Information on EC 1.1.1.134 - dTDP-6-deoxy-L-talose 4-dehydrogenase (NADP+)

for references in articles please use BRENDA:EC1.1.1.134
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The expected taxonomic range for this enzyme is: Escherichia coli

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EC NUMBER
COMMENTARY hide
1.1.1.134
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RECOMMENDED NAME
GeneOntology No.
dTDP-6-deoxy-L-talose 4-dehydrogenase (NADP+)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dTDP-6-deoxy-beta-L-talose + NADP+ = dTDP-4-dehydro-beta-L-rhamnose + NADPH + H+
show the reaction diagram
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
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-
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SYSTEMATIC NAME
IUBMB Comments
dTDP-6-deoxy-beta-L-talose:NADP+ 4-oxidoreductase
Oxidation on the 4-position of the hexose moiety takes place only while the substrate is bound to another enzyme that catalyses epimerization at C-3 and C-5.
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CAS REGISTRY NUMBER
COMMENTARY hide
37250-65-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
045
-
-
Manually annotated by BRENDA team
045
-
-
Manually annotated by BRENDA team
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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
TDP-6-deoxy-D-xylo-4-hexosulose + NADPH
TDP-6-deoxy-L-talose + NADP+
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
TDP-6-deoxy-D-xylo-4-hexosulose + NADPH
TDP-6-deoxy-L-talose + NADP+
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
-
cofactor
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.134)
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)