Any feedback?
Information on EC 4.2.1.47 - GDP-mannose 4,6-dehydratase
for references in articles please use BRENDA:EC4.2.1.47Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
4.2.1.47 GDP-mannose 4,6-dehydrataseIUBMB 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 .
Specify your search results
Word Map
- 4.2.1.47
- alginate
-
fucosylation
- gdp-l-fucose
- mucoid
- l-fucose
- gdp-4-keto-6-deoxy-d-mannose
-
gdp-mannuronic
- gdp-d-rhamnose
- phosphomannomutase
-
fucosyltransferase
-
gdp-4-keto-6-deoxymannose
- d-rhamnose
- synthesis
- biotechnology
The enzyme appears in 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 dehydratase, gdp-mannose 4,6 dehydratase, gdp-d-mannose dehydratase, pbcv-1 gmd, m-gmd, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bceN
Dm-gmd
-
-
-
-
GDP-alpha-D-mannose 4,6-dehydratase
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 4,6-dehydratase
-
-
-
-
GDP-mannose dehydratase
-
-
-
-
GDP-mannose dehydrogenase
GMD
Guanosine 5'-diphosphate-D-mannose oxidoreductase
-
-
-
-
Guanosine diphosphomannose 4,6-dehydratase
-
-
-
-
Guanosine diphosphomannose oxidoreductase
-
-
-
-
ORF13.7
-
-
-
-
PBCV-1 GMD
GDP-D-mannose 4,6-dehydratase
-
-
-
-
GMD
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GDP-alpha-D-mannose = GDP-4-dehydro-alpha-D-rhamnose + H2O
-
-
-
-
GDP-alpha-D-mannose = GDP-4-dehydro-alpha-D-rhamnose + H2O
mechanism
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
37211-59-9
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GDP-4-dehydro-6-deoxy-D-mannose
GDP-D-rhamnose
i.e., GDP-6-deoxy-D-lyxo-hexos-4-ulose
-
-
?
GDP-alpha-D-mannose
GDP-4-dehydro-alpha-D-rhamnose + H2O
-
-
-
?
GDP-D-mannose
GDP-4-dehydro-6-deoxy-D-mannose + H2O
-
-
-
-
?
GDP-D-mannose
GDP-4-dehydro-6-deoxy-D-mannose + H2O
Paramecium bursaria Chlorella virus-1
-
-
-
-
?
GDP-mannose
GDP-4-dehydro-6-deoxy-D-mannose + H2O
-
ATCV-1GMD has no reductase activity
-
-
?
GDP-mannose
GDP-4-dehydro-6-deoxy-D-mannose + H2O
-
-
-
?
GDP-mannose
GDP-4-dehydro-6-deoxy-D-mannose + H2O
-
-
-
?
GDP-mannose
GDP-4-dehydro-6-deoxy-D-mannose + H2O
Paramecium bursaria Chlorella virus-1
-
ATCV-1GMD has no reductase activity
-
-
?
GDP-mannose
GDP-4-dehydro-6-deoxy-D-mannose + H2O
-
key regulatory enzyme controlling alginate biosynthesis in mucoid strain of pseudomonas aeruginosa
-
-
?
GDP-mannose
GDP-4-dehydro-6-deoxy-D-mannose + H2O
is a bifunctional 4,6-dehydratase, and a stereospecific 4-reductase. A conserved amino acid side chain (Arg185) may be crucial for orienting substrate and cofactor
-
-
?
GDP-mannose
GDP-4-dehydro-6-deoxy-D-mannose + H2O
-
stereochemistry and mechanism
-
?
additional information
?
-
first step in the de novo pathway of GDP-L-fucose biosynthesis
-
?
additional information
?
-
-
first step in the de novo pathway of GDP-L-fucose biosynthesis
-
?
additional information
?
-
-
co-expression and activities of GDP-mannose 4,6-dehydratase and GDP-L-fucose synthetase lead toptoduction of GDP-L-fucose
-
-
?
additional information
?
-
-
co-expression and activities of GDP-mannose 4,6-dehydratase and GDP-L-fucose synthetase lead toptoduction of GDP-L-fucose
-
-
?
additional information
?
-
key step in the de novo pathway of GDP-L-fucose biosynthesis
-
?
additional information
?
-
-
key step in the de novo pathway of GDP-L-fucose biosynthesis
-
?
additional information
?
-
-
enzyme of the constitutively active de novo pathway for biosynthesis of GDP-L-fucose
-
-
?
additional information
?
-
Paramecium bursaria chlorella virus
-
enzyme is involved in modification of structural proteins
-
-
?
additional information
?
-
-
enzyme of the constitutively active de novo pathway for biosynthesis of GDP-L-fucose
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GDP-mannose
GDP-4-dehydro-6-deoxy-D-mannose + H2O
-
key regulatory enzyme controlling alginate biosynthesis in mucoid strain of pseudomonas aeruginosa
-
-
?
GDP-alpha-D-mannose
GDP-4-dehydro-alpha-D-rhamnose + H2O
-
-
-
?
additional information
?
-
first step in the de novo pathway of GDP-L-fucose biosynthesis
-
?
additional information
?
-
-
first step in the de novo pathway of GDP-L-fucose biosynthesis
-
?
additional information
?
-
-
co-expression and activities of GDP-mannose 4,6-dehydratase and GDP-L-fucose synthetase lead toptoduction of GDP-L-fucose
-
-
?
additional information
?
-
-
co-expression and activities of GDP-mannose 4,6-dehydratase and GDP-L-fucose synthetase lead toptoduction of GDP-L-fucose
-
-
?
additional information
?
-
key step in the de novo pathway of GDP-L-fucose biosynthesis
-
?
additional information
?
-
-
key step in the de novo pathway of GDP-L-fucose biosynthesis
-
?
additional information
?
-
-
enzyme of the constitutively active de novo pathway for biosynthesis of GDP-L-fucose
-
-
?
additional information
?
-
Paramecium bursaria chlorella virus
-
enzyme is involved in modification of structural proteins
-
-
?
additional information
?
-
-
enzyme of the constitutively active de novo pathway for biosynthesis of GDP-L-fucose
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
Paramecium bursaria Chlorella virus-1
-
the enzymatically active proteins contain tightly bound NADPH that essential for maintaining the oligomerization status as well as for the stabilization and function of the enzyme
NADPH
-
the enzymatically active proteins contain tightly bound NADPH that is essential for maintaining the oligomerization status as well as for the stabilization and function of the enzyme
NADPH
addition of NADPH results in the gradual, His6-GMD-dependent reduction of GDP-6-deoxy-D-lyxo-hexos-4-ulose to GDP-D-rhamnose
additional information
Paramecium bursaria Chlorella virus-1
-
the enzyme has a very low affinity for NADP+
-
additional information
-
the enzyme has a very low affinity for NADP+
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
additional information
divalent cations are not required for GMD activity
additional information
-
divalent cations are not required for GMD activity
additional information
GMD activity is not affected by Ca2+ at 5 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Mg2+
high concentrations of MgCl2 (25 mM) have an inhibitory effect on enzyme activity
NADP+
-
conversion of NADPH to NADP+ results in complete inactivation of the enzyme
NADP+
Paramecium bursaria Chlorella virus-1
-
conversion of NADPH to NADP+ results in complete inactivation of the enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
specific activity activity of GDP-mannose dehydrogense increases with dissolved oxygen tension of up to 25% of air saturation and maintains the maximal value up to at least 70% of air saturation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
Glycomic Profiling Highlights Increased Fucosylation in Pseudomyxoma Peritonei.
Cerebral Hemorrhage
Protein fucosylation is required for Notch dependent vascular integrity in zebrafish.
Colonic Neoplasms
Deficiency of GMD leads to escape from NK cell-mediated tumor surveillance through modulation of TRAIL signaling.
Colonic Neoplasms
GDP-mannose-4,6-dehydratase (GMDS) deficiency renders colon cancer cells resistant to tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) receptor- and CD95-mediated apoptosis by inhibiting complex II formation.
Colorectal Neoplasms
Mutation of GDP-mannose-4,6-dehydratase in colorectal cancer metastasis.
Cystic Fibrosis
Alginate biosynthetic enzymes in mucoid and nonmucoid Pseudomonas aeruginosa: overproduction of phosphomannose isomerase, phosphomannomutase, and GDP-mannose pyrophosphorylase by overexpression of the phosphomannose isomerase (pmi) gene.
Cystic Fibrosis
Control of alginate synthesis in Pseudomonas aeruginosa: regulation of the algR1 gene.
Dehydration
A Parsimonious Mechanism of Sugar Dehydration by Human GDP-Mannose-4,6-dehydratase.
Dehydration
Preparative synthesis of GDP-beta-L-fucose by recombinant enzymes from enterobacterial sources.
Infections
Evolution and comparative genomics of Campylobacter jejuni ST-677 clonal complex.
Neoplasm Metastasis
GDP-mannose-4,6-dehydratase (GMDS) deficiency renders colon cancer cells resistant to tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) receptor- and CD95-mediated apoptosis by inhibiting complex II formation.
Neoplasm Metastasis
Mutation of GDP-mannose-4,6-dehydratase in colorectal cancer metastasis.
Neoplasms
GDP-mannose-4,6-dehydratase (GMDS) deficiency renders colon cancer cells resistant to tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) receptor- and CD95-mediated apoptosis by inhibiting complex II formation.
Tuberculosis
Deciphering the genetic bases of the structural diversity of phenolic glycolipids in strains of the Mycobacterium tuberculosis complex.
Virus Diseases
Paramecium bursaria Chlorella virus 1 encodes two enzymes involved in the biosynthesis of GDP-L-fucose and GDP-D-rhamnose.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.024
GDP-alpha-D-mannose
at pH 7.4 and 25°C, in the presence of 1 mol MgCl2 per mol of protein
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
GDP-alpha-D-mannose
at pH 7.4 and 25°C, in the presence of 1 mol MgCl2 per mol of protein
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.977
GDP-alpha-D-mannose
at pH 7.4 and 25°C, in the presence of 1 mol MgCl2 per mol of protein
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.913
GDP-alpha-D-mannose
at pH 7.4 and 25°C, in the presence of 1 mol MgCl2 per mol of protein
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 11
pH 5: 45% of maximal activity, pH 11: 75% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 55
25°C: about 60% of maximal activity, 55°C: about 70% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
syncytia induced by nematode Heterodera schachtii
UniProt
brenda
expression of GMD is higher in macrophages than in endothelial cells
-
-
brenda
expression of GMD was higher in macrophages than in endothelial cells
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
-
mutations in this enzyme participate in the progression of colorectal cancer
metabolism
physiological function
evolution
-
GMD belongs to the reductase-epimerase-dehydrogenase superfamily which has a catalytic triad, Ser-Tyr-Lys, that is highly conserved
evolution
-
GMD belongs to the reductase-epimerase-dehydrogenase superfamily which has a catalytic triad, Ser-Tyr-Lys, that is highly conserved
-
metabolism
GMD catalyzes the first step in the de novo synthesis pathways of GDP-L-fucose, overview
metabolism
the first step of the de novo pathway starting from GDP-D-mannose is a dehydration reaction catalysed by the specific nucleotide-sugar dehydratase GMD resulting in GDP-L-fucose synthesis
metabolism
-
the enzyme is required for Fng-dependent Notch signaling and the fucosylation of bulk proteins
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
physiological function
-
GMD is involved in the breakdown of ingested polysaccharides into a form that could not be absorbed and utilized by the host otherwise
physiological function
-
GMD is involved in the breakdown of ingested polysaccharides into a form that could not be absorbed and utilized by the host otherwise
-
Show AA Sequence and Transmembrane Helices (28462 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
140000
41200
3 * 45000, recombinant His-tagged GMD, SDS-PAGE, 3 * 41200, about, sequence calculation
42000
45000
45000
3 * 45000, recombinant His-tagged GMD, SDS-PAGE, 3 * 41200, about, sequence calculation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
tetramer
trimer
additional information
dimer
-
homodimer, gel filtration, equilibrium ultracentrifugation experiments
trimer
3 * 45000, recombinant His-tagged GMD, SDS-PAGE, 3 * 41200, about, sequence calculation
additional information
-
NADPH is essential for maintaining the oligomerization status
additional information
Paramecium bursaria Chlorella virus-1
-
NADPH is essential for maintaining the oligomerization status
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, complexed with NADPH, GDP and GDP-D-rhamnose
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
deletion of alpha-1,3-fucose and alpha-1,4-fucose residues in Nicotiana benthamiana plants N-glycans by repression of the GMD gene using virus-induced gene silencing and RNA interference, GMD expression analysis, and MALDI-TOF-mass spectrometric analysis of N-glycans in wild-type and mutant plants, overview
additional information
-
deletion of alpha-1,3-fucose and alpha-1,4-fucose residues in Nicotiana benthamiana plants N-glycans by repression of the GMD gene using virus-induced gene silencing and RNA interference, GMD expression analysis, and MALDI-TOF-mass spectrometric analysis of N-glycans in wild-type and mutant plants, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
His6-GMD loses activity slowly in the course of enzyme-substrate incubations, particularly at 37°C, but 4,6-dehydratase activity is still detectable after incubation for 16 h at 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
NADPH is essential for stabilization and function of the enzyme
NADPH is essential for stabilization and function of the enzyme
Paramecium bursaria Chlorella virus-1
-
NADPH is essential for stabilization and function of the enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is not very sensitive to oxidative inactivation. Specific activity activity of GDP-mannose dehydrogense increases with dissolved oxygen tension of up to 25% of air saturation and maintains the maximal value up to at least 70% of air saturation
-
665895
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by ultrasonication, centrifugation, on Ni2+-nitrilotriacetic acid resin and by anion exchange chromatography, to greater than 95% purity
GSH-Sepharose 4B column chromatography
only isoenzyme L-GMD and isoenzyme M-GMD are soluble, isoenzyme S-GMD is inactive and forms a precipitate
recombinant His-tagged GMD from Escherichia coli by nickel affinity chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
coexpression with GDP-4-keto-6-deioxymannose-3,5-epimerase-4-reductase, which is required for enzymatic activity after expresseion in Saccharomyces cerevisiae
-
expressed in Escherichia coli as glutathione S-transferase fusion protein
expression in Escherichia coli
GDP-D-mannose-4,6-dehydratase and GDP-4-keto-6-deoxymannose 3, 5-epimerase 4-reductase, the two crucial enzymes for the de novo GDP-L-fucose biosynthesis, are overexpressed in recombinant Escherichia coli by constructing inducible overexpression vectors. Optimum expression conditions in recombinant Escherichia coli BL21(DE3) are 25°C and 0.1 mM isopropyl-beta-D-thioglucopyranoside. Maximum GDP-L-fucose concentration of 38.9 mg/l is obtained in a glucose-limited fed-batch cultivation, and it is enhanced further by coexpression of NADPH-regenerating glucose-6-phosphate dehydrogenase encoded by the zwf gene to achieve 55.2 mg/l GDP-L-fucose under the same cultivation condition
-
GMD sequence determination and analysis, sequence comparison and phylogenetic tree, functional overexpression of soluble GMD in Escherichia coli strain BL21(DE3) from an IPTG-inducible expression vector, optimum expression conditions are 30°C and 0.1 mM IPTG
-
into pET28a+ to construct pLW1534, expressed in Escherichia coli BL21 as His-tagged fusion protein
expressed in Escherichia coli as glutathione S-transferase fusion protein
Paramecium bursaria Chlorella virus-1
-
expressed in Escherichia coli as glutathione S-transferase fusion protein
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
repression of the GMD gene is thus very useful for deleting immunogenic total fucose residues and facilitating the production of pharmaceutical glycoproteins in plants
synthesis
synthesis
GMD knockout CHO cells are ideal host cells for the manufacture of completely non-fucosylated therapeutic antibodies and completely O-fucose-negative therapeutics as well
synthesis
repression of the GMD gene is thus very useful for deleting immunogenic total fucose residues and facilitating the production of pharmaceutical glycoproteins in plants
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ripka, J.; Adamany, A.; Stanley, P.
Two chinese hamster ovary glycosylation mutants affected in the conversion of GDP-mannose to GDP-fucose
Arch. Biochem. Biophys.
249
533-545
1986
Metazoa, Bacteria, Cricetulus griseus, Embryophyta
brenda
Broschat, K.O.; Chang, S.; Serif, G.
Purification and characterization of GDP-D-mannose 4,6 dehydratase from porcine thyroid
Eur. J. Biochem.
153
397-401
1985
Sus scrofa
brenda
Liao, T.H.; Barber, G.A.
Purification of guanosine 5'-diphosphate d-mannose oxidoreductase from Phaseolus vulgaris
Biochim. Biophys. Acta
276
85-93
1972
Phaseolus vulgaris
brenda
Elbein, A.D.; Heath, E.C.
The biosynthesis of cell wall lipopolysaccharide in Escherichia coli
J. Biol. Chem.
240
1926-1931
1965
Escherichia coli
brenda
Oths, P.J.; Mayer, R.M.; Floss, H.G.
Stereochemistry and mechanism of the GDP-mannose dehydratase reaction
Carbohydr. Res.
198
91-100
1990
Saccharomyces cerevisiae
brenda
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
brenda
Sturla, L.; Bisso, A.; Zanardi, D.; Benatti, U.; De Flora, A.; Tonetti, M.
Expression, purification and characterization of GDP-D-mannose 4,6,-dehydratase from Escherichia coli
FEBS Lett.
412
126-130
1997
Escherichia coli, Klebsiella pneumoniae
brenda
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)
brenda
Yamamoto, K.; Katayama, I.; Onoda, Y.; Inami, M.; Kumagai, H.; Tochikura, T.
Evidence that the enzyme catalyzing the conversion of guanosine diphosphate D-mannose to a 4-keto sugar nucleotide intermediate requires nicotinamide adenine dinucleotide phosphate
Arch. Biochem. Biophys.
300
694-698
1993
Klebsiella pneumoniae
brenda
Bonin, C.P.; Potter, I.; Vanzin, G.F.; Reiter, W.D.
The MUR1 gene of Arabidopsis thaliana encodes an isoform of GDP-D-mannose-4,6-dehydratase, catalyzing the first step in the de novo synthesis of GDP-L-fucose
Proc. Natl. Acad. Sci. USA
94
2085-2090
1997
Arabidopsis thaliana (P93031), Arabidopsis thaliana
brenda
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
Metazoa, Bacteria, Bos taurus, Escherichia coli, Homo sapiens, Klebsiella pneumoniae, Nereis sp., Sus scrofa
brenda
Mulichak, A.M.; Bonin, C.P.; Reiter, W.D.; Garavito, R.M.
Structure of the MUR1 GDP-mannose 4,6-dehydratase from Arabidopsis thaliana: implications for ligand binding and specificity
Biochemistry
41
15578-15589
2002
Arabidopsis thaliana (P93031), Arabidopsis thaliana
brenda
Suzuki, N.; Nakano, Y.; Yoshida, Y.; Nezu, T.; Terada, Y.; Yamashita, Y.; Koga, T.
Guanosine diphosphate-4-keto-6-deoxy-D-mannose reductase in the pathway for the synthesis of GDP-6-deoxy-D-talose in Actinobacillus actinomycetemcomitans
Eur. J. Biochem.
269
5963-5971
2002
Aggregatibacter actinomycetemcomitans
brenda
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
brenda
Nakayama, K.; Maeda, Y.; Jigami, Y.
Interaction of GDP-4-keto-6-deoxymannose-3,5-epimerase-4-reductase with GDP-mannose-4,6-dehydratase stabilizes the enzyme activity for formation of GDP-fucose from GDP-mannose
Glycobiology
13
673R-680R
2003
Arabidopsis thaliana
-
brenda
Webb, N.A.; Mulichak, A.M.; Lam, J.S.; Rocchetta, H.L.; Garavito, R.M.
Crystal structure of a tetrameric GDP-D-mannose 4,6-dehydratase from a bacterial GDP-D-rhamnose biosynthetic pathway
Protein Sci.
13
529-539
2004
Pseudomonas aeruginosa
brenda
Somoza, J.R.; Menon, S.; Schmidt, H.; Joseph-McCarthy, D.; Dessen, A.; Stahl, M.L.; Somers, W.S.; Sullivan, F.X.
Structural and kinetic analysis of Escherichia coli GDP-mannose 4,6 dehydratase provides insights into the enzyme's catalytic mechanism and regulation by GDP-fucose
Structure Fold. Des.
8
123-135
2000
Escherichia coli
brenda
Rosano, C.; Zuccotti, S.; Sturla, L.; Fruscione, F.; Tonetti, M.; Bolognesi, M.
Quaternary assembly and crystal structure of GDP-D-mannose 4,6 dehydratase from Paramecium bursaria Chlorella virus
Biochem. Biophys. Res. Commun.
339
191-195
2006
Paramecium bursaria chlorella virus
brenda
Tatnell, P.J.; Russell, N.J.; Gacesa, P.
A metabolic study of the activity of GDP-mannose dehydrogenase and concentrations of activated intermediates of alginate biosynthesis in Pseudomonas aeruginosa
J. Gen. Microbiol.
139
119-127
1993
Pseudomonas aeruginosa
brenda
Leitao, J.H.; Sa-Correia, I.
Oxygen-dependent alginate synthesis and enzymes in Pseudomonas aeruginosa
J. Gen. Microbiol.
139
441-445
1993
Pseudomonas aeruginosa
brenda
Niittymaki, J.; Mattila, P.; Renkonen, R.
Differential gene expression of GDP-L-fucose-synthesizing enzymes, GDP-fucose transporter and fucosyltransferase VII
APMIS
114
539-548
2006
Mus musculus, Rattus norvegicus
brenda
Byun, S.G.; Kim, M.D.; Lee, W.H.; Lee, K.J.; Han, N.S.; Seo, J.H.
Production of GDP-L-fucose, L-fucose donor for fucosyloligosaccharide synthesis, in recombinant Escherichia coli
Appl. Microbiol. Biotechnol.
74
768-775
2007
Escherichia coli
brenda
Fruscione, F.; Sturla, L.; Duncan, G.; Van Etten, J.L.; Valbuzzi, P.; De Flora, A.; Di Zanni, E.; Tonetti, M.
Differential role of NADP+ and NADPH in the activity and structure of GDP-D-mannose 4,6-dehydratase from two Chlorella viruses
J. Biol. Chem.
283
184-193
2008
Paramecium bursaria Chlorella virus-1, Acanthocystis turfacea chlorella virus 1
brenda
Kanda, Y.; Imai-Nishiya, H.; Kuni-Kamochi, R.; Mori, K.; Inoue, M.; Kitajima-Miyama, K.; Okazaki, A.; Iida, S.; Shitara, K.; Satoh, M.
Establishment of a GDP-mannose 4,6-dehydratase (GMD) knockout host cell line: a new strategy for generating completely non-fucosylated recombinant therapeutics
J. Biotechnol.
130
300-310
2007
Cricetulus griseus (Q8K3X3), Cricetulus griseus
brenda
Siddique, S.; Endres, S.; Atkins, J.M.; Szakasits, D.; Wieczorek, K.; Hofmann, J.; Blaukopf, C.; Urwin, P.E.; Tenhaken, R.; Grundler, F.M.; Kreil, D.P.; Bohlmann, H.
Myo-inositol oxygenase genes are involved in the development of syncytia induced by Heterodera schachtii in Arabidopsis roots
New Phytol.
184
457-472
2009
Arabidopsis thaliana (P93031), Arabidopsis thaliana (Q9SNY3)
brenda
Ren, Y.; Perepelov, A.V.; Wang, H.; Zhang, H.; Knirel, Y.A.; Wang, L.; Chen, W.
Biochemical characterization of GDP-L-fucose de novo synthesis pathway in fungus Mortierella alpina
Biochem. Biophys. Res. Commun.
391
1663-1669
2010
Mortierella alpina (D3JU53), Mortierella alpina
brenda
King, J.D.; Poon, K.K.; Webb, N.A.; Anderson, E.M.; McNally, D.J.; Brisson, J.R.; Messner, P.; Garavito, R.M.; Lam, J.S.
The structural basis for catalytic function of GMD and RMD, two closely related enzymes from the GDP-D-rhamnose biosynthesis pathway
FEBS J.
276
2686-2700
2009
Pseudomonas aeruginosa (Q51366), Pseudomonas aeruginosa
brenda
Jang, M.; Lee, W.; Shin, S.; Han, N.; Seo, J.; Kim, M.
Molecular cloning of the genes for GDP-mannose 4,6-dehydratase and GDP-L-fucose synthetase from Bacteroides thetaiotaomicron
Food Sci. Biotechnol.
19
849-855
2010
Bacteroides thetaiotaomicron, Bacteroides thetaiotaomicron VPI-5482
-
brenda
Matsuo, K.; Matsumura, T.
Deletion of fucose residues in plant N-glycans by repression of the GDP-mannose 4,6-dehydratase gene using virus-induced gene silencing and RNA interference
Plant Biotechnol. J.
9
264-281
2011
Nicotiana benthamiana (B7XH28), Nicotiana benthamiana
brenda
Chin, Y.W.; Park, J.B.; Park, Y.C.; Kim, K.H.; Seo, J.H.
Metabolic engineering of Corynebacterium glutamicum to produce GDP-L-fucose from glucose and mannose
Bioprocess Biosyst. Eng.
36
749-756
2013
Escherichia coli
brenda
Matsuo, K.; Kagaya, U.; Itchoda, N.; Tabayashi, N.; Matsumura, T.
Deletion of plant-specific sugar residues in plant N-glycans by repression of GDP-D-mannose 4,6-dehydratase and beta-1,2-xylosyltransferase genes
J. Biosci. Bioeng.
118
448-454
2014
Nicotiana benthamiana
brenda
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
brenda
Sousa, S.A.; Feliciano, J.R.; Pinheiro, P.F.; Leitao, J.H.
Biochemical and functional studies on the Burkholderia cepacia complex bceN gene, encoding a GDP-D-mannose 4,6-dehydratase
PLoS ONE
8
e56902
2013
Burkholderia cepacia (B4EFL2), Burkholderia cepacia J2315 (B4EFL2)
brenda
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
brenda
Ayukawa, T.; Matsumoto, K.; Ishikawa, H.O.; Ishio, A.; Yamakawa, T.; Aoyama, N.; Suzuki, T.; Matsuno, K.
Rescue of Notch signaling in cells incapable of GDP-L-fucose synthesis by gap junction transfer of GDP-L-fucose in Drosophila
Proc. Natl. Acad. Sci. USA
109
15318-15323
2012
Drosophila melanogaster
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 4.2.1.47)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
