?
D-mannitol-1-phosphate + NAD+
D-fructose-6-phosphate + NADH
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Substrates: -
Products: -
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r
D-sorbitol 6-phosphate + NAD+
D-glucose 6-phosphate + NADH + H+
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Substrates: 38.8% of the activity compared to D-mannitol 1-phosphate
Products: -
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r
ethanol + NAD+
acetaldehyde + NADH
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Substrates: 56% of the activity compared to D-mannitol 1-phosphate
Products: -
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r
D-arabitol 1-phosphate + NAD+
D-xylulose 5-phosphate + NADH + H+
Substrates: -
Products: -
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r
D-arabitol 1-phosphate + NAD+
D-xylulose 5-phosphate + NADH + H+
Substrates: -
Products: -
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r
D-arabitol 1-phosphate + NAD+
D-xylulose 5-phosphate + NADH + H+
Substrates: -
Products: -
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r
D-arabitol 1-phosphate + NAD+
D-xylulose 5-phosphate + NADH + H+
A0A0U4Y4V3
Substrates: -
Products: -
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r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: -
Products: -
Products: -
?
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: -
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: higher activity with NADPH compared to NADH
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: -
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: higher activity with NADPH compared to NADH
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: -
Products: -
Products: -
?
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: -
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: higher activity with NADPH compared to NADH
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Acinetobacter baumannii CCUG 19606
Substrates: -
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Acinetobacter baumannii CCUG 19606
Substrates: higher activity with NADPH compared to NADH
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: -
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: higher activity with NADPH compared to NADH
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: -
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: higher activity with NADPH compared to NADH
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: -
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: higher activity with NADPH compared to NADH
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: -
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: higher activity with NADPH compared to NADH
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: -
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: higher activity with NADPH compared to NADH
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: -
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: higher activity with NADPH compared to NADH
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
-
Substrates: -
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
-
Substrates: -
Products: -
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r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: -
Products: -
Products: -
r
D-fructose 6-phosphate + NADPH + H+
D-mannitol 1-phosphate + NADP+
Substrates: -
Products: -
Products: -
?
D-fructose 6-phosphate + NADPH + H+
D-mannitol 1-phosphate + NADP+
Substrates: higher activity with NADPH compared to NADH
Products: -
Products: -
r
D-fructose 6-phosphate + NADPH + H+
D-mannitol 1-phosphate + NADP+
Substrates: higher activity with NADPH compared to NADH
Products: -
Products: -
r
D-fructose 6-phosphate + NADPH + H+
D-mannitol 1-phosphate + NADP+
Substrates: -
Products: -
Products: -
?
D-fructose 6-phosphate + NADPH + H+
D-mannitol 1-phosphate + NADP+
Substrates: higher activity with NADPH compared to NADH
Products: -
Products: -
r
D-fructose 6-phosphate + NADPH + H+
D-mannitol 1-phosphate + NADP+
Acinetobacter baumannii CCUG 19606
Substrates: higher activity with NADPH compared to NADH
Products: -
Products: -
r
D-fructose 6-phosphate + NADPH + H+
D-mannitol 1-phosphate + NADP+
Substrates: higher activity with NADPH compared to NADH
Products: -
Products: -
r
D-fructose 6-phosphate + NADPH + H+
D-mannitol 1-phosphate + NADP+
Substrates: higher activity with NADPH compared to NADH
Products: -
Products: -
r
D-fructose 6-phosphate + NADPH + H+
D-mannitol 1-phosphate + NADP+
Substrates: higher activity with NADPH compared to NADH
Products: -
Products: -
r
D-fructose 6-phosphate + NADPH + H+
D-mannitol 1-phosphate + NADP+
Substrates: higher activity with NADPH compared to NADH
Products: -
Products: -
r
D-fructose 6-phosphate + NADPH + H+
D-mannitol 1-phosphate + NADP+
Substrates: higher activity with NADPH compared to NADH
Products: -
Products: -
r
D-fructose 6-phosphate + NADPH + H+
D-mannitol 1-phosphate + NADP+
Substrates: higher activity with NADPH compared to NADH
Products: -
Products: -
r
D-fructose 6-phosphate + NADPH + H+
D-mannitol 1-phosphate + NADP+
-
Substrates: -
Products: -
Products: -
r
D-fructose 6-phosphate + NADPH + H+
D-mannitol 1-phosphate + NADP+
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: the enzyme is involved in mannitol biosynthesis, which is required for plant pathogenicity by Alternaria alternata, overview
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: the enzyme is involved in mannitol biosynthesis, which is required for plant pathogenicity by Alternaria alternata, overview
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
Substrates: 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
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: AfM1PDH primarily functions as a D-fructose-6-phosphate reductase and is specific for its natural pair of substrates
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: highly specific for both substrates
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: random bi-bi kinetic with two dead-end complexes
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
A0A0U4Y4V3
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
Substrates: the enzyme shows higher activity in the reduction reaction
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
Ectocarpus siliculosus Ec32 / CCAP 1310/4
Substrates: the enzyme shows higher activity in the reduction reaction
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
Ectocarpus siliculosus Ec32 / CCAP 1310/4
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: part of the phosphoenolpyruvate phosphotransferase system
Products: -
Products: -
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: highly specific for both substrates
Products: -
Products: -
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: highly specific for both substrates
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: favours reverse reaction
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: highly specific for both substrates
Products: -
Products: -
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: the enzyme competes with two sorbitol-6-phosphate dehydrogenase for D-fructose 6-phosphate, metabolic flux in engineered organisms, overview
Products: -
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r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
Substrates: -
Products: -
Products: -
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
Substrates: -
Products: -
Products: -
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: highly specific for both substrates
Products: -
Products: -
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: part of the phosphoenolpyruvate phosphotransferase system
Products: -
Products: -
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NADP+
D-fructose 6-phosphate + NADPH + H+
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NADP+
D-fructose 6-phosphate + NADPH + H+
Substrates: -
Products: -
Products: -
r
additional information
?
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Substrates: D-mannitol 1-phosphate (M1P) binds to the active site composed of the N- and C-terminal subdomains of the PD domain. Here, M1P is positioned in a straight chain configuration, such that the phosphate and mannitol moieties make extensive contact with the core and cap subdomains, respectively. Upon M1P binding, the alpha2-turn-alpha3 region from the cap subdomain reorients toward the active site, and the sugar alcohol moiety is sandwiched by the alpha2-turn-alpha3 and alpha1. Substrate binding analysis, overview
Products: -
Products: -
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additional information
?
-
Substrates: D-mannitol 1-phosphate (M1P) binds to the active site composed of the N- and C-terminal subdomains of the PD domain. Here, M1P is positioned in a straight chain configuration, such that the phosphate and mannitol moieties make extensive contact with the core and cap subdomains, respectively. Upon M1P binding, the alpha2-turn-alpha3 region from the cap subdomain reorients toward the active site, and the sugar alcohol moiety is sandwiched by the alpha2-turn-alpha3 and alpha1. Substrate binding analysis, overview
Products: -
Products: -
-
additional information
?
-
Substrates: D-mannitol 1-phosphate (M1P) binds to the active site composed of the N- and C-terminal subdomains of the PD domain. Here, M1P is positioned in a straight chain configuration, such that the phosphate and mannitol moieties make extensive contact with the core and cap subdomains, respectively. Upon M1P binding, the alpha2-turn-alpha3 region from the cap subdomain reorients toward the active site, and the sugar alcohol moiety is sandwiched by the alpha2-turn-alpha3 and alpha1. Substrate binding analysis, overview
Products: -
Products: -
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additional information
?
-
Acinetobacter baumannii CCUG 19606
Substrates: D-mannitol 1-phosphate (M1P) binds to the active site composed of the N- and C-terminal subdomains of the PD domain. Here, M1P is positioned in a straight chain configuration, such that the phosphate and mannitol moieties make extensive contact with the core and cap subdomains, respectively. Upon M1P binding, the alpha2-turn-alpha3 region from the cap subdomain reorients toward the active site, and the sugar alcohol moiety is sandwiched by the alpha2-turn-alpha3 and alpha1. Substrate binding analysis, overview
Products: -
Products: -
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additional information
?
-
Substrates: D-mannitol 1-phosphate (M1P) binds to the active site composed of the N- and C-terminal subdomains of the PD domain. Here, M1P is positioned in a straight chain configuration, such that the phosphate and mannitol moieties make extensive contact with the core and cap subdomains, respectively. Upon M1P binding, the alpha2-turn-alpha3 region from the cap subdomain reorients toward the active site, and the sugar alcohol moiety is sandwiched by the alpha2-turn-alpha3 and alpha1. Substrate binding analysis, overview
Products: -
Products: -
-
additional information
?
-
Substrates: D-mannitol 1-phosphate (M1P) binds to the active site composed of the N- and C-terminal subdomains of the PD domain. Here, M1P is positioned in a straight chain configuration, such that the phosphate and mannitol moieties make extensive contact with the core and cap subdomains, respectively. Upon M1P binding, the alpha2-turn-alpha3 region from the cap subdomain reorients toward the active site, and the sugar alcohol moiety is sandwiched by the alpha2-turn-alpha3 and alpha1. Substrate binding analysis, overview
Products: -
Products: -
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additional information
?
-
Substrates: D-mannitol 1-phosphate (M1P) binds to the active site composed of the N- and C-terminal subdomains of the PD domain. Here, M1P is positioned in a straight chain configuration, such that the phosphate and mannitol moieties make extensive contact with the core and cap subdomains, respectively. Upon M1P binding, the alpha2-turn-alpha3 region from the cap subdomain reorients toward the active site, and the sugar alcohol moiety is sandwiched by the alpha2-turn-alpha3 and alpha1. Substrate binding analysis, overview
Products: -
Products: -
-
additional information
?
-
Substrates: D-mannitol 1-phosphate (M1P) binds to the active site composed of the N- and C-terminal subdomains of the PD domain. Here, M1P is positioned in a straight chain configuration, such that the phosphate and mannitol moieties make extensive contact with the core and cap subdomains, respectively. Upon M1P binding, the alpha2-turn-alpha3 region from the cap subdomain reorients toward the active site, and the sugar alcohol moiety is sandwiched by the alpha2-turn-alpha3 and alpha1. Substrate binding analysis, overview
Products: -
Products: -
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additional information
?
-
Substrates: D-mannitol 1-phosphate (M1P) binds to the active site composed of the N- and C-terminal subdomains of the PD domain. Here, M1P is positioned in a straight chain configuration, such that the phosphate and mannitol moieties make extensive contact with the core and cap subdomains, respectively. Upon M1P binding, the alpha2-turn-alpha3 region from the cap subdomain reorients toward the active site, and the sugar alcohol moiety is sandwiched by the alpha2-turn-alpha3 and alpha1. Substrate binding analysis, overview
Products: -
Products: -
-
additional information
?
-
Substrates: D-mannitol 1-phosphate (M1P) binds to the active site composed of the N- and C-terminal subdomains of the PD domain. Here, M1P is positioned in a straight chain configuration, such that the phosphate and mannitol moieties make extensive contact with the core and cap subdomains, respectively. Upon M1P binding, the alpha2-turn-alpha3 region from the cap subdomain reorients toward the active site, and the sugar alcohol moiety is sandwiched by the alpha2-turn-alpha3 and alpha1. Substrate binding analysis, overview
Products: -
Products: -
-
additional information
?
-
Substrates: MtlD is a bifunctional enzyme of mannitol biosynthesis that combines mannitol-1-phosphate dehydrogenase and phosphatase activities in a single polypeptide chain
Products: -
Products: -
?
additional information
?
-
Substrates: MtlD is a bifunctional enzyme of mannitol biosynthesis that combines mannitol-1-phosphate dehydrogenase and phosphatase activities in a single polypeptide chain
Products: -
Products: -
?
additional information
?
-
-
Substrates: important role for Lys213 in the catalytic mechanism of M1PDH
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: required for assimilation of mannitol and glucitol
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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+
Products: -
Products: -
?
additional information
?
-
Substrates: 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)
Products: -
Products: -
?
additional information
?
-
Substrates: 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)
Products: -
Products: -
?
additional information
?
-
Substrates: 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)
Products: -
Products: -
?
additional information
?
-
Substrates: EsM1PDH1cat isozyme is specific for D-fructose 6-phosphate and D-mannitol 1-phosphate
Products: -
Products: -
?
additional information
?
-
Substrates: EsM1PDH1cat isozyme is specific for D-fructose 6-phosphate and D-mannitol 1-phosphate
Products: -
Products: -
?
additional information
?
-
Substrates: EsM1PDH1cat isozyme is specific for D-fructose 6-phosphate and D-mannitol 1-phosphate
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with D-glucose 6-phosphate, sorbitol 6-phosphate, D-fructose 1-phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with D-glucose 6-phosphate, sorbitol 6-phosphate, D-fructose 1-phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: mannitol 1-phosphate metabolism is required for sporulation in planta of the wheat pathogen Stagonospora nodorum
Products: -
Products: -
?
additional information
?
-
-
Substrates: mannitol 1-phosphate metabolism is required for sporulation in planta of the wheat pathogen Stagonospora nodorum
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-fructose 6-phosphate + NADPH + H+
D-mannitol 1-phosphate + NADP+
-
Substrates: -
Products: -
Products: -
r
D-sorbitol 6-phosphate + NAD+
D-glucose 6-phosphate + NADH + H+
-
Substrates: 38.8% of the activity compared to D-mannitol 1-phosphate
Products: -
Products: -
r
ethanol + NAD+
acetaldehyde + NADH
-
Substrates: 56% of the activity compared to D-mannitol 1-phosphate
Products: -
Products: -
r
D-arabitol 1-phosphate + NAD+
D-xylulose 5-phosphate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-arabitol 1-phosphate + NAD+
D-xylulose 5-phosphate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-arabitol 1-phosphate + NAD+
D-xylulose 5-phosphate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: -
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: -
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: -
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Acinetobacter baumannii CCUG 19606
Substrates: -
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: -
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: -
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: -
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: -
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: -
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
Substrates: -
Products: -
Products: -
r
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
-
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: the enzyme is involved in mannitol biosynthesis, which is required for plant pathogenicity by Alternaria alternata, overview
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: the enzyme is involved in mannitol biosynthesis, which is required for plant pathogenicity by Alternaria alternata, overview
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: AfM1PDH primarily functions as a D-fructose-6-phosphate reductase and is specific for its natural pair of substrates
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: highly specific for both substrates
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: random bi-bi kinetic with two dead-end complexes
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
A0A0U4Y4V3
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
Substrates: the enzyme shows higher activity in the reduction reaction
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
Ectocarpus siliculosus Ec32 / CCAP 1310/4
Substrates: the enzyme shows higher activity in the reduction reaction
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: part of the phosphoenolpyruvate phosphotransferase system
Products: -
Products: -
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: highly specific for both substrates
Products: -
Products: -
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: highly specific for both substrates
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: favours reverse reaction
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: highly specific for both substrates
Products: -
Products: -
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: the enzyme competes with two sorbitol-6-phosphate dehydrogenase for D-fructose 6-phosphate, metabolic flux in engineered organisms, overview
Products: -
Products: -
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: highly specific for both substrates
Products: -
Products: -
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: part of the phosphoenolpyruvate phosphotransferase system
Products: -
Products: -
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NADP+
D-fructose 6-phosphate + NADPH + H+
Substrates: -
Products: -
Products: -
r
D-mannitol 1-phosphate + NADP+
D-fructose 6-phosphate + NADPH + H+
Substrates: -
Products: -
Products: -
r
additional information
?
-
Substrates: MtlD is a bifunctional enzyme of mannitol biosynthesis that combines mannitol-1-phosphate dehydrogenase and phosphatase activities in a single polypeptide chain
Products: -
Products: -
?
additional information
?
-
Substrates: MtlD is a bifunctional enzyme of mannitol biosynthesis that combines mannitol-1-phosphate dehydrogenase and phosphatase activities in a single polypeptide chain
Products: -
Products: -
?
additional information
?
-
-
Substrates: required for assimilation of mannitol and glucitol
Products: -
Products: -
?
additional information
?
-
Substrates: 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)
Products: -
Products: -
?
additional information
?
-
Substrates: 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)
Products: -
Products: -
?
additional information
?
-
Substrates: 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)
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: mannitol 1-phosphate metabolism is required for sporulation in planta of the wheat pathogen Stagonospora nodorum
Products: -
Products: -
?
additional information
?
-
-
Substrates: mannitol 1-phosphate metabolism is required for sporulation in planta of the wheat pathogen Stagonospora nodorum
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
additional information
isozyme EsM1PDH1 highly prefers NADH/NAD+ to NADP+/NADPH
-
additional information
isozyme EsM1PDH1 highly prefers NADH/NAD+ to NADP+/NADPH
-
additional information
AbMtlD catalyzes the reduction of F6P with NADH, and the specificity constant (kcat/Km) for NADH is 20fold lower than that of NADPH, AbMtlD exhibits a higher specificity for NADPH. The binding mode of NADH in the closed state is nearly identical to the NADPH-binding mode, apart from those residues that are involved in the interaction with the NADPH C2'O-phosphate moiety
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
required, Mg2+ binding is observed proximal to D16 in wild-type AbMtlD, indicating the importance of D16 in Mg2+ coordination
NaCl
additional information
NaCl
activity is strictly salt dependent, with highest stimulation at 600 mM NaCl
additional information
enzyme MtlD has a requirement for salt and high osmolarity
additional information
-
5 and 10 mM concentrations of MgSO4, MnSO4, FeCl3, ZnCl2, CoCl2, and LiCl have no effect on the enzyme activity
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INHIBITOR
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
dihydrocelastrol
competitive inhibitor, presence of dihydrocelastrol effectively reduces bacterial cell viability during host infection
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
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 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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
sodium gluconate
at 1.5 M, 135% of maximum activity obtained with NaCl
sodium glutamate
highest stimulations up to 41 U/mg at 0.8-1.2 M
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Role of mannitol metabolism in the pathogenicity of the necrotrophic fungus Alternaria brassicicola.
Infections
Targeting Mannitol Metabolism as an Alternative Antimicrobial Strategy Based on the Structure-Function Study of Mannitol-1-Phosphate Dehydrogenase in Staphylococcus aureus.
Lymphatic Metastasis
IMPDH2 is highly expressed in breast cancer and predicts unfavourable prognosis.
Neoplasm Metastasis
IMPDH2 is highly expressed in breast cancer and predicts unfavourable prognosis.
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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
1 - 1.8
D-fructose 6-phosphate
mutant H434C/Y469C, pH 7.5, 34°C
0.0886
D-mannitol 1-phosphate
pH 7.5, temperature not specified in the publication
0.38
D-mannitol 1-phosphate
recombinant enzyme, pH 9.0, 30°C
additional information
additional information
kinetic isotope effects, overview
-
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
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2256.91
D-fructose 6-phosphate
mutant A466C/Y427C, pH 7.5, 34°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
139.06
D-fructose 6-phosphate
mutant A466C/Y427C, pH 7.5, 34°C
148.98
D-fructose 6-phosphate
mutant H434C/Y469C, pH 7.5, 34°C
170
D-fructose 6-phosphate
recombinant enzyme, pH 7.0, 30°C
29
D-mannitol 1-phosphate
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+
0.004
dihydrocelastrol
pH 7.5, temperature not specified in the publication
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
0.014
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
0.02
arabitol phosphate dehydrogenase activity in mannitol grown cells of strains MG3, pH 7.2, 30°C
0.026
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
0.05
arabitol phosphate dehydrogenase activity in arabitol grown cells of strains MG3, pH 7.2, 30°C
18.6
-
mature conidiospores, pH not specified in the publication, temperature not specified in the publication
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
453.9
-
sporulating mycelium, 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
additional information
additional information
-
1 unit defined as change of 0.01 in optical density at 340 nm during 30-90 second interval
additional information
-
1 unit defined as change of 0.01 in optical density at 340 nm during 30-90 second interval
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.1
7.2
7.5
9.5
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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)
6 - 9
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 40
-
70% of maximal activity at 15°C or 35°C, and 50% at 10°C or 40°C
5 - 50
35% of maximum activity at 5-10°C, less than 5% at 50°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
hyperexpression of enzyme upon growth on mannitol as sole carbon source
-
-
brenda
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
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
reductase activity affected by the presence of nitrate during growth
brenda
additional information
-
poor expression of MpdA in conidiospores, expression anaylsis
brenda
additional information
growth of Bacillus methanolicus strain MGA3 on arabitol as single carbon source and as co-substrate to mannitol. Although arabitol supports growth of strain MGA3 as a sole source of carbon and energy, the strain grows at a lower growth rate than with its preferred sugar alcohol substrate mannitol. Mannitol is utilized faster than arabitol and co-consumption of both sugar alcohols is observed, overview
brenda
additional information
-
growth of Bacillus methanolicus strain MGA3 on arabitol as single carbon source and as co-substrate to mannitol. Although arabitol supports growth of strain MGA3 as a sole source of carbon and energy, the strain grows at a lower growth rate than with its preferred sugar alcohol substrate mannitol. Mannitol is utilized faster than arabitol and co-consumption of both sugar alcohols is observed, overview
-
brenda
additional information
-
growth of Bacillus methanolicus strain MGA3 on arabitol as single carbon source and as co-substrate to mannitol. Although arabitol supports growth of strain MGA3 as a sole source of carbon and energy, the strain grows at a lower growth rate than with its preferred sugar alcohol substrate mannitol. Mannitol is utilized faster than arabitol and co-consumption of both sugar alcohols is observed, overview
-
brenda
additional information
-
gene mtlD is constitutively expressed even when no mannitol wis present in the growth medium
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
the enzyme belongs to the medium chain dehydrogenases
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
evolution
evolutionary adaptation of AbMtlD by fusion of dehydrogenase and phosphatase domains to facilitate efficient unidirectional enzymatic production of mannitol, unifying regulatory control and minimizing the intracellular concentration of toxic mannitol-1-phosphate during salt stress. Bifunctional M1P dehydrogenase (DH)/phosphatase (PD) is composed of an N-terminal PD domain belonging to the haloacid dehalogenase (HAD) superfamily and a C-terminal DH domain. The catalytic residues (D16, D18, T118, K151, E175, and D176) from the core domain are conserved in the HAD family. Residues at the active site of the cap subdomain are highly distinct among the members of the HAD family
evolution
-
evolutionary adaptation of AbMtlD by fusion of dehydrogenase and phosphatase domains to facilitate efficient unidirectional enzymatic production of mannitol, unifying regulatory control and minimizing the intracellular concentration of toxic mannitol-1-phosphate during salt stress. Bifunctional M1P dehydrogenase (DH)/phosphatase (PD) is composed of an N-terminal PD domain belonging to the haloacid dehalogenase (HAD) superfamily and a C-terminal DH domain. The catalytic residues (D16, D18, T118, K151, E175, and D176) from the core domain are conserved in the HAD family. Residues at the active site of the cap subdomain are highly distinct among the members of the HAD 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
-
evolutionary adaptation of AbMtlD by fusion of dehydrogenase and phosphatase domains to facilitate efficient unidirectional enzymatic production of mannitol, unifying regulatory control and minimizing the intracellular concentration of toxic mannitol-1-phosphate during salt stress. Bifunctional M1P dehydrogenase (DH)/phosphatase (PD) is composed of an N-terminal PD domain belonging to the haloacid dehalogenase (HAD) superfamily and a C-terminal DH domain. The catalytic residues (D16, D18, T118, K151, E175, and D176) from the core domain are conserved in the HAD family. Residues at the active site of the cap subdomain are highly distinct among the members of the HAD family
-
evolution
-
evolutionary adaptation of AbMtlD by fusion of dehydrogenase and phosphatase domains to facilitate efficient unidirectional enzymatic production of mannitol, unifying regulatory control and minimizing the intracellular concentration of toxic mannitol-1-phosphate during salt stress. Bifunctional M1P dehydrogenase (DH)/phosphatase (PD) is composed of an N-terminal PD domain belonging to the haloacid dehalogenase (HAD) superfamily and a C-terminal DH domain. The catalytic residues (D16, D18, T118, K151, E175, and D176) from the core domain are conserved in the HAD family. Residues at the active site of the cap subdomain are highly distinct among the members of the HAD family
-
evolution
Acinetobacter baumannii CCUG 19606
-
evolutionary adaptation of AbMtlD by fusion of dehydrogenase and phosphatase domains to facilitate efficient unidirectional enzymatic production of mannitol, unifying regulatory control and minimizing the intracellular concentration of toxic mannitol-1-phosphate during salt stress. Bifunctional M1P dehydrogenase (DH)/phosphatase (PD) is composed of an N-terminal PD domain belonging to the haloacid dehalogenase (HAD) superfamily and a C-terminal DH domain. The catalytic residues (D16, D18, T118, K151, E175, and D176) from the core domain are conserved in the HAD family. Residues at the active site of the cap subdomain are highly distinct among the members of the HAD family
-
evolution
-
evolutionary adaptation of AbMtlD by fusion of dehydrogenase and phosphatase domains to facilitate efficient unidirectional enzymatic production of mannitol, unifying regulatory control and minimizing the intracellular concentration of toxic mannitol-1-phosphate during salt stress. Bifunctional M1P dehydrogenase (DH)/phosphatase (PD) is composed of an N-terminal PD domain belonging to the haloacid dehalogenase (HAD) superfamily and a C-terminal DH domain. The catalytic residues (D16, D18, T118, K151, E175, and D176) from the core domain are conserved in the HAD family. Residues at the active site of the cap subdomain are highly distinct among the members of the HAD family
-
evolution
-
evolutionary adaptation of AbMtlD by fusion of dehydrogenase and phosphatase domains to facilitate efficient unidirectional enzymatic production of mannitol, unifying regulatory control and minimizing the intracellular concentration of toxic mannitol-1-phosphate during salt stress. Bifunctional M1P dehydrogenase (DH)/phosphatase (PD) is composed of an N-terminal PD domain belonging to the haloacid dehalogenase (HAD) superfamily and a C-terminal DH domain. The catalytic residues (D16, D18, T118, K151, E175, and D176) from the core domain are conserved in the HAD family. Residues at the active site of the cap subdomain are highly distinct among the members of the HAD family
-
evolution
-
evolutionary adaptation of AbMtlD by fusion of dehydrogenase and phosphatase domains to facilitate efficient unidirectional enzymatic production of mannitol, unifying regulatory control and minimizing the intracellular concentration of toxic mannitol-1-phosphate during salt stress. Bifunctional M1P dehydrogenase (DH)/phosphatase (PD) is composed of an N-terminal PD domain belonging to the haloacid dehalogenase (HAD) superfamily and a C-terminal DH domain. The catalytic residues (D16, D18, T118, K151, E175, and D176) from the core domain are conserved in the HAD family. Residues at the active site of the cap subdomain are highly distinct among the members of the HAD family
-
evolution
-
evolutionary adaptation of AbMtlD by fusion of dehydrogenase and phosphatase domains to facilitate efficient unidirectional enzymatic production of mannitol, unifying regulatory control and minimizing the intracellular concentration of toxic mannitol-1-phosphate during salt stress. Bifunctional M1P dehydrogenase (DH)/phosphatase (PD) is composed of an N-terminal PD domain belonging to the haloacid dehalogenase (HAD) superfamily and a C-terminal DH domain. The catalytic residues (D16, D18, T118, K151, E175, and D176) from the core domain are conserved in the HAD family. Residues at the active site of the cap subdomain are highly distinct among the members of the HAD family
-
evolution
-
evolutionary adaptation of AbMtlD by fusion of dehydrogenase and phosphatase domains to facilitate efficient unidirectional enzymatic production of mannitol, unifying regulatory control and minimizing the intracellular concentration of toxic mannitol-1-phosphate during salt stress. Bifunctional M1P dehydrogenase (DH)/phosphatase (PD) is composed of an N-terminal PD domain belonging to the haloacid dehalogenase (HAD) superfamily and a C-terminal DH domain. The catalytic residues (D16, D18, T118, K151, E175, and D176) from the core domain are conserved in the HAD family. Residues at the active site of the cap subdomain are highly distinct among the members of the HAD family
-
malfunction
-
deletion of gene mtlD results in a complete loss of salt-dependent mannitol biosynthesis
malfunction
A0A0U4Y4V3
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
-
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 synthesis of mannitol is catalyzed by mannitol-1-phosphate (M1P) dehydrogenase/phosphatase (MtlD), a bifunctional M1P dehydrogenase (DH)/phosphatase (PD) composed of an N-terminal PD domain belonging to the haloacid dehalogenase (HAD) superfamily and a C-terminal DH domain. This enzyme catalyzes the first step of the reduction of fructose-6-phosphate (F6P) to M1P with NADPH as a reductant (EC 1.1.1.17), followed by the dephosphorylation of M1P to mannitol (EC 3.1.3.22)
metabolism
-
the synthesis of mannitol is catalyzed by mannitol-1-phosphate (M1P) dehydrogenase/phosphatase (MtlD), a bifunctional M1P dehydrogenase (DH)/phosphatase (PD) composed of an N-terminal PD domain belonging to the haloacid dehalogenase (HAD) superfamily and a C-terminal DH domain. This enzyme catalyzes the first step of the reduction of fructose-6-phosphate (F6P) to M1P with NADPH as a reductant (EC 1.1.1.17), followed by the dephosphorylation of M1P to mannitol (EC 3.1.3.22)
-
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
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
-
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 synthesis of mannitol is catalyzed by mannitol-1-phosphate (M1P) dehydrogenase/phosphatase (MtlD), a bifunctional M1P dehydrogenase (DH)/phosphatase (PD) composed of an N-terminal PD domain belonging to the haloacid dehalogenase (HAD) superfamily and a C-terminal DH domain. This enzyme catalyzes the first step of the reduction of fructose-6-phosphate (F6P) to M1P with NADPH as a reductant (EC 1.1.1.17), followed by the dephosphorylation of M1P to mannitol (EC 3.1.3.22)
-
metabolism
-
the synthesis of mannitol is catalyzed by mannitol-1-phosphate (M1P) dehydrogenase/phosphatase (MtlD), a bifunctional M1P dehydrogenase (DH)/phosphatase (PD) composed of an N-terminal PD domain belonging to the haloacid dehalogenase (HAD) superfamily and a C-terminal DH domain. This enzyme catalyzes the first step of the reduction of fructose-6-phosphate (F6P) to M1P with NADPH as a reductant (EC 1.1.1.17), followed by the dephosphorylation of M1P to mannitol (EC 3.1.3.22)
-
metabolism
Acinetobacter baumannii CCUG 19606
-
the synthesis of mannitol is catalyzed by mannitol-1-phosphate (M1P) dehydrogenase/phosphatase (MtlD), a bifunctional M1P dehydrogenase (DH)/phosphatase (PD) composed of an N-terminal PD domain belonging to the haloacid dehalogenase (HAD) superfamily and a C-terminal DH domain. This enzyme catalyzes the first step of the reduction of fructose-6-phosphate (F6P) to M1P with NADPH as a reductant (EC 1.1.1.17), followed by the dephosphorylation of M1P to mannitol (EC 3.1.3.22)
-
metabolism
-
the synthesis of mannitol is catalyzed by mannitol-1-phosphate (M1P) dehydrogenase/phosphatase (MtlD), a bifunctional M1P dehydrogenase (DH)/phosphatase (PD) composed of an N-terminal PD domain belonging to the haloacid dehalogenase (HAD) superfamily and a C-terminal DH domain. This enzyme catalyzes the first step of the reduction of fructose-6-phosphate (F6P) to M1P with NADPH as a reductant (EC 1.1.1.17), followed by the dephosphorylation of M1P to mannitol (EC 3.1.3.22)
-
metabolism
-
the synthesis of mannitol is catalyzed by mannitol-1-phosphate (M1P) dehydrogenase/phosphatase (MtlD), a bifunctional M1P dehydrogenase (DH)/phosphatase (PD) composed of an N-terminal PD domain belonging to the haloacid dehalogenase (HAD) superfamily and a C-terminal DH domain. This enzyme catalyzes the first step of the reduction of fructose-6-phosphate (F6P) to M1P with NADPH as a reductant (EC 1.1.1.17), followed by the dephosphorylation of M1P to mannitol (EC 3.1.3.22)
-
metabolism
-
the synthesis of mannitol is catalyzed by mannitol-1-phosphate (M1P) dehydrogenase/phosphatase (MtlD), a bifunctional M1P dehydrogenase (DH)/phosphatase (PD) composed of an N-terminal PD domain belonging to the haloacid dehalogenase (HAD) superfamily and a C-terminal DH domain. This enzyme catalyzes the first step of the reduction of fructose-6-phosphate (F6P) to M1P with NADPH as a reductant (EC 1.1.1.17), followed by the dephosphorylation of M1P to mannitol (EC 3.1.3.22)
-
metabolism
-
the synthesis of mannitol is catalyzed by mannitol-1-phosphate (M1P) dehydrogenase/phosphatase (MtlD), a bifunctional M1P dehydrogenase (DH)/phosphatase (PD) composed of an N-terminal PD domain belonging to the haloacid dehalogenase (HAD) superfamily and a C-terminal DH domain. This enzyme catalyzes the first step of the reduction of fructose-6-phosphate (F6P) to M1P with NADPH as a reductant (EC 1.1.1.17), followed by the dephosphorylation of M1P to mannitol (EC 3.1.3.22)
-
metabolism
-
the synthesis of mannitol is catalyzed by mannitol-1-phosphate (M1P) dehydrogenase/phosphatase (MtlD), a bifunctional M1P dehydrogenase (DH)/phosphatase (PD) composed of an N-terminal PD domain belonging to the haloacid dehalogenase (HAD) superfamily and a C-terminal DH domain. This enzyme catalyzes the first step of the reduction of fructose-6-phosphate (F6P) to M1P with NADPH as a reductant (EC 1.1.1.17), followed by the dephosphorylation of M1P to mannitol (EC 3.1.3.22)
-
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
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
A0A0U4Y4V3
Corynebacterium glutamicum is a natural D-arabitol utilizer that requires arabitol-utilizing mannitol-1-phosphate 5-dehydrogenase MtlD for arabitol catabolism
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 bifunctional mannitol-1-phosphate dehydrogenase/phosphatase (AbMtlD) catalyzes the conversion of fructose-6-phosphate to mannitol in two consecutive steps unifying regulatory control and minimizing the intracellular concentration of toxic mannitol-1-phosphate during salt stress. Mannitol biosynthesis is essential for Acinetobacter baumannii to cope with osmotic stress. In de novo synthesis of mannitol, the molecular mechanism of reduction and dephosphorylation of fructose-6-phosphate to mannitol is highly dependent on the substrate shuffling from one protomer to the other protomer by a unique helix-loop-helix domain-mediated dimer formation, thus ensuring unidirectional and efficient biosynthesis of mannitol. Acinetobacter baumannii uses several means to mitigate the damage from desiccation by enhancing water retention through the accumulation of compatible solutes, capsule formation, and biofilm formation
physiological function
-
after deletion of the mtlD gene, cells no longer accumulate mannitol and growth is completely impaired at high salt concentrations
-
physiological function
-
the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase (AbMtlD) catalyzes the conversion of fructose-6-phosphate to mannitol in two consecutive steps unifying regulatory control and minimizing the intracellular concentration of toxic mannitol-1-phosphate during salt stress. Mannitol biosynthesis is essential for Acinetobacter baumannii to cope with osmotic stress. In de novo synthesis of mannitol, the molecular mechanism of reduction and dephosphorylation of fructose-6-phosphate to mannitol is highly dependent on the substrate shuffling from one protomer to the other protomer by a unique helix-loop-helix domain-mediated dimer formation, thus ensuring unidirectional and efficient biosynthesis of mannitol. Acinetobacter baumannii uses several means to mitigate the damage from desiccation by enhancing water retention through the accumulation of compatible solutes, capsule formation, and biofilm formation
-
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
-
the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase (AbMtlD) catalyzes the conversion of fructose-6-phosphate to mannitol in two consecutive steps unifying regulatory control and minimizing the intracellular concentration of toxic mannitol-1-phosphate during salt stress. Mannitol biosynthesis is essential for Acinetobacter baumannii to cope with osmotic stress. In de novo synthesis of mannitol, the molecular mechanism of reduction and dephosphorylation of fructose-6-phosphate to mannitol is highly dependent on the substrate shuffling from one protomer to the other protomer by a unique helix-loop-helix domain-mediated dimer formation, thus ensuring unidirectional and efficient biosynthesis of mannitol. Acinetobacter baumannii uses several means to mitigate the damage from desiccation by enhancing water retention through the accumulation of compatible solutes, capsule formation, and biofilm formation
-
physiological function
-
the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase (AbMtlD) catalyzes the conversion of fructose-6-phosphate to mannitol in two consecutive steps unifying regulatory control and minimizing the intracellular concentration of toxic mannitol-1-phosphate during salt stress. Mannitol biosynthesis is essential for Acinetobacter baumannii to cope with osmotic stress. In de novo synthesis of mannitol, the molecular mechanism of reduction and dephosphorylation of fructose-6-phosphate to mannitol is highly dependent on the substrate shuffling from one protomer to the other protomer by a unique helix-loop-helix domain-mediated dimer formation, thus ensuring unidirectional and efficient biosynthesis of mannitol. Acinetobacter baumannii uses several means to mitigate the damage from desiccation by enhancing water retention through the accumulation of compatible solutes, capsule formation, and biofilm formation
-
physiological function
Acinetobacter baumannii CCUG 19606
-
the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase (AbMtlD) catalyzes the conversion of fructose-6-phosphate to mannitol in two consecutive steps unifying regulatory control and minimizing the intracellular concentration of toxic mannitol-1-phosphate during salt stress. Mannitol biosynthesis is essential for Acinetobacter baumannii to cope with osmotic stress. In de novo synthesis of mannitol, the molecular mechanism of reduction and dephosphorylation of fructose-6-phosphate to mannitol is highly dependent on the substrate shuffling from one protomer to the other protomer by a unique helix-loop-helix domain-mediated dimer formation, thus ensuring unidirectional and efficient biosynthesis of mannitol. Acinetobacter baumannii uses several means to mitigate the damage from desiccation by enhancing water retention through the accumulation of compatible solutes, capsule formation, and biofilm formation
-
physiological function
-
the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase (AbMtlD) catalyzes the conversion of fructose-6-phosphate to mannitol in two consecutive steps unifying regulatory control and minimizing the intracellular concentration of toxic mannitol-1-phosphate during salt stress. Mannitol biosynthesis is essential for Acinetobacter baumannii to cope with osmotic stress. In de novo synthesis of mannitol, the molecular mechanism of reduction and dephosphorylation of fructose-6-phosphate to mannitol is highly dependent on the substrate shuffling from one protomer to the other protomer by a unique helix-loop-helix domain-mediated dimer formation, thus ensuring unidirectional and efficient biosynthesis of mannitol. Acinetobacter baumannii uses several means to mitigate the damage from desiccation by enhancing water retention through the accumulation of compatible solutes, capsule formation, and biofilm formation
-
physiological function
-
the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase (AbMtlD) catalyzes the conversion of fructose-6-phosphate to mannitol in two consecutive steps unifying regulatory control and minimizing the intracellular concentration of toxic mannitol-1-phosphate during salt stress. Mannitol biosynthesis is essential for Acinetobacter baumannii to cope with osmotic stress. In de novo synthesis of mannitol, the molecular mechanism of reduction and dephosphorylation of fructose-6-phosphate to mannitol is highly dependent on the substrate shuffling from one protomer to the other protomer by a unique helix-loop-helix domain-mediated dimer formation, thus ensuring unidirectional and efficient biosynthesis of mannitol. Acinetobacter baumannii uses several means to mitigate the damage from desiccation by enhancing water retention through the accumulation of compatible solutes, capsule formation, and biofilm formation
-
physiological function
-
the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase (AbMtlD) catalyzes the conversion of fructose-6-phosphate to mannitol in two consecutive steps unifying regulatory control and minimizing the intracellular concentration of toxic mannitol-1-phosphate during salt stress. Mannitol biosynthesis is essential for Acinetobacter baumannii to cope with osmotic stress. In de novo synthesis of mannitol, the molecular mechanism of reduction and dephosphorylation of fructose-6-phosphate to mannitol is highly dependent on the substrate shuffling from one protomer to the other protomer by a unique helix-loop-helix domain-mediated dimer formation, thus ensuring unidirectional and efficient biosynthesis of mannitol. Acinetobacter baumannii uses several means to mitigate the damage from desiccation by enhancing water retention through the accumulation of compatible solutes, capsule formation, and biofilm formation
-
physiological function
-
the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase (AbMtlD) catalyzes the conversion of fructose-6-phosphate to mannitol in two consecutive steps unifying regulatory control and minimizing the intracellular concentration of toxic mannitol-1-phosphate during salt stress. Mannitol biosynthesis is essential for Acinetobacter baumannii to cope with osmotic stress. In de novo synthesis of mannitol, the molecular mechanism of reduction and dephosphorylation of fructose-6-phosphate to mannitol is highly dependent on the substrate shuffling from one protomer to the other protomer by a unique helix-loop-helix domain-mediated dimer formation, thus ensuring unidirectional and efficient biosynthesis of mannitol. Acinetobacter baumannii uses several means to mitigate the damage from desiccation by enhancing water retention through the accumulation of compatible solutes, capsule formation, and biofilm formation
-
physiological function
-
the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase (AbMtlD) catalyzes the conversion of fructose-6-phosphate to mannitol in two consecutive steps unifying regulatory control and minimizing the intracellular concentration of toxic mannitol-1-phosphate during salt stress. Mannitol biosynthesis is essential for Acinetobacter baumannii to cope with osmotic stress. In de novo synthesis of mannitol, the molecular mechanism of reduction and dephosphorylation of fructose-6-phosphate to mannitol is highly dependent on the substrate shuffling from one protomer to the other protomer by a unique helix-loop-helix domain-mediated dimer formation, thus ensuring unidirectional and efficient biosynthesis of mannitol. Acinetobacter baumannii uses several means to mitigate the damage from desiccation by enhancing water retention through the accumulation of compatible solutes, capsule formation, and biofilm formation
-
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
additional information
the analysis of the crystal structure of AbMtlD reveals the catalytic role of the helix-loop-helix (HLH) domain of AbMtlD. Enzyme structure analysis, structure-function analysis, and structure comparisons, detailed overview
additional information
-
the analysis of the crystal structure of AbMtlD reveals the catalytic role of the helix-loop-helix (HLH) domain of AbMtlD. Enzyme structure analysis, structure-function analysis, and structure comparisons, detailed overview
-
additional information
-
the analysis of the crystal structure of AbMtlD reveals the catalytic role of the helix-loop-helix (HLH) domain of AbMtlD. Enzyme structure analysis, structure-function analysis, and structure comparisons, detailed overview
-
additional information
-
the analysis of the crystal structure of AbMtlD reveals the catalytic role of the helix-loop-helix (HLH) domain of AbMtlD. Enzyme structure analysis, structure-function analysis, and structure comparisons, detailed overview
-
additional information
Acinetobacter baumannii CCUG 19606
-
the analysis of the crystal structure of AbMtlD reveals the catalytic role of the helix-loop-helix (HLH) domain of AbMtlD. Enzyme structure analysis, structure-function analysis, and structure comparisons, detailed overview
-
additional information
-
the analysis of the crystal structure of AbMtlD reveals the catalytic role of the helix-loop-helix (HLH) domain of AbMtlD. Enzyme structure analysis, structure-function analysis, and structure comparisons, detailed overview
-
additional information
-
the analysis of the crystal structure of AbMtlD reveals the catalytic role of the helix-loop-helix (HLH) domain of AbMtlD. Enzyme structure analysis, structure-function analysis, and structure comparisons, detailed overview
-
additional information
-
the analysis of the crystal structure of AbMtlD reveals the catalytic role of the helix-loop-helix (HLH) domain of AbMtlD. Enzyme structure analysis, structure-function analysis, and structure comparisons, detailed overview
-
additional information
-
the analysis of the crystal structure of AbMtlD reveals the catalytic role of the helix-loop-helix (HLH) domain of AbMtlD. Enzyme structure analysis, structure-function analysis, and structure comparisons, detailed overview
-
additional information
-
the analysis of the crystal structure of AbMtlD reveals the catalytic role of the helix-loop-helix (HLH) domain of AbMtlD. Enzyme structure analysis, structure-function analysis, and structure comparisons, detailed overview
-
Show AA Sequence and Transmembrane Helices (5733 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
42000
additional information
AbMtlD exists predominantly in a monomeric state in the gel filtration buffer, and only a minor fraction appears as a dimer
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
?
x * 42000, recombinant His-tagged EsM1PDH1 isozyme, SDS-PAGE
dimer
the dimeric AbMtlD is constituted by two protomers, each with a dehydrogenase and phosphatase domain. AbMtlD dimers are composed of a putative product/substrate tunnel and substrate-binding site connecting the dehydrogenase (DH) and phosphatase (PD) catalytic domains. Each of the AbMtlD protomers constitutes a three-domain structure comprising a HAD superfamily-conserved PD domain at the N terminus, a DH domain at the C terminus, and a small HLH domain, together forming a door-lever-like structure
dimer
-
the dimeric AbMtlD is constituted by two protomers, each with a dehydrogenase and phosphatase domain. AbMtlD dimers are composed of a putative product/substrate tunnel and substrate-binding site connecting the dehydrogenase (DH) and phosphatase (PD) catalytic domains. Each of the AbMtlD protomers constitutes a three-domain structure comprising a HAD superfamily-conserved PD domain at the N terminus, a DH domain at the C terminus, and a small HLH domain, together forming a door-lever-like structure
-
dimer
-
the dimeric AbMtlD is constituted by two protomers, each with a dehydrogenase and phosphatase domain. AbMtlD dimers are composed of a putative product/substrate tunnel and substrate-binding site connecting the dehydrogenase (DH) and phosphatase (PD) catalytic domains. Each of the AbMtlD protomers constitutes a three-domain structure comprising a HAD superfamily-conserved PD domain at the N terminus, a DH domain at the C terminus, and a small HLH domain, together forming a door-lever-like structure
-
dimer
Acinetobacter baumannii CCUG 19606
-
the dimeric AbMtlD is constituted by two protomers, each with a dehydrogenase and phosphatase domain. AbMtlD dimers are composed of a putative product/substrate tunnel and substrate-binding site connecting the dehydrogenase (DH) and phosphatase (PD) catalytic domains. Each of the AbMtlD protomers constitutes a three-domain structure comprising a HAD superfamily-conserved PD domain at the N terminus, a DH domain at the C terminus, and a small HLH domain, together forming a door-lever-like structure
-
dimer
-
the dimeric AbMtlD is constituted by two protomers, each with a dehydrogenase and phosphatase domain. AbMtlD dimers are composed of a putative product/substrate tunnel and substrate-binding site connecting the dehydrogenase (DH) and phosphatase (PD) catalytic domains. Each of the AbMtlD protomers constitutes a three-domain structure comprising a HAD superfamily-conserved PD domain at the N terminus, a DH domain at the C terminus, and a small HLH domain, together forming a door-lever-like structure
-
dimer
-
the dimeric AbMtlD is constituted by two protomers, each with a dehydrogenase and phosphatase domain. AbMtlD dimers are composed of a putative product/substrate tunnel and substrate-binding site connecting the dehydrogenase (DH) and phosphatase (PD) catalytic domains. Each of the AbMtlD protomers constitutes a three-domain structure comprising a HAD superfamily-conserved PD domain at the N terminus, a DH domain at the C terminus, and a small HLH domain, together forming a door-lever-like structure
-
dimer
-
the dimeric AbMtlD is constituted by two protomers, each with a dehydrogenase and phosphatase domain. AbMtlD dimers are composed of a putative product/substrate tunnel and substrate-binding site connecting the dehydrogenase (DH) and phosphatase (PD) catalytic domains. Each of the AbMtlD protomers constitutes a three-domain structure comprising a HAD superfamily-conserved PD domain at the N terminus, a DH domain at the C terminus, and a small HLH domain, together forming a door-lever-like structure
-
dimer
-
the dimeric AbMtlD is constituted by two protomers, each with a dehydrogenase and phosphatase domain. AbMtlD dimers are composed of a putative product/substrate tunnel and substrate-binding site connecting the dehydrogenase (DH) and phosphatase (PD) catalytic domains. Each of the AbMtlD protomers constitutes a three-domain structure comprising a HAD superfamily-conserved PD domain at the N terminus, a DH domain at the C terminus, and a small HLH domain, together forming a door-lever-like structure
-
dimer
-
the dimeric AbMtlD is constituted by two protomers, each with a dehydrogenase and phosphatase domain. AbMtlD dimers are composed of a putative product/substrate tunnel and substrate-binding site connecting the dehydrogenase (DH) and phosphatase (PD) catalytic domains. Each of the AbMtlD protomers constitutes a three-domain structure comprising a HAD superfamily-conserved PD domain at the N terminus, a DH domain at the C terminus, and a small HLH domain, together forming a door-lever-like structure
-
dimer
-
the dimeric AbMtlD is constituted by two protomers, each with a dehydrogenase and phosphatase domain. AbMtlD dimers are composed of a putative product/substrate tunnel and substrate-binding site connecting the dehydrogenase (DH) and phosphatase (PD) catalytic domains. Each of the AbMtlD protomers constitutes a three-domain structure comprising a HAD superfamily-conserved PD domain at the N terminus, a DH domain at the C terminus, and a small HLH domain, together forming a door-lever-like structure
-
additional information
structure-based sequence comparisons, overview
additional information
structure-based sequence comparisons, overview
additional information
structure-based sequence comparisons, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, sitting drop vapor diffusion method, mixing of equal volumes of 5 mg/ml protein solution in presence of 5 mM mannitol with the precipitant solution containing 0.15-0.25 M NaI and 20% PEG 3350. Crystals are harvested and crushed with seed bead in mother liquor comprising 0.25 M NaI and 20% PEG3350 to prepare a 1:2000 ratio of seed dilution for seeding experiments. Well-diffracting crystals are obtained by the sitting drop vapor diffusion method at 18°C within 1-2 weeks in precipitant solution containing 0.1 M Bis-Tris propane, pH 6.5, 0.15-0.25 M Na2SO4, 0.2 M NaBr (can be substituted with 0.1 M potassium acetate or 0.1 M KI), 0.02 M MgCl2, and 14-18% PEG 3350 with a ratio of 3:2:1 or 2:3:1 of protein:precipitant:seed dilution, the method for crystallization of enzyme mutant D16A is slightly modified, X-ray diffraction structure determination and analysis. The structure of AbMtlD is initially determined by single-wavelength anomalous diffraction (SAD) using selenomethionine (Se-Met)-substituted protein to a resolution of 3.1 A. The resulting model is used as a search model by molecular replacement to solve the structure of unliganded AbMtlD at 2.6 A, substrate-bound AbMtlD, and an AbMtlD-D16A variant
structure at 1.7 A resolution and molecular docking of inhibition dihydrocelastrol
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A466C
site-directed mutagenesis, the mutant shows unaltered mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme
A466C/Y427C
site-directed mutagenesis, the mutant shows highly increased mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme
D16A
site-directed mutagenesis, the mutant shows the mutant shows increased mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme as well as increased activity with NADPH, but no mannitol-1-phosphate dephosphorylation activity
H434C/Y469C
site-directed mutagenesis, the mutant shows highly increased mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme
M417A
site-directed mutagenesis, the mutant shows reduced mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme
R609A
site-directed mutagenesis, the mutant shows highly reduced mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme, but increased activity with NADPH
R613A
site-directed mutagenesis, the mutant shows reduced mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme
W531A
site-directed mutagenesis, the mutant shows highly increased mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme
Y427C
site-directed mutagenesis, the mutant shows highly reduced mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme
Y469C
site-directed mutagenesis, the mutant shows highly reduced mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme
D16A
-
site-directed mutagenesis, the mutant shows the mutant shows increased mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme as well as increased activity with NADPH, but no mannitol-1-phosphate dephosphorylation activity
-
M417A
-
site-directed mutagenesis, the mutant shows reduced mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme
-
W531A
-
site-directed mutagenesis, the mutant shows highly increased mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme
-
D16A
-
site-directed mutagenesis, the mutant shows the mutant shows increased mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme as well as increased activity with NADPH, but no mannitol-1-phosphate dephosphorylation activity
-
M417A
-
site-directed mutagenesis, the mutant shows reduced mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme
-
W531A
-
site-directed mutagenesis, the mutant shows highly increased mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme
-
D16A
Acinetobacter baumannii CCUG 19606
-
site-directed mutagenesis, the mutant shows the mutant shows increased mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme as well as increased activity with NADPH, but no mannitol-1-phosphate dephosphorylation activity
-
M417A
Acinetobacter baumannii CCUG 19606
-
site-directed mutagenesis, the mutant shows reduced mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme
-
W531A
Acinetobacter baumannii CCUG 19606
-
site-directed mutagenesis, the mutant shows highly increased mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme
-
D16A
-
site-directed mutagenesis, the mutant shows the mutant shows increased mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme as well as increased activity with NADPH, but no mannitol-1-phosphate dephosphorylation activity
-
M417A
-
site-directed mutagenesis, the mutant shows reduced mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme
-
W531A
-
site-directed mutagenesis, the mutant shows highly increased mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme
-
D16A
-
site-directed mutagenesis, the mutant shows the mutant shows increased mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme as well as increased activity with NADPH, but no mannitol-1-phosphate dephosphorylation activity
-
M417A
-
site-directed mutagenesis, the mutant shows reduced mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme
-
W531A
-
site-directed mutagenesis, the mutant shows highly increased mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme
-
D16A
-
site-directed mutagenesis, the mutant shows the mutant shows increased mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme as well as increased activity with NADPH, but no mannitol-1-phosphate dephosphorylation activity
-
M417A
-
site-directed mutagenesis, the mutant shows reduced mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme
-
W531A
-
site-directed mutagenesis, the mutant shows highly increased mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme
-
D16A
-
site-directed mutagenesis, the mutant shows the mutant shows increased mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme as well as increased activity with NADPH, but no mannitol-1-phosphate dephosphorylation activity
-
M417A
-
site-directed mutagenesis, the mutant shows reduced mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme
-
W531A
-
site-directed mutagenesis, the mutant shows highly increased mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme
-
D16A
-
site-directed mutagenesis, the mutant shows the mutant shows increased mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme as well as increased activity with NADPH, but no mannitol-1-phosphate dephosphorylation activity
-
M417A
-
site-directed mutagenesis, the mutant shows reduced mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme
-
W531A
-
site-directed mutagenesis, the mutant shows highly increased mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme
-
D16A
-
site-directed mutagenesis, the mutant shows the mutant shows increased mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme as well as increased activity with NADPH, but no mannitol-1-phosphate dephosphorylation activity
-
M417A
-
site-directed mutagenesis, the mutant shows reduced mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme
-
W531A
-
site-directed mutagenesis, the mutant shows highly increased mannitol-1-phosphate dehydrogenase activity compared to wild-type enzyme
-
additional information
additional information
generation of inactive deletion mutant DELTAHLH
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
A0A0U4Y4V3
functional complementation of arabitol dehydrogenase activity of gene MtlD in Corynebacterium glutamicum DELTAmtlD deletion mutant by gene atlD of Bacillus methanolicus strain MG3
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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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 wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by metal affinity chromatography and gel filtration
recombinant His6-tagged enzyme 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 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 His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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
-
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
differential gene expression analysis of Bacillus methanolicus strain MGA3 cells grown on arabitol as compared to mannitol via transcriptome sequencing (RNA-seq), quantitative RT-PCR expression analysis, the enzyme can be induced by arabitol
expression of MtlD is strongly dependent on high osmolarity, not discriminating between different salts or sugars
in Bacillus methanolicus, RNA levels for atlD are higher while lower for mtlD during growth with both carbon sources as compared to growth with mannitol alone
in Corynebacterium glutamicum, arabitol induces expression of genes rbtT, mtlD, sixA, xylB and atlR, and glucose represses expression of mtlD
A0A0U4Y4V3
induction of the enzyme in cell culture by isopropyl 1-thio-beta-D-galactopyranoside
the presence of glycine betaine or choline repress promoter activation
differential gene expression analysis of Bacillus methanolicus strain MGA3 cells grown on arabitol as compared to mannitol via transcriptome sequencing (RNA-seq), quantitative RT-PCR expression analysis, the enzyme can be induced by arabitol
differential gene expression analysis of Bacillus methanolicus strain MGA3 cells grown on arabitol as compared to mannitol via transcriptome sequencing (RNA-seq), quantitative RT-PCR expression analysis, the enzyme can be induced by arabitol
-
-
differential gene expression analysis of Bacillus methanolicus strain MGA3 cells grown on arabitol as compared to mannitol via transcriptome sequencing (RNA-seq), quantitative RT-PCR expression analysis, the enzyme can be induced by arabitol
-
-
expression of MtlD is strongly dependent on high osmolarity, not discriminating between different salts or sugars
expression of MtlD is strongly dependent on high osmolarity, not discriminating between different salts or sugars
-
-
in Bacillus methanolicus, RNA levels for atlD are higher while lower for mtlD during growth with both carbon sources as compared to growth with mannitol alone
in Bacillus methanolicus, RNA levels for atlD are higher while lower for mtlD during growth with both carbon sources as compared to growth with mannitol alone
-
-
in Bacillus methanolicus, RNA levels for atlD are higher while lower for mtlD during growth with both carbon sources as compared to growth with mannitol alone
-
-
the presence of glycine betaine or choline repress promoter activation
the presence of glycine betaine or choline repress promoter activation
-
-
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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
analysis
pharmacology
-
inhibition of AfM1PDH might be a useful target for therapy of Aspergillus fumigatus infections
synthesis
analysis
application of CRISPRi-dCas9 technique for gene repression
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schmatz D.M.; Baginsky W.F.; Turner, M.J.
Evidence for and characterization of a mannitol cycle in Eimeria tenella
Mol. Biochem. Parasitol.
32
263-270
1989
Eimeria tenella (O96437), Eimeria tenella
brenda
Liss, M.; Horwitz, S.B.; Kaplan, N.O.
D-Mannitol 1-phosphate dehydrogenase and D-sorbitol 6-phosphate dehydrogenase in Aerobacter aerogenes
J. Biol. Chem.
237
1342-1350
1962
Klebsiella aerogenes
brenda
Novotny, M.J.; Reizer, J.; Esch, F.; Saier, M.H.
Purification and properties of D-mannitol-1-phosphate dehydrogenase and D-glucitol-6-phosphate dehydrogenase from Escherichia coli
J. Bacteriol.
159
986-990
1984
Escherichia coli
brenda
Mehta, R.J.; Fare, L.R.; Shearer, M.E.; Nash, C.H.
Mannitol oxidation in two Micromonospora isolates and in representative species of other actinomycetes
Appl. Environ. Microbiol.
33
1013-1015
1977
Amycolatopsis lactamdurans, Micromonospora sp., no activity in Actinoplanes missouriensis, no activity in Mycobacterium smegmatis, no activity in Nocardia erythropolis
brenda
Otte, S.; Lengeler, J.W.
The mtl genes and the mannitol-1-phosphate dehydrogenase from Klebsiella pneumoniae KAY2026
FEMS Microbiol. Lett.
194
221-227
2001
Klebsiella pneumoniae
brenda
Survarna, K.; Bartiss, A.; Wong, B.
Mannitol-1-phosphate dehydrogenase from Cryptococcus neoformans is a zinc-containing long-chain alcohol/polyol dehydrogenase
Microbiology
146
2705-2713
2000
Cryptococcus neoformans
brenda
Henstra, S.A.; Tolner, B.; Ten Hoeve Duurkens, R.H.; Konings, W.N.; Robillard, G.T.
Cloning, expression, and isolation of the mannitol transport protein from the thermophilic bacterium Bacillus stearothermophilus
J. Bacteriol.
178
5586-5591
1996
Geobacillus stearothermophilus
brenda
Singh, S.P.; Rogers, P.J.
Isolation and characterization of mannitol-1-phosphate dehydrogenase from Brochothrix thermosphacta
J. Gen. Appl. Microbiol.
39
327-337
1993
Brochothrix thermosphacta
-
brenda
Honeyman, A.L.; Curtiss III, R.
Isolation, characterization, and nucleotide sequence of the Streptococcus mutans mannitol-phosphate dehydrogenase gene and the mannitol-specific factor III gene of the phosphoenolpyruvate phosphotransferase system
Infect. Immun.
60
3369-3375
1992
Streptococcus mutans
brenda
Fischer, R.; von Strandmann, R.P.; Hengstenberg, W.
Mannitol-specific phosphoenolpyruvate-dependent phosphotransferase system of Enterococcus faecalis: Molecular cloning and nucleotide sequences of the enzyme III Mtl gene and the mannitol-1-phosphate dehydrogenase gene, expression in Escherichia coli, and comparison of the gene products with similar enzymes
J. Bacteriol.
173
3709-3715
1991
Enterococcus faecalis, Staphylococcus carnosus
brenda
Chase, T.
Mannitol-1-phosphate dehydrogenase of Escherichia coli
Biochem. J.
239
435-443
1986
Escherichia coli
brenda
Foreman, J.E.; Niehaus, W.G.
Zn2+-induced cooperativity of mannitol-1-phosphate dehydrogenase from Aspergillus parasiticus
J. Biol. Chem.
260
10019-10022
1985
Aspergillus parasiticus, Aspergillus niger
brenda
Kiser, R.C.; Niehaus, W.G.
Purification and kinetic characterization of mannitol-1-phosphate dehydrogenase from Aspergillus niger
Arch. Biochem. Biophys.
211
613-621
1981
Aspergillus niger
brenda
Brown, A.T.; Bowles, R.D.
Polyol metabolism by a caries-conductive Streptococcus: Purification and properties of a nicotinamide adenine dinucleotide-dependent mannitol-1-phosphate dehydrogenase
Infect. Immun.
16
163-173
1977
Streptococcus mutans
brenda
Hankinson, O.; Cove, D.J.
Regulation of mannitol-1-phosphate dehydrogenase in Aspergillus nidulans
Can. J. Microbiol.
21
99-101
1975
Aspergillus nidulans
brenda
Wolff, J.B.; Kaplan, N.O.
D-Mannitol-1-phosphate dehydrogenase from E. coli
Methods Enzymol.
1
346-348
1955
Escherichia coli
-
brenda
Wisselink, H.W.; Mars, A.E.; van der Meer, P.; Eggink, G.; Hugenholtz, J.
Metabolic engineering of mannitol production in Lactococcus lactis: influence of overexpression of mannitol 1-phosphate dehydrogenase in different genetic backgrounds
Appl. Environ. Microbiol.
70
4286-4292
2004
Pseudolactococcus plantarum
brenda
Watanabe, S.; Hamano, M.; Kakeshita, H.; Bunai, K.; Tojo, S.; Yamaguchi, H.; Fujita, Y.; Wong, S.L.; Yamane, K.
Mannitol-1-phosphate dehydrogenase (MtlD) is required for mannitol and glucitol assimilation in Bacillus subtilis: possible cooperation of mtl and gut operons
J. Bacteriol.
185
4816-4824
2003
Bacillus subtilis
brenda
Iwamoto, K.; Kawanobe, H.; Ikawa, T.; Shiraiwa, Y.
Characterization of salt-regulated mannitol-1-phosphate dehydrogenase in the red alga Caloglossa continua
Plant Physiol.
133
893-900
2003
Caloglossa continua
brenda
Chiang, Y.; Stushnoff, C.; McSay, A.E.; Jones, M.L.; Bohnert, H.J.
Overexpression of mannitol-1-phosphate dehydrogenase increases mannitol accumulation and adds protection against chilling injury in Petunia
J. Am. Soc. Hort. Sci.
130
605-610
2005
Escherichia coli
-
brenda
Solomon, P.S.; Tan, K.C.; Oliver, R.P.
Mannitol 1-phosphate metabolism is required for sporulation in planta of the wheat pathogen Stagonospora nodorum
Mol. Plant Microbe Interact.
18
110-115
2005
Parastagonospora nodorum (Q0U6E8), Parastagonospora nodorum
brenda
Tang, W.; Peng, X.; Newton, R.J.
Enhanced tolerance to salt stress in transgenic loblolly pine simultaneously expressing two genes encoding mannitol-1-phosphate dehydrogenase and glucitol-6-phosphate dehydrogenase
Plant Physiol. Biochem.
43
139-146
2005
Agrobacterium tumefaciens
brenda
Ladero, V.; Ramos, A.; Wiersma, A.; Goffin, P.; Schanck, A.; Kleerebezem, M.; Hugenholtz, J.; Smid, E.J.; Hols, P.
High-level production of the low-calorie sugar sorbitol by Lactobacillus plantarum through metabolic engineering
Appl. Environ. Microbiol.
73
1864-1872
2007
Lactiplantibacillus plantarum
brenda
Krahulec, S.; Armao, G.C.; Weber, H.; Klimacek, M.; Nidetzky, B.
Characterization of recombinant Aspergillus fumigatus mannitol-1-phosphate 5-dehydrogenase and its application for the stereoselective synthesis of protio and deuterio forms of D-mannitol 1-phosphate
Carbohydr. Res.
343
1414-1423
2008
Aspergillus fumigatus (Q4X1A4), Aspergillus fumigatus
brenda
Velez, H.; Glassbrook, N.J.; Daub, M.E.
Mannitol biosynthesis is required for plant pathogenicity by Alternaria alternata
FEMS Microbiol. Lett.
285
122-129
2008
Alternaria alternata, Alternaria alternata A5
brenda
Pujni, D.; Chaudhary, A.; Rajam, M.V.
Increased tolerance to salinity and drought in transgenic indica rice by mannitol accumulation
J. Plant Biochem. Biotechnol.
16
1-7
2007
Escherichia coli
-
brenda
Krahulec, S.; Armao, G.C.; Bubner, P.; Klimacek, M.; Nidetzky, B.
Polyol-specific long-chain dehydrogenases/reductases of mannitol metabolism in Aspergillus fumigatus: biochemical characterization and pH studies of mannitol 2-dehydrogenase and mannitol-1-phosphate 5-dehydrogenase
Chem. Biol. Interact.
178
274-282
2009
Aspergillus fumigatus
brenda
Wang, Z.L.; Ying, S.H.; Feng, M.G.
Gene cloning and catalysis features of a new mannitol-1-phosphate dehydrogenase (BbMPD) from Beauveria bassiana
Carbohydr. Res.
345
50-54
2010
Beauveria bassiana (C7FDI4), Beauveria bassiana
brenda
Aguilar-Osorio, G.; Vankuyk, P.A.; Seiboth, B.; Blom, D.; Solomon, P.S.; Vinck, A.; Kindt, F.; Woesten, H.A.; de Vries, R.P.
Spatial and developmental differentiation of mannitol dehydrogenase and mannitol-1-phosphate dehydrogenase in Aspergillus niger
Eukaryot. Cell
9
1398-1402
2010
Aspergillus niger
brenda
Sand, M.; Mingote, A.I.; Santos, H.; Mueller, V.; Averhoff, B.
Mannitol, a compatible solute synthesized by Acinetobacter baylyi in a two-step pathway including a salt-induced and salt-dependent mannitol-1-phosphate dehydrogenase
Environ. Microbiol.
15
2187-2197
2013
Acinetobacter baylyi
brenda
Krahulec, S.; Armao, G.C.; Klimacek, M.; Nidetzky, B.
Enzymes of mannitol metabolism in the human pathogenic fungus Aspergillus fumigatus--kinetic properties of mannitol-1-phosphate 5-dehydrogenase and mannitol 2-dehydrogenase, and their physiological implications
FEBS J.
278
1264-1276
2011
Aspergillus fumigatus
brenda
Rambhatla, P.; Kumar, S.; Floyd, J.T.; Varela, M.F.
Molecular cloning and characterization of mannitol-1-phosphate dehydrogenase from Vibrio cholerae
J. Microbiol. Biotechnol.
21
914-920
2011
Vibrio cholerae serotype O1
brenda
Rousvoal, S.; Groisillier, A.; Dittami, S.; Michel, G.; Boyen, C.; Tonon, T.
Mannitol-1-phosphate dehydrogenase activity in Ectocarpus siliculosus, a key role for mannitol synthesis in brown algae
Planta
233
261-273
2011
Ectocarpus siliculosus (D8LI09), Ectocarpus siliculosus (D7FMJ8), Ectocarpus siliculosus (D7G793), Ectocarpus siliculosus, Ectocarpus siliculosus Ec32 / CCAP 1310/4 (D8LI09), Ectocarpus siliculosus Ec32 / CCAP 1310/4 (D7FMJ8), Ectocarpus siliculosus Ec32 / CCAP 1310/4 (D7G793)
brenda
Sand, M.; Rodrigues, M.; Gonzalez, J.M.; de Crecy-Lagard, V.; Santos, H.; Mueller, V.; Averhoff, B.
Mannitol-1-phosphate dehydrogenases/phosphatases: a family of novel bifunctional enzymes for bacterial adaptation to osmotic stress
Environ. Microbiol.
17
711-719
2015
Acinetobacter baylyi (Q6FBP5), Acinetobacter baylyi ATCC 33305 (Q6FBP5)
brenda
Bonin, P.; Groisillier, A.; Raimbault, A.; Guibert, A.; Boyen, C.; Tonon, T.
Molecular and biochemical characterization of mannitol-1-phosphate dehydrogenase from the model brown alga Ectocarpus sp.
Phytochemistry
117
509-520
2015
Ectocarpus siliculosus (D8LI09), Ectocarpus siliculosus (D7FMJ8), Ectocarpus siliculosus (D7G793)
brenda
Bhauso, T.D.; Radhakrishnan, T.; Kumar, A.; Mishra, G.P.; Dobaria, J.R.; Patel, K.; Rajam, M.V.
Overexpression of bacterial mtlD gene in peanut improves drought tolerance through accumulation of mannitol
ScientificWorldJournal
2014
125967
2014
Escherichia coli (P09424)
brenda
Goudarzi, A.; Jafari, M.; Safaie, N.; Mohammad Jafari, S.
Transgenic sugar beet expressing a bacterial mannitol-1-phosphate dehydrogenase (mtlD) gene shows enhanced resistance to fungal pathogens
Sugar Tech.
18
192-203
2016
Escherichia coli (P09424)
-
brenda
Zeidler, S.; Hubloher, J.; Koenig, P.; Ngu, N.; Scholz, A.; Averhoff, B.; Mueller, V.
Salt induction and activation of MtlD, the key enzyme in the synthesis of the compatible solute mannitol in Acinetobacter baumannii
MicrobiologyOpen
7
e00614
2018
Acinetobacter baumannii (D0C7J2), Acinetobacter baumannii ATCC 19606 (D0C7J2)
brenda
Schultenkaemper, K.; Brito, L.F.; Lopez, M.G.; Brautaset, T.; Wendisch, V.F.
Establishment and application of CRISPR interference to affect sporulation, hydrogen peroxide detoxification, and mannitol catabolism in the methylotrophic thermophile Bacillus methanolicus
Appl. Microbiol. Biotechnol.
103
5879-5889
2019
Bacillus methanolicus (I3E3X0), Bacillus methanolicus, Bacillus methanolicus MGA3 (I3E3X0)
brenda
Lim, J.Y.; Jang, S.H.; Park, H.M.
Mannitol-1-phosphate dehydrogenase, MpdA, is required for mannitol production in vegetative cells and involved in hyphal branching, heat resistance of conidia and sexual development in Aspergillus nidulans
Curr. Genet.
67
613-630
2021
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
Bacillus methanolicus (I3E3X0), Bacillus methanolicus ATCC 53907 (I3E3X0), Bacillus methanolicus MGA3 (I3E3X0), Corynebacterium glutamicum (A0A0U4Y4V3)
brenda
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
Tam, H.; Konig, P.; Himpich, S.; Ngu, N.; Abele, R.; Muller, V.; Pos, K.
Unidirectional mannitol synthesis of Acinetobacter baumannii MtlD is facilitated by the helix-loop-helix-mediated dimer formation
Proc. Natl. Acad. Sci. USA
119
e2107994119
2022
Acinetobacter baumannii (D0C7J2), Acinetobacter baumannii 81 (D0C7J2), Acinetobacter baumannii ATCC 19606 (D0C7J2), Acinetobacter baumannii CCUG 19606 (D0C7J2), Acinetobacter baumannii CIP 70.34 (D0C7J2), Acinetobacter baumannii DSM 30007 (D0C7J2), Acinetobacter baumannii JCM 6841 (D0C7J2), Acinetobacter baumannii NBRC 109757 (D0C7J2), Acinetobacter baumannii NCIMB 12457 (D0C7J2), Acinetobacter baumannii NCTC 12156 (D0C7J2)
brenda
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