Information on EC 1.1.1.342 - CDP-paratose synthase

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The expected taxonomic range for this enzyme is: Salmonella enterica subsp. enterica serovar Typhi

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EC NUMBER
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1.1.1.342
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RECOMMENDED NAME
GeneOntology No.
CDP-paratose synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
CDP-alpha-D-paratose + NADP+ = CDP-4-dehydro-3,6-dideoxy-alpha-D-glucose + NADPH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
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CDP-paratose biosynthesis
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CDP-tyvelose biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
CDP-alpha-D-paratose:NADP+ 4-oxidoreductase
The enzyme is involved in synthesis of paratose and tyvelose, unusual 3,6-dideoxyhexose sugars that form part of the O-antigen in the lipopolysaccharides of several enteric bacteria. Isolated from Salmonella enterica subsp. enterica serovar Typhi (Salmonella typhi).
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
Salmonella serogroup polymorphism based on abequose and paratose arose by divergence from an ancestral gene to give abequose and paratose synthase in different strains or species, and this happened in a bacterial group with low G+C content. Later a recombination event brought either paratose synthase gene rfbS or abeqouse synthase gene rJbJ into the genetic background of the other. These events were followed by one form being picked up by a Salmonella strain and becoming adapted to put a dideoxyhexose into its own 0-antigen
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
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LITERATURE
(Substrate)
COMMENTARY
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LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CDP-4-dehydro-3,6-dideoxy-alpha-D-glucose + NADPH + H+
CDP-alpha-D-paratose + NADP+
show the reaction diagram
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conversion is almost quantitative
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additional information
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enzyme catalyzes the stereospecific hydride transfer of the pro-S hydrogen from the C-4' position of the reduced coenzyme to C-4 of the substrate, CDP-3,6-dideoxy-D-glycero-D-glycero-4-hexulose. The overall equilibrium of this catalysis greatly favors the formation of the reduced sugar product and the oxidized coenzyme
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
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NADPH is 10fold prefered over NADH
NADPH
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NADPH is 10fold prefered over NADH. Enzyme exhibits a high affinity for NADPH with a much smaller dissociation constant of 0.005microM compared to the Km of 0.26 mM
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adenosine triphosphate ribose
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competitive inhibitor with respect to NADPH and either an uncompetitive or a mixed type inhibitor with respect to CDP-3,6-dideoxy-D-glycero-D-glycero-4-hexulose
CDP
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competitive inhibitor with respect to CDP-3,6-dideoxy-D-glycero-D-glycero-4-hexulose and either an uncompetitive or a mixed type inhibitor with respect to NADPH
CDP-paratose
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competitive inhibitor against CDP-3,6-dideoxy-D-glycero-D-glycero-4-hexulose and mixed type or uncompetitive inhibitor with respect to NADPH
NADP+
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mixed type or uncompetitive inhibitor with respect to CDP-3,6-dideoxy-D-glycero-D-glycero-4-hexulose and competitive inhibitor for NADPH
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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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
7
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buffer 0.2 M potassium phosphate
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
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2 * 29000, SDS-PAGE, 2 * 31501, calculated
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 29000, SDS-PAGE, 2 * 31501, calculated
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is very unstable at low protein concentration
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, stable for at least 1 year
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.342)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)