Information on EC 1.1.1.187 - GDP-4-dehydro-D-rhamnose reductase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

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EC NUMBER
COMMENTARY hide
1.1.1.187
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RECOMMENDED NAME
GeneOntology No.
GDP-4-dehydro-D-rhamnose reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GDP-alpha-D-rhamnose + NAD(P)+ = GDP-4-dehydro-alpha-D-rhamnose + NAD(P)H + H+
show the reaction diagram
In the reverse reaction, a mixture of GDP-D-rhamnose and its C-4 epimer is formed
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Fructose and mannose metabolism
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Amino sugar and nucleotide sugar metabolism
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GDP-D-rhamnose biosynthesis
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GDP-6-deoxy-D-talose biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
GDP-6-deoxy-alpha-D-mannose:NAD(P)+ 4-oxidoreductase
The enzyme, which operates in the opposite direction to that shown, forms a mixture of GDP-alpha-D-rhamnose and its C-4 epimer, GDP-6-deoxy-alpha-D-talose. cf. EC 1.1.1.281, GDP-4-dehydro-6-deoxy-D-mannose reductase and EC 1.1.1.135, GDP-6-deoxy-D-talose 4-dehydrogenase.
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CAS REGISTRY NUMBER
COMMENTARY hide
9075-56-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
soil bacterium GS, ATCC 19241
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Manually annotated by BRENDA team
pathovar glycinea
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Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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effect of deficiency in GDP-D-rhamnose biosynthetic genes, including GDP-4-keto-6-deoxy-D-mannose reductase, on lipopolysaccharide structure and pathogenicity in soybean, Glycine max cv. Shirofumi. The mutant strain DELTArmd shows highly reduced antimicrobial susceptibility with chloramphenicol, ampicillinm or spectinomycin. The mutant DELTArmd strain also shows increased degrees of adhesion to the polystyrene surface of the micro-titrate plates. It has higher hydrophobicity of the cell surface than the wild-type strain, but has normal flagellin glycans
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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 + NAD(P)H
GDP-6-deoxy-D-mannose + NAD(P)+
show the reaction diagram
GDP-4-dehydro-6-deoxy-D-mannose + NAD(P)H
GDP-D-talometylose + NAD(P)+
show the reaction diagram
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lacks precise stereoselectivity with respect to its hydrogen receptor carbonyl function
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?
GDP-4-dehydro-6-deoxy-D-mannose + NADPH
GDP-6-deoxy-D-talose + NADP+
show the reaction diagram
GDP-4-dehydro-alpha-D-rhamnose + NAD(P)H + H+
GDP-alpha-D-rhamnose + NAD(P)+
show the reaction diagram
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r
GDP-6-deoxy-D-lyxo-4-hexulose + NAD(P)H
GDP-alpha-D-rhamnose + NAD(P)+
show the reaction diagram
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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 + NAD(P)H
GDP-6-deoxy-D-mannose + NAD(P)+
show the reaction diagram
GDP-4-dehydro-6-deoxy-D-mannose + NAD(P)H
GDP-D-talometylose + NAD(P)+
show the reaction diagram
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lacks precise stereoselectivity with respect to its hydrogen receptor carbonyl function
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
GDP-alpha-D-mannose
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competitive inhibitor
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025 - 0.05
GDP-4-dehydro-6-deoxy-D-mannose
0.027
NADH
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0.028
NADPH
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.72
GDP-mannose
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competitive inhibition
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7
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with NADPH as reductant
8
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with NADH as reductant
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000 - 70000
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gel filtration
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56
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loss of activity in 5 min
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
DTT reduces instability at room temperature from 51% to 35%
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389366
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, half-life: 5 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to homogeneity, fractionation-, chromatography-techniques
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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construction of enzyme deletion mutant DELTArmd. The mutant strain shows highly reduced antimicrobial susceptibility with chloramphenicol, ampicillin or spectinomycin. Structural analysis of lipopolysaccharides in the mutant strain, NMR and mass spectrrometry analysis, overview
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.187)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)