Information on EC 1.1.1.255 - mannitol dehydrogenase

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The expected taxonomic range for this enzyme is: asterids

EC NUMBER
COMMENTARY
1.1.1.255
-
RECOMMENDED NAME
GeneOntology No.
mannitol dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
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-
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redox reaction
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-
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reduction
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-
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PATHWAY
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+.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
mannitol 1-dehydrogenase
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-
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mannitol 1-oxidoreductase
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-
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mannitol:mannose 1-oxidoreductase
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MTD
Q38707
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NAD-dependent mannitol dehydrogenase
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CAS REGISTRY NUMBER
COMMENTARY
144941-29-7
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
celery; L. var. dulce Mill. Pers.
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-
Manually annotated by BRENDA team
celery; L. var. dulce Mill. Pers. cv Florida 638
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-
Manually annotated by BRENDA team
gene APIg1
UniProt
Manually annotated by BRENDA team
expression in Nicotiana tabacum
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-arabinitol + NAD+
D-lyxose + NADH + H+
show the reaction diagram
-
-
-
r
D-glucitol + NAD+
D-gulose + NADH
show the reaction diagram
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low activity
-
r
D-glucitol + NAD+
D-gulose + NADH
show the reaction diagram
-
not oxidized by higher plants
-
r
D-iditol + NAD+
D-idose + NADH
show the reaction diagram
-
-
-
r
D-mannitol + NAD+
D-mannose + NADH + H+
show the reaction diagram
-
-
-
r
D-mannitol + NAD+
D-mannose + NADH + H+
show the reaction diagram
-
-
-
r
D-mannitol + NAD+
D-mannose + NADH + H+
show the reaction diagram
-
-
-
r
D-mannitol + NAD+
D-mannose + NADH + H+
show the reaction diagram
-
-
-
r
D-mannitol + NAD+
D-mannose + NADH + H+
show the reaction diagram
Q38707
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-
-
?
D-mannitol + NAD+
D-mannose + NADH + H+
show the reaction diagram
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highest activity, aldoses having 2S chirality are not reducible, with the exception of D-idose, marked preference for aldopentose and aldohexose, same stereospecificity in either direction with the same absolute configuration at C-2
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r
D-mannitol + NAD+
D-mannose + NADH + H+
show the reaction diagram
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mannitol pool size is important for regulating salt tolerance
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r
D-talose + NADH
D-altritol + NAD+
show the reaction diagram
-
-
-
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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-
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r
L-arabinitol + NAD+
L-arabinose + NADH
show the reaction diagram
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-
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r
L-iditol + NAD+
L-idose + NADH
show the reaction diagram
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less than 10% activity
-
r
additional information
?
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no cinnamyl alcohol dehydrogenase activity
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-arabinitol + NAD+
D-lyxose + NADH + H+
show the reaction diagram
-
-
-
r
D-iditol + NAD+
D-idose + NADH
show the reaction diagram
-
-
-
r
D-mannitol + NAD+
D-mannose + NADH + H+
show the reaction diagram
-
-
-
r
D-mannitol + NAD+
D-mannose + NADH + H+
show the reaction diagram
-
-
-
r
D-mannitol + NAD+
D-mannose + NADH + H+
show the reaction diagram
-
-
-
r
D-mannitol + NAD+
D-mannose + NADH + H+
show the reaction diagram
-
highest activity, aldoses having 2S chirality are not reducible, with the exception of D-idose, marked preference for aldopentose and aldohexose, same stereospecificity in either direction with the same absolute configuration at C-2
-
r
D-mannitol + NAD+
D-mannose + NADH + H+
show the reaction diagram
-
mannitol pool size is important for regulating salt tolerance
-
r
D-talose + NADH
D-altritol + NAD+
show the reaction diagram
-
-
-
ir
D-threitol + NAD+
D-threose + NADH
show the reaction diagram
-
25% activity
-
r
i-erythreitol + NAD+
? + NADH
show the reaction diagram
-
16% activity
-
?
i-ribitol + NAD+
L-ribose + NADH
show the reaction diagram
-
-
-
r
L-arabinitol + NAD+
L-arabinose + NADH
show the reaction diagram
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-
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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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
ADP
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weak inhibition at 1 mM
ADP
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Ki: 0.24 mM at pH 7.0
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
NADH
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strong inhibition at 0.1 mM
D-threose
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competitive inhibition, Ki: 18 mM
additional information
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EDTA and EGTA did not affect enzyme activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
Q38707
MTD is secreted into the apoplast after treatment with salicylic acid
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KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
64
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D-Mannitol
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at pH 9.5
72
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D-Mannitol
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400
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D-Mannitol
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at pH 7.0
745
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D-mannose
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0.14
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NAD+
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at pH 9.5
0.23
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NAD+
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at pH 7.0
0.26
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NAD+
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0.00127
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NADH
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SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
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enzyme activity is repressed in cells grown in various amendments of hexoses, sugar repression appears to be mediated by hexokinases
Manually annotated by BRENDA team
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pathogen-induced endogenous enzyme
Manually annotated by BRENDA team
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highest activity for cells grown in mannitol
Manually annotated by BRENDA team
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2-3fold higher enzyme activity in mannitol-grown cells
Manually annotated by BRENDA team
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pathogen-induced endogenous enzyme
Manually annotated by BRENDA team
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cap cell; meristematic cell
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35000
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Q38707
SDS-PAGE
40000
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PAGE and immunoblot analysis
43000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
monomer
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1 * 40000, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-80°C, stable for several months
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Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
to homogeneity, affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Nicotiana tabacum variant Burley 21
Q38707
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
Q38707
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
diagnostics
Q38707
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
biotechnology
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constitutive expression of enzyme in Nicotiana tabacum confers significantly enhanced resistance to Alternaria alternata, but not to Cercospora nicotianae