Information on EC 2.6.1.59 - dTDP-4-amino-4,6-dideoxygalactose transaminase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.6.1.59
-
RECOMMENDED NAME
GeneOntology No.
dTDP-4-amino-4,6-dideoxygalactose transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dTDP-4-amino-4,6-dideoxy-alpha-D-galactose + 2-oxoglutarate = dTDP-4-dehydro-6-deoxy-alpha-D-galactose + L-glutamate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
dTDP-N-acetylthomosamine biosynthesis
-
-
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
type VO
-
-
Manually annotated by BRENDA team
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-amino-4,6-dideoxy-D-galactose + 2-oxoglutarate
dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamate
show the reaction diagram
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
-
-
-
?
TDP-4-dehydro-6-deoxy-D-glucose + L-glutamate
TDP-4-amino-4,6-dideoxy-D-galactose + 2-oxoglutarate
show the reaction diagram
additional information
?
-
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-4-amino-4,6-dideoxy-D-galactose + 2-oxoglutarate
dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(aminooxy)acetic acid
-
hydroxylamine
-
L-cysteine
-
strong
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Maleate
-
stabilizing effect
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.22
2-oxoglutarate
-
pH 7.0, 38C
0.11
dTDP-4-dehydro-6-deoxy-D-glucose
pH 7.5, 25C
7.9
L-glutamate
-
pH 7.0, 38C
0.16
TDP-4-amino-4,6-dideoxy-D-galactose
-
pH 7.0, 38C
1
TDP-4-keto-6-deoxy-D-glucose
-
pH 7.0, 38C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.38
dTDP-4-dehydro-6-deoxy-D-glucose
Escherichia coli
P27833
pH 7.5, 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.62
dTDP-4-dehydro-6-deoxy-D-glucose
Escherichia coli
P27833
pH 7.5, 25C
3071
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.01
-
pH 7.0, 38C
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
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44000
4 * 44000, SDS-PAGE
180000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
4 * 44000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
-
10 min: 7% remaining activity, 72% remaining activity with addition of pyridoxal 5'-phosphate, 86% remaining activity with addition of pyridoxal 5'-phosphate and potassium maleate
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
crude extract and partially purified enzyme are unstable, necessity of addition of pyridoxal phosphate during purification
-
maleate enhances stabilizing effect of pyridoxal phosphate
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0C or -15C, purified enzyme, stable for several weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21
Show AA Sequence (816 entries)
Please use the Sequence Search for a specific query.