Information on EC 1.1.1.17 - mannitol-1-phosphate 5-dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.1.1.17
-
RECOMMENDED NAME
GeneOntology No.
mannitol-1-phosphate 5-dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-mannitol 1-phosphate + NAD+ = D-fructose 6-phosphate + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
intramolecular phosphate transfer
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
mannitol cycle
-
-
mannitol degradation I
-
-
degradation of sugar alcohols
-
-
Fructose and mannose metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
D-mannitol-1-phosphate:NAD+ 5-oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9028-24-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene mtlD or ACIAD1672
-
-
Manually annotated by BRENDA team
strain A5
-
-
Manually annotated by BRENDA team
strain A5
-
-
Manually annotated by BRENDA team
hyperexpression of enzyme upon growth on mannitol as sole carbon source
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
formerly Microbacterium thermosphactum
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
strains BC-1751, BC-2079
-
-
Manually annotated by BRENDA team
no activity in Actinoplanes missouriensis
-
-
-
Manually annotated by BRENDA team
no activity in Mycobacterium smegmatis
-
-
-
Manually annotated by BRENDA team
no activity in Nocardia erythropolis
-
-
-
Manually annotated by BRENDA team
Mdp1 is disrupted by insertion mutagenesis, and the resulting mpd1 strain lacks all detectable NAD+-linked mannitol 1-phosphate dehydrogenase activity
Uniprot
Manually annotated by BRENDA team
gene mtlD
-
-
Manually annotated by BRENDA team
gene mtlD
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
-
deletion of gene mtlD results in a complete loss of salt-dependent mannitol biosynthesis
metabolism
physiological function
additional information
-
ATP, ADP and AMP do not affect the activity of AfM1PDH, suggesting the absence of flux control by cellular energy charge at the level of D-fructose 6-phosphate reduction
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
show the reaction diagram
D-fructose 6-phosphate + NADPH + H+
D-mannitol 1-phosphate + NADP+
show the reaction diagram
D-fructose-6-phosphate + NADH
D-mannitol-1-phosphate + NAD+
show the reaction diagram
-
-
-
-
r
D-mannitol 1-phosphate + 3-acetylpyridine-NAD+
D-fructose 6-phosphate + ?
show the reaction diagram
-
7% of the activity compared to NAD+
-
?
D-mannitol 1-phosphate + acetylpyridine adenine dinucleotide
D-fructose 6-phosphate + ?
show the reaction diagram
-
50% of the activity compared to NAD+
-
?
D-mannitol 1-phosphate + dichlorophenolindophenol
D-fructose 6-phosphate + reduced dichlorophenolindophenol
show the reaction diagram
-
higher activity than for NAD+
-
?
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
show the reaction diagram
D-mannitol 1-phosphate + nicotinamide 6-(2-hydoxyethylamino) purine dinucleotide
D-fructose 6-phosphate + ?
show the reaction diagram
-
75% of the activity compared to NAD+
-
?
D-mannitol 1-phosphate + nicotinamide hypoxanthine dinucleotide
D-fructose 6-phosphate + ?
show the reaction diagram
-
84% of the activity compared to NAD+
-
?
D-mannitol-1-phosphate + NAD+
D-fructose-6-phosphate + NADH
show the reaction diagram
-
-
-
-
r
D-sorbitol 6-phosphate + NAD+
D-glucose 6-phosphate + NADH + H+
show the reaction diagram
-
38.8% of the activity compared to D-mannitol 1-phosphate
-
r
ethanol + NAD+
acetaldehyde + NADH
show the reaction diagram
-
56% of the activity compared to D-mannitol 1-phosphate
-
r
hexitol phosphate + NAD+
? + NADH
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-fructose 6-phosphate + NADH + H+
D-mannitol 1-phosphate + NAD+
show the reaction diagram
-
-
-
-
r
D-fructose 6-phosphate + NADPH + H+
D-mannitol 1-phosphate + NADP+
show the reaction diagram
-
-
-
-
r
D-mannitol 1-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
show the reaction diagram
D-sorbitol 6-phosphate + NAD+
D-glucose 6-phosphate + NADH + H+
show the reaction diagram
-
38.8% of the activity compared to D-mannitol 1-phosphate
-
r
ethanol + NAD+
acetaldehyde + NADH
show the reaction diagram
-
56% of the activity compared to D-mannitol 1-phosphate
-
r
hexitol phosphate + NAD+
? + NADH
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
2fold activation at 5 mM, no activation of ethanol oxidation
Zn2+
-
1.14 Zn atoms/monomer
additional information
-
5 and 10 mM concentrations of MgSO4, MnSO4, FeCl3, ZnCl2, CoCl2, and LiCl have no effect on the nezyme activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
weak inhibition
2,2'-bipyridyl
-
weak inhibition
4,7-phenanthroline
-
weak inhibition
4-hydroxymercuribenzoate
strong inhibition; strong inhibition; strong inhibition
5,5'-dithiobis-(2-nitrobenzoate)
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complete inactivation at 0.24 mM
adenosine
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48% inhibition of fructose 6-phosphate reduction
adenosine diphosphoribose
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competitive inhibition with respect to NADH, noncompetitive inhibition with respect to D-fructose 6-phosphate
Ca2+
35.9% inhibition at 10 mM of the reverse reaction
cytidine
-
17% inhibition of fructose 6-phosphate reduction
D-fructose 1,6-diphosphate
-
12% inhibition of mannitol 1-phosphate oxidation
D-fructose 6-phosphate
D-glucose 6-phosphate
-
competitive inhibition with respect to D-fructose 6-phosphate, noncompetitive inhibition with respect to NADH
D-mannitol 1-phosphate
-
competitive inhibition with respect to D-fructose 6-phosphate, noncompetitive inhibition with respect to NADH
diethyldicarbonate
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60% inhibition at 1 mM
diethyldithiocarbamate
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95% inactivation, prevented by presence of 2-mercaptoethanol
DTT
46.0% inhibition at 10 mM of the reverse reaction
fructose-6-phosphate
-
substrate inhibition above 0.5 mM
GTP
-
11% inhibition of mannitol 1-phosphate oxidation
guanosine
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10% inhibition of fructose 6-phosphate reduction
Li+
24.4% inhibition at 50 mM of the reverse reaction
Mg2+
31.2% inhibition at 10 mM of the reverse reaction
Mn2+
31.3% inhibition at 50 mM of the reverse reaction
N-ethylmaleimide
-
1 mM, 80% inhibition of reduction and oxidation reaction
NAD+
-
competitive inhibition with respect to NADH, noncompetitive inhibition with respect to D-fructose 6-phosphate
p-hydroxymercuribenzoate
-
0.5 mM, complete inhibition of reduction and oxidation reaction, 2-mercaptoethanol protects
phosphoenolpyruvate
-
14% inhibition of mannitol 1-phosphate oxidation
SDS
80.1% inhibition at 1 mM of the reverse reaction
thymidine
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8% inhibition of fructose 6-phosphate reduction
uridine
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16% inhibition of fructose 6-phosphate reduction
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2 - 13.6
D-fructose 6-phosphate
188.8 - 1458
D-fructose-6-phosphate
0.038 - 2
D-mannitol 1-phosphate
48.9 - 138
D-mannitol-1-phosphate
0.94
ethanol
-
cosubstrate: NAD+
0.8
hexitol phosphate
-
cosubstrate: NAD+
0.05 - 32
NAD+
0.005 - 56.9
NADH
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
125 - 132
D-fructose 6-phosphate
0.0019 - 10.6
D-mannitol 1-phosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
41 - 1310
D-fructose 6-phosphate
87
80
D-mannitol 1-phosphate
Aspergillus fumigatus
-
pH 7.1, 25C, recombinant enzyme
2652
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8
1,10-phenanthroline
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-
11
2,2'-bipyridyl
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-
12
4,7-phenanthroline
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-
0.7 - 2
ADP
1.6 - 2.2
ATP
3.33
D-fructose 6-phosphate
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able to inhibit the forward reaction to 100%, competitive inhibition with respect to mannitol 1-phosphate, noncompetitive inhibition with respect to NAD+
0.002
NADH
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pH 10.0, 25C, recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.002
algal extract, pH 6.3, 30C, in presence of NaCl; algal extract, pH 6.3, 30C, in presence of NaCl; algal extract, pH 6.3, 30C, in presence of NaCl
0.01
41C, pH 7.5
0.03
-
crude extract, D-mannitol 1-phosphate oxidation
0.03 - 0.05
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crude extract, D-mannitol 1-phosphate oxidation
0.09
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crude extract, D-mannitol 1-phosphate oxidation
0.1
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crude extract, D-mannitol 1-phosphate oxidation
0.13
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crude extract, dehydrogenase activity
0.28
-
crude extract, reductase activity
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, 30C, fructose 6-phosphate reduction
17.6
oxidation reaction, purified recombinant enzyme
18
-
purified enzyme, D-fructose 6-phosphate reduction
18.6
-
mature conidiospores, pH not specified in the publication, temperature not specified in the publication
68.3
-
non-sporulating mycelium, pH not specified in the publication, temperature not specified in the publication
116
-
purified enzyme D-mannitol 1-phosphate oxidation
130
-
D-fructose 6-phosphate reduction with NADPH, pH 7.0, 30C
169
reduction reaction, purified recombinant enzyme
228.6
-
reduction, pH 7.0, 25C, presence of 100 mM NaCl
453.9
-
sporulating mycelium, pH not specified in the publication, temperature not specified in the publication
673.7
pH 7.0, 37C, purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7
-
oxidation of D-mannitol 1-phosphate
6
-
reduction, optimum may be below pH 6.0
6.3
reduction reaction; reduction reaction; reduction reaction
6.5
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reduction of D-fructose 6-phosphate
7 - 7.5
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NADH-dependent reduction of D-fructose 6-phosphate
7.2
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reduction, in presence of 200 mM NaCl
8.5 - 9
-
oxidation of D-mannitol 1-phosphate
9
-
oxidation, assay at
9 - 9.5
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NAD+-dependent oxidation of D-mannitol 1-phosphate
9.5 - 10
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reduction of D-fructose 6-phosphate
10
-
assay at, oxidation reaction
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 10
activity range, profile, overview
5.5 - 10
-
more than 95% of its original activity
6 - 9
-
65% and 50% of maximal activity, respectively
6 - 10
-
for the oxidative and reductive direction of the reactions under conditions where substrate is limiting (kcat/K) or saturating (kcat)
6 - 9
-
no sharp optimum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 40
-
70% of maximal activity at 15C or 35C, and 50% at 10C or 40C
15 - 45
activity range, profile, overview
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
-
gel filtration
45500
-
gel filtration
50000
-
gel filtration
53000
-
gel filtration
148000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
stable for one week
40 - 50
-
half-life is 20 h at 40C, the enzyme displays remarkable stability at 40C and even at 50C
40
-
stable during 20 min
55
-
45% loss of activity in 10 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
loss of activity partially protected by addition of substrates
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, 0.05 M Tris-HCl, pH 7.5, presence of 2-mercaptoethanol, long term storage without loss of activity
-
4C, 0.03 M imidazole-HCl, pH 7.3, several months
-
4C, 0.05 M Tris-HCl, pH 7.6, 0.05 M NaCl, 5 mM 2-mercaptoethanol, stable for weeks
-
4C, purified native enzyme, the enzyme retains high activity during storage for two weeks
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
precipitation techniques
-
recombinant enzyme
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recombinant enzyme 2.1fold from Escherichia coli by affinity chromatography
recombinant His-tagged MtlD by nickel affinity chromatography
-
recombinant His6-tagged nezyme from Escherichia coli strain SG13009 by nickel affinity chromatography
-
to homogeneity, chromatography steps, affinity chromatography
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to homogeneity, chromatography techniques
wild-type and mutant
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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
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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 mtlD or ACIAD1672, DNA and amino acid sequence determination and analysis, real-time-PCR expression analysis, expression of His-tagged enzyme
-
gene mtld1, encoded in the mannitol operon, sequence comparison, real-time PCR expression analysis, expression as His6-tagged protein in Escherichia coli strain SG13009
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heterologous expression in Escherichia coli JM109
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high level overexpression in Escherichia coli strain JM109
overexpression in Escherichia coli
-
overexpression of enzyme in Lactococcus lactis, small amounts of mannitol are formed in growing cells of lactate dehydrogenase deficient or phosphofructokinase-reduced strains, while resting cells of lactate-dehydrogenase deficient strain convert 25% of glucose into mannitol
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Petunia hybrida (Hook) Vilm. cv. Mitchell is transformed with an Escherichia coli gene encoding mannitol 1-phosphate dehydrogenase. The high-mannitol containing lines are more tolerant of chilling stress than the low mannitol containing transgenic lines and wild-type. In the higher mannitol lines only 0.04% to 0.06% of the total osmotic potential generated from all solutes can be attributed to mannitol, thus its action is more like that of an osmoprotectant rather than an osmoregulator
-
recombinant expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
induction of the enzyme in cell culture by isopropyl 1-thio-beta-D-galactopyranoside
M1PDH becomes strongly upregulated during heat shock
-
the enzyme is salt-dependent and salt-induced, overview
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K213A
-
residual activity
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
-
Petunia hybrida (Hook) Vilm. cv. Mitchell is transformed with an Escherichia coli gene encoding mannitol 1-phosphate dehydrogenase. The high-mannitol containing lines are more tolerant of chilling stress than the low mannitol containing transgenic lines and wild-type. In the higher mannitol lines only 0.04% to 0.06% of the total osmotic potential generated from all solutes can be attributed to mannitol, thus its action is more like that of an osmoprotectant rather than an osmoregulator. Metabolic engineering of osmoprotectant synthesis pathways can be used to improve stress tolerance in horticultural crops
pharmacology
-
inhibition of AfM1PDH might be a useful target for therapy of Aspergillus fumigatus infections
synthesis
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