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Information on EC 4.2.1.47 - GDP-mannose 4,6-dehydratase and Organism(s) Homo sapiens

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.47 GDP-mannose 4,6-dehydratase
IUBMB Comments
The bacterial enzyme requires bound NAD+. This enzyme forms the first step in the biosynthesis of GDP-alpha-D-rhamnose and GDP-beta-L-fucose. In Aneurinibacillus thermoaerophilus L420-91T, this enzyme acts as a bifunctional enzyme, catalysing the above reaction as well as the reaction catalysed by EC 1.1.1.281, GDP-4-dehydro-6-deoxy-D-mannose reductase . Belongs to the short-chain dehydrogenase/reductase enzyme family, having homologous structures and a conserved catalytic triad of Lys, Tyr and Ser/Thr residues .
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
gdp-mannose dehydrogenase, gdp-mannose 4,6-dehydratase, gdp-d-mannose 4,6-dehydratase, gdp-d-mannose-4,6-dehydratase, gdp-mannose-4,6-dehydratase, gdp-mannose 4,6 dehydratase, gdp-mannose dehydratase, gdp-d-mannose dehydratase, pbcv-1 gmd, m-gmd, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Dm-gmd
-
-
-
-
GDP-D-mannose 4,6-dehydratase
-
-
-
-
GDP-D-mannose 4-oxido-6-reductase
-
-
-
-
GDP-D-mannose dehydratase
-
-
-
-
GDP-D-mannose-4,6-dehydratase
-
-
GDP-mannose 4,6-dehydratase
-
-
-
-
GDP-mannose dehydratase
-
-
-
-
GDP-mannose-4,6-dehydratase
-
-
GMDS
-
-
Guanosine 5'-diphosphate-D-mannose oxidoreductase
-
-
-
-
Guanosine diphosphomannose 4,6-dehydratase
-
-
-
-
Guanosine diphosphomannose oxidoreductase
-
-
-
-
L-GMD
isoenzyme
M-GMD
isoenzyme
ORF13.7
-
-
-
-
S-GMD
isoenzyme
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
GDP-mannose 4,6-hydro-lyase (GDP-4-dehydro-6-deoxy-D-mannose-forming)
The bacterial enzyme requires bound NAD+. This enzyme forms the first step in the biosynthesis of GDP-alpha-D-rhamnose and GDP-beta-L-fucose. In Aneurinibacillus thermoaerophilus L420-91T, this enzyme acts as a bifunctional enzyme, catalysing the above reaction as well as the reaction catalysed by EC 1.1.1.281, GDP-4-dehydro-6-deoxy-D-mannose reductase [5]. Belongs to the short-chain dehydrogenase/reductase enzyme family, having homologous structures and a conserved catalytic triad of Lys, Tyr and Ser/Thr residues [6].
CAS REGISTRY NUMBER
COMMENTARY hide
37211-59-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GDP-mannose
GDP-4-dehydro-6-deoxy-D-mannose + H2O
show the reaction diagram
GDPmannose
?
show the reaction diagram
additional information
?
-
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
GDPmannose
?
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
GDP
competitive
GDP-L-fucose
GDP-L-glucose
competitive
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
-
activates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0035 - 0.00364
GDP-mannose
0.003 - 0.08
GDPmannose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8
GDP-mannose
pH 8, M-GMD and L-GMD
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0113
GDP-L-fucose
pH 8
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.11
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
additional information
-
including cultured cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
mutations in this enzyme participate in the progression of colorectal cancer
metabolism
-
the enzyme is required for the first step of fucose synthesis. The enzyme is a cytosolic partner of tankyrase 1 that inhibits its poly(ADP-ribose) polymerase activity and influences its stability
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GMDS_HUMAN
372
0
41950
Swiss-Prot
other Location (Reliability: 3)
B2R9X3_HUMAN
372
0
41851
TrEMBL
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38700
isoenzyme S-GMD, SDS-PAGE
40000
-
x * 40000, SDS-PAGE
40200
isoenzyme M-GMD, SDS-PAGE
42000
isoenzyme L-GMD, SDS-PAGE
80000
isoenzyme M-GMD, dimeric form, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 40000, SDS-PAGE
dimer
L-GMD and M-GMD form a homodimer, M-GMD: 2 * 40200, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, presence of reducing agents, 36 h, 50% loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
only isoenzyme L-GMD and isoenzyme M-GMD are soluble, isoenzyme S-GMD is inactive and forms a precipitate
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
L-GMD, S-GMD and M-GMD, expressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sullivan, F.X.; Kumar, R.; Kriz, R.; Stahl, M.; Xu, G.Y.; Rouse, G.; Chang, X.J.; Boodhoo, A.; Potvin, B.; Cumming, D.A.
Molecular cloning of human GDP-mannose 4,6-Dehydratase and reconstitution of GDP-fucose biosynthesis in vitro
J. Biol. Chem.
273
8193-8202
1998
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Sturla, L.; Etzioni, A.; Biso, A.; Zanardi, D.; De Flora, G.; Silengo, L.; De Flora, A.; Tonetti, M.
Defective intracellular activity of GDP-D-mannose 4,6-dehydratase in leukocyte adhesion deficiency type II syndrome
FEBS Lett.
429
274-278
1998
Homo sapiens (O60547)
Manually annotated by BRENDA team
Tonetti, M.; Sturla, L.; Bisso, A.; Zanardi, D.; Benatti, U.; De Flora, A.
The metabolism of 6-deoxyhexoses in bacterial and animal cells
Biochimie
80
923-931
1998
Bacteria, Bos taurus, Escherichia coli, Homo sapiens, Klebsiella pneumoniae, Metazoa, Nereis sp., Sus scrofa
Manually annotated by BRENDA team
Bisso, A.; Sturla, L.; Zanardi, D.; De Flora, A.; Tonetti, M.
Structural and enzymatic characterization of human recombinant GDP-D-mannose-4,6-dehydratase
FEBS Lett.
456
370-374
1999
Homo sapiens (O60547), Homo sapiens
Manually annotated by BRENDA team
Bisht, K.K.; Dudognon, C.; Chang, W.G.; Sokol, E.S.; Ramirez, A.; Smith, S.
GDP-mannose-4,6-dehydratase is a cytosolic partner of tankyrase 1 that inhibits its poly(ADP-ribose) polymerase activity
Mol. Cell. Biol.
32
3044-3053
2012
Homo sapiens
Manually annotated by BRENDA team
Nakayama, K.; Moriwaki, K.; Imai, T.; Shinzaki, S.; Kamada, Y.; Murata, K.; Miyoshi, E.
Mutation of GDP-mannose-4,6-dehydratase in colorectal cancer metastasis
PLoS ONE
8
e70298
2013
Homo sapiens
Manually annotated by BRENDA team