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Information on EC 2.6.1.59 - dTDP-4-amino-4,6-dideoxygalactose transaminase and Organism(s) Escherichia coli and UniProt Accession P27833

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EC Tree
     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.59 dTDP-4-amino-4,6-dideoxygalactose transaminase
IUBMB Comments
A pyridoxal-phosphate protein.
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This record set is specific for:
Escherichia coli
UNIPROT: P27833
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
aminotransferase, thymidine diphosphoaminodideoxygalactose, thymidine diphosphate 4-keto-6-deoxy-D-glucose transaminase, thymidine diphospho-4-keto-6-deoxy-D-glucose glucamic transaminase, thymidine diphospho-4-keto-6-deoxy-D-glucose transaminase, WecE, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminotransferase, thymidine diphosphoaminodideoxygalactose
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-
-
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thymidine diphosphate 4-keto-6-deoxy-D-glucose transaminase
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-
-
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thymidine diphospho-4-keto-6-deoxy-D-glucose glucamic transaminase
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-
-
-
thymidine diphospho-4-keto-6-deoxy-D-glucose transaminase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
dTDP-4,6-dideoxy-D-galactose:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY hide
72560-97-5
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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
dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamate
dTDP-4-amino-4,6-dideoxy-D-galactose + 2-oxoglutarate
show the reaction diagram
-
-
-
?
dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamine
dTDP-4-amino-4,6-dideoxy-D-galactose + 2-oxoglutaramate
show the reaction diagram
65% of the activity with L-glutamate
-
-
?
dTDP-4-dehydro-6-deoxy-D-mannose + L-glutamate
? + 2-oxoglutarate
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(aminooxy)acetic acid
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hydroxylamine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11
dTDP-4-dehydro-6-deoxy-D-glucose
pH 7.5, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.38
dTDP-4-dehydro-6-deoxy-D-glucose
pH 7.5, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.62
dTDP-4-dehydro-6-deoxy-D-glucose
pH 7.5, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
180000
gel filtration
44000
4 * 44000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
4 * 44000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hwang, B.Y.; Lee, H.J.; Yang, Y.H.; Joo, H.S.; Kim, B.G.
Characterization and investigation of substrate specificity of the sugar aminotransferase WecE from E. coli K12
Chem. Biol.
11
915-925
2004
Escherichia coli (P27833)
Manually annotated by BRENDA team