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Information on EC 1.1.1.255 - mannitol dehydrogenase and Organism(s) Apium graveolens and UniProt Accession Q38707

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IUBMB Comments
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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This record set is specific for:
Apium graveolens
UNIPROT: Q38707
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Word Map
The taxonomic range for the selected organisms is: Apium graveolens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
mannitol dehydrogenase, mannitol:mannose 1-oxidoreductase, nad-dependent mannitol dehydrogenase, mannitol 1-oxidoreductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
mannitol 1-dehydrogenase
-
-
-
-
mannitol 1-oxidoreductase
-
-
-
-
mannitol:mannose 1-oxidoreductase
-
-
NAD-dependent mannitol dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-mannitol + NAD+
D-mannose + NADH + H+
show the reaction diagram
-
-
-
?
D-arabinitol + NAD+
D-lyxose + NADH + H+
show the reaction diagram
-
-
-
r
D-glucitol + NAD+
D-gulose + NADH
show the reaction diagram
D-iditol + NAD+
D-idose + NADH
show the reaction diagram
-
-
-
r
D-mannitol + NAD+
D-mannose + NADH + H+
show the reaction diagram
D-talose + NADH
D-altritol + NAD+
show the reaction diagram
-
-
-
ir
D-threitol + NAD+
D-threose + NADH
show the reaction diagram
-
25% activity
-
r
galactitol + NAD+
galactose + NADH
show the reaction diagram
-
low activity
-
r
i-erythreitol + NAD+
? + NADH
show the reaction diagram
-
16% activity
-
?
i-galactitol + NAD+
L-galactose + NADH
show the reaction diagram
-
not oxidized by higher plants
-
r
i-ribitol + NAD+
L-ribose + NADH
show the reaction diagram
-
-
-
r
L-arabinitol + NAD+
L-arabinose + NADH
show the reaction diagram
-
-
-
r
L-iditol + NAD+
L-idose + NADH
show the reaction diagram
-
less than 10% activity
-
r
additional information
?
-
-
no cinnamyl alcohol dehydrogenase activity
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-mannitol + NAD+
D-mannose + NADH + H+
show the reaction diagram
-
-
-
?
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
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
-
-
-
r
L-iditol + NAD+
L-idose + NADH
show the reaction diagram
-
less than 10% activity
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
dose dependent decrease in enzyme activity
1,4-dithioerythritol
-
1.09 mM, 50% inhibition, partially reversed by diamide
1,4-dithiothreitol
-
0.57 mM, 50% inhibition, reversed by diamide
2-mercaptoethanol
-
30 mM, 50% inhibition, partially reversed by diamide
AMP
-
Ki: 0.50-0.80 mM at pH 9.5, Ki = 0.64 mM at pH 7.0
ATP
-
Ki: 1.10 mM at pH 7.0
D-mannose
-
competitive inhibition, Ki: 200 mM
D-threose
-
competitive inhibition, Ki: 18 mM
NADH
-
strong inhibition at 0.1 mM
additional information
-
EDTA and EGTA did not affect enzyme activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
MTD is secreted into the apoplast after treatment with salicylic acid
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
64 - 400
D-mannitol
745
D-mannose
-
-
0.14 - 0.26
NAD+
0.00127
NADH
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.32
-
D-mannitol
1.9
-
at pH 9.5
2.2
-
at pH 7.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
D-mannose reduction
7.5 - 9
-
not greatly affected between
9.5
-
D-mannitol oxidation
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
young leaf
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MTDH_APIGR
365
0
39691
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
SDS-PAGE
40000
43000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 40000, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, stable for several months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to homogeneity, affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Nicotiana tabacum variant Burley 21
expressed in zonal geranium (Pelargonium x hortorum)
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
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Stoop, J.M.H.; Chilton, W.S.; Pharr, D.M.
Substrate stereospecificity of the NAD-dependent mannitol dehydrogenase from celery
Phytochemistry
43
1145-1150
1996
Apium graveolens
-
Manually annotated by BRENDA team
Stoop, J.M.H.; Williamson, J.D.; Conkling, M.A.; Pharr, D.M.
Purification of NAD-dependent mannitol dehydrogenase from celery suspension culture
Plant Physiol.
108
1219-1225
1995
Apium graveolens
Manually annotated by BRENDA team
Williamson, J.D.; Stoop, J.M.H.; Massel, M.O.; Conkling, M.A.; Pharr, D.M.
Sequence analysis of a mannitol dehydrogenase cDNA from plants reveals a function for the pathogenesis-related protein ELI3
Proc. Natl. Acad. Sci. USA
92
7148-7152
1995
Apium graveolens
Manually annotated by BRENDA team
Stoop, J.M.H.; Pharr, D.M.
Effect of different carbon sources on relative growth rate, internal carbohydrates, and mannitol 1-oxidoreductase activity in celery suspension culture
Plant Physiol.
103
1001-1008
1993
Apium graveolens
Manually annotated by BRENDA team
Stoop, J.M.H.; Pharr, D.M.
Partial purification and characterization of mannitol:mannose 1-oxidoreductase from celeriac (Apium graveolens var. rapaceum) roots
Arch. Biochem. Biophys.
298
612-619
1992
Apium graveolens
Manually annotated by BRENDA team
Stoop, J.M.H.; Williamson, J.D.; Conkling, M.A.; MacKay, J.J.; Pharr, D.M.
Characterization of NAD-dependent mannitol dehydrogenase from celery as affected by ions, chelators, reducing agents and metabolites
Plant Sci.
131
43-51
1998
Apium graveolens
-
Manually annotated by BRENDA team
Yamamoto, Y.T.; Zamski, E.; Williamson, J.D.; Conkling, M.A.; Pharr, D.M.
Subcellular localization of celery mannitol dehydrogenase. A cytosolic metabolic enzyme in nuclei
Plant Physiol.
115
1397-1403
1997
Apium graveolens
Manually annotated by BRENDA team
Prata, R.T.N.; Williamson, J.D.; Conkling, M.A.; Pharr, D.M.
Sugar repression of mannitol dehydrogenase activity in celery cells
Plant Physiol.
114
307-314
1997
Apium graveolens
Manually annotated by BRENDA team
Mustorp, S.; Engdahl-Axelsson, C.; Svensson, U.; Holck, A.
Detection of celery (Apium graveolens), mustard (Sinapis alba, Brassica juncea, Brassica nigra) and sesame (Sesamum indicum) in food by real-time PCR
Eur. Food Res. Technol.
226
771-778
2008
Apium graveolens (Q38707)
Manually annotated by BRENDA team
Cheng, F.Y.; Zamski, E.; Guo, W.W.; Pharr, D.M.; Williamson, J.D.
Salicylic acid stimulates secretion of the normally symplastic enzyme mannitol dehydrogenase: a possible defense against mannitol-secreting fungal pathogens
Planta
230
1093-1103
2009
Apium graveolens (Q38707)
Manually annotated by BRENDA team
Williamson, J.; Desai, A.; Krasnyanski, S.; Ding, F.; Guo, W.; Nguyen, T.; Olson, H.; Dole, J.; Allen, G.
Overexpression of mannitol dehydrogenase in zonal geranium confers increased resistance to the mannitol secreting fungal pathogen Botrytis cinerea
Plant Cell Tissue Organ Cult.
115
367-375
2013
Apium graveolens (Q38707)
-
Manually annotated by BRENDA team