Information on EC 2.6.1.90 - dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose transaminase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.6.1.90
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RECOMMENDED NAME
GeneOntology No.
dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose transaminase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose + 2-oxoglutarate = dTDP-3-dehydro-6-deoxy-alpha-D-galactopyranose + L-glutamate
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
dTDP-3-acetamido-alpha-D-fucos biosynthesis
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dTDP-D-ravidosamine and dTDP-4-acetyl-D-ravidosamine biosynthesis
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Polyketide sugar unit biosynthesis
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein. The enzyme is involved in the biosynthesis of dTDP-3-acetamido-3,6-dideoxy-alpha-D-galactose. The reaction occurs in the reverse direction.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dTDP-3-dehydro-6-deoxy-alpha-D-galactopyranose + L-glutamate
dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose + 2-oxoglutarate
show the reaction diagram
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
dTDP-3-dehydro-6-deoxy-alpha-D-galactopyranose + L-glutamate
dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose + 2-oxoglutarate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
metal ions are not required
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 55
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 41710, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
to increase the stability, the enzyme is concentrated by ultrafiltration before storage at 4C or -20C and supplemented with 50% glycerol
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, the concentrated enzyme preparations are stable at 4C for several months with only a marginal decrease of enzyme activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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overexpression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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synthesis of TDP-D-ravidosamine, necessary for future in vitro glycosylation assays. TDP-D-ravidosamine is the anticipated sugar donor substrate of RavGT (the glycosyltransferase that links D-ravidosamine to the polyketide derived backbone defuco-gilvocarcin V). Defuco-gilvocarcin V exhibits superior anticancer/antibacterial activities