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
Biosynthesis of antibiotics
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dTDP-3-acetamido-alpha-D-fucose 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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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
pyridoxal 5'-phosphate
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additional information
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enzyme utilizes an oxidized quinone as co-factor
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41710
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2 * 41710, SDS-PAGE
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 4°C or -20°C and supplemented with 50% glycerol
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, the concentrated enzyme preparations are stable at 4°C for several months with only a marginal decrease of enzyme activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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overexpression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
Show AA Sequence (108 entries)
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