Information on EC 1.1.1.255 - mannitol dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.255
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RECOMMENDED NAME
GeneOntology No.
mannitol dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-mannitol + NAD+ = D-mannose + NADH + H+
show the reaction diagram
The enzyme from Apium graveolens (celery) oxidizes alditols with a minimum requirement of 2R chirality at the carbon adjacent to the primary carbon undergoing the oxidation. The enzyme is specific for NAD+ and does not use NADP+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
mannitol degradation II
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SYSTEMATIC NAME
IUBMB Comments
mannitol:NAD+ 1-oxidoreductase
The enzyme from Apium graveolens (celery) oxidizes alditols with a minimum requirement of 2R chirality at the carbon adjacent to the primary carbon undergoing the oxidation. The enzyme is specific for NAD+ and does not use NADP+.
CAS REGISTRY NUMBER
COMMENTARY hide
144941-29-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
expression in Nicotiana tabacum
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Manually annotated by BRENDA team
tobacco
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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overexpression of MtD in zonal geranium (Pelargonium x hortorum) provides increased resistance to Botrytis cinerea. Botrytis secretes mannitol in cultures containing plant extract to suppress the plant's ROS signaling pathway
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-arabinitol + NAD+
D-lyxose + NADH + H+
show the reaction diagram
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r
D-glucitol + NAD+
D-gulose + NADH
show the reaction diagram
D-iditol + NAD+
D-idose + NADH
show the reaction diagram
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-
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r
D-mannitol + NAD+
D-mannose + NADH + H+
show the reaction diagram
D-talose + NADH
D-altritol + NAD+
show the reaction diagram
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ir
D-threitol + NAD+
D-threose + NADH
show the reaction diagram
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25% activity
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r
galactitol + NAD+
galactose + NADH
show the reaction diagram
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low activity
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r
i-erythreitol + NAD+
? + NADH
show the reaction diagram
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16% activity
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?
i-galactitol + NAD+
L-galactose + NADH
show the reaction diagram
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not oxidized by higher plants
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r
i-ribitol + NAD+
L-ribose + NADH
show the reaction diagram
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r
L-arabinitol + NAD+
L-arabinose + NADH
show the reaction diagram
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r
L-iditol + NAD+
L-idose + NADH
show the reaction diagram
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less than 10% activity
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r
additional information
?
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no cinnamyl alcohol dehydrogenase activity
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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-arabinitol + NAD+
D-lyxose + NADH + H+
show the reaction diagram
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r
D-iditol + NAD+
D-idose + NADH
show the reaction diagram
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r
D-mannitol + NAD+
D-mannose + NADH + H+
show the reaction diagram
D-talose + NADH
D-altritol + NAD+
show the reaction diagram
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ir
D-threitol + NAD+
D-threose + NADH
show the reaction diagram
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25% activity
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r
i-erythreitol + NAD+
? + NADH
show the reaction diagram
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16% activity
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?
i-ribitol + NAD+
L-ribose + NADH
show the reaction diagram
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r
L-arabinitol + NAD+
L-arabinose + NADH
show the reaction diagram
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r
L-iditol + NAD+
L-idose + NADH
show the reaction diagram
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less than 10% activity
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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dose dependent decrease in enzyme activity
1,4-dithioerythritol
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1.09 mM, 50% inhibition, partially reversed by diamide
1,4-dithiothreitol
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0.57 mM, 50% inhibition, reversed by diamide
2-mercaptoethanol
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30 mM, 50% inhibition, partially reversed by diamide
AMP
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Ki: 0.50-0.80 mM at pH 9.5, Ki = 0.64 mM at pH 7.0
ATP
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Ki: 1.10 mM at pH 7.0
D-mannose
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competitive inhibition, Ki: 200 mM
D-threose
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competitive inhibition, Ki: 18 mM
NADH
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strong inhibition at 0.1 mM
additional information
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EDTA and EGTA did not affect enzyme activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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MTD is secreted into the apoplast after treatment with salicylic acid
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
64 - 400
D-mannitol
745
D-mannose
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0.14 - 0.26
NAD+
0.00127
NADH
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.32
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D-mannitol
1.9
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at pH 9.5
2.2
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at pH 7.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
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D-mannose reduction
7.5 - 9
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not greatly affected between
9.5
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D-mannitol oxidation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
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SDS-PAGE
43000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 40000, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, stable for several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to homogeneity, affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Nicotiana tabacum variant Burley 21
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expressed in zonal geranium (Pelargonium x hortorum)
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gene APIg1, DNA and amino acid sequence determination, analysis, and comparison, development of a quantitative PCR-based DNA detection method for use in food samples, overview
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
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constitutive expression of enzyme in Nicotiana tabacum confers significantly enhanced resistance to Alternaria alternata, but not to Cercospora nicotianae
diagnostics
the enzyme is a major food allergen and its occurance in food, e.g. in celery sticks, celeriac, celery powder, or celery seeds, is required to be labeled, development of a quantitative PCR-based DNA detection method for use in food samples, overview