Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 4.2.1.47 - GDP-mannose 4,6-dehydratase and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q51366

for references in articles please use BRENDA:EC4.2.1.47
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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 .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Pseudomonas aeruginosa
UNIPROT: Q51366
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
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
GDP-D-mannose-4,6-dehydratase
-
Dm-gmd
-
-
-
-
GDP-D-mannose 4,6-dehydratase
-
-
-
-
GDP-D-mannose 4-oxido-6-reductase
-
-
-
-
GDP-D-mannose 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
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GDP-alpha-D-mannose = GDP-4-dehydro-alpha-D-rhamnose + H2O
show the reaction diagram
mechanism
-
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-4-dehydro-6-deoxy-D-mannose
GDP-D-rhamnose
show the reaction diagram
i.e., GDP-6-deoxy-D-lyxo-hexos-4-ulose
-
-
?
GDP-mannose
GDP-4-dehydro-6-deoxy-D-mannose + H2O
show the reaction diagram
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
show the reaction diagram
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
GDP-mannose
GDP-4-dehydro-6-deoxy-D-mannose + H2O
show the reaction diagram
-
key regulatory enzyme controlling alginate biosynthesis in mucoid strain of pseudomonas aeruginosa
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01402
GDP-mannose
pH 7.5, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.82
GDP-mannose
pH 7.5, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
630
GDP-mannose
pH 7.5, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002859
GDP-mannose
pH 7.5, 37°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
-
homotetramer, crystallization experiments
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complexed with NADPH and GDP, hanging drop vapor diffusion method
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 25% glycerol, 1 year
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by ultrasonication, centrifugation, on Ni2+-nitrilotriacetic acid resin and by anion exchange chromatography, to greater than 95% purity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
His6-GMD expressed from the pQE-30-gmd vector
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Leitao, J.H.; Sa-Correia, I.
Oxygen-dependent alginate synthesis and enzymes in Pseudomonas aeruginosa
J. Gen. Microbiol.
139
441-445
1993
Pseudomonas aeruginosa
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team