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