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
-
-
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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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-
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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
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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 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
-
-
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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
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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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pathogen-induced endogenous enzyme
Manually annotated by BRENDA team
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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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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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meristematic cell, cap 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