Information on EC 2.6.1.33 - dTDP-4-amino-4,6-dideoxy-D-glucose transaminase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.6.1.33
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RECOMMENDED NAME
GeneOntology No.
dTDP-4-amino-4,6-dideoxy-D-glucose transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dTDP-4-amino-4,6-dideoxy-alpha-D-glucose + 2-oxoglutarate = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + L-glutamate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
dTDP-D-desosamine biosynthesis
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dTDP-N-acetylviosamine biosynthesis
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Polyketide sugar unit biosynthesis
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Acarbose and validamycin biosynthesis
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
dTDP-4-amino-4,6-dideoxy-D-glucose:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-19-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain K12, gene WecC
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Manually annotated by BRENDA team
strain O7
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Manually annotated by BRENDA team
strain type 7
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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-dehydro-6-deoxy-alpha-D-glucopyranose + L-glutamate
dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose + 2-oxoglutarate
show the reaction diagram
dTDP-4-dehydro-6-deoxy-D-glucose + glycine
dTDP-4-amino-4,6-dideoxy-D-galactose + glyoxylate
show the reaction diagram
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L-glycine, poor amino donor
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-
?
dTDP-4-dehydro-6-deoxy-D-glucose + L-alanine
dTDP-4-amino-4,6-dideoxy-D-galactose + pyruvate
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-glutamate
dTDP-4-amino-4,6-dideoxy-D-glucose + 2-oxoglutarate
show the reaction diagram
dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamine
dTDP-4-amino-4,6-dideoxy-D-galactose + 2-oxoglutamine
show the reaction diagram
dTDP-4-dehydro-6-deoxy-D-mannose + L-glutamate
dTDP-4-amino-6-deoxy-D-mannose + 2-oxoglutarate
show the reaction diagram
additional information
?
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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
dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose + L-glutamate
dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose + 2-oxoglutarate
show the reaction diagram
Q9ZGH0
the enzyme is involved in biosynthesis of desosamine
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?
dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamate
dTDP-4-amino-4,6-dideoxy-D-glucose + 2-oxoglutarate
show the reaction diagram
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(aminooxy)acetic acid
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complete inhibition by a mixture of hydroxylamine, (aminooxy)acetic acid, and gabaculine as inhibitors specific for pyridoxal 5'-phosphate-dependent enzymes
gabaculine
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complete inhibition by a mixture of hydroxylamine, (aminooxy)acetic acid, and gabaculine as inhibitors specific for pyridoxal 5'-phosphate-dependent enzymes
hydroxylamine
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complete inhibition by a mixture of hydroxylamine, (aminooxy)acetic acid, and gabaculine as inhibitors specific for pyridoxal 5'-phosphate-dependent enzymes
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.22
2-oxoglutarate
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38C, pH 7.0-7.6
0.0458 - 0.98
dTDP-4-dehydro-6-deoxy-D-glucose
5.1
L-glutamate
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38C, pH 7.0-7.6
0.032
TDP-4-amino-4,6-dideoxy-D-glucose
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38C, pH 7.0-7.6
0.14
TDP-4-keto-6-deoxy-D-glucose
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38C, pH 7.0-7.6
additional information
additional information
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kinetics in a coupled assay
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.74 - 5.66
dTDP-4-dehydro-6-deoxy-D-glucose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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activity measurement in a coupled assay with NADH-dependent L-GDH
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9.5
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enzyme shows over 80% of maximal activity at pH 6.0 and pH 8.0, and very low activity below pH 5.0 and above pH 9.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38
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assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 45
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25% of maximal activity at 45C
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
180000
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recombinant His6-tagged enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
each subunit of the dimeric enzyme contains 12 alpha-helices and 14 alpha-strands
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop method of vapor diffusion. The structure of DesI is solved in complex with its product, dTDP-4-amino-4,6-dideoxyglucose, to a nominal resolution of 2.1 A. Each subunit of the dimeric enzyme contains 12 alpha-helices and 14 alpha-strands. Crystals belong to the space group P2(1)2(1)2(1) with unit cell dimensions of 59.5 A, 66.8 A, 242.0 A and one dimer per asymmetric unit. Crystal dimensions are typically 1 mm * 0.6 mm * 0.2 mm
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0C or -15C, partially purified enzyme, stable for several weeks
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0C, crude cell extract, stable for several days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial from strain B, 28fold
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recombinant C-terminally His6-tagged enzyme from strain BL21(DE3) by nickel chelate and hydrophobic interaction chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression with His-tag
gene WecC, amino acid sequence determination and analysis, overexpression of C-terminally His6-tagged enzyme in strain BL21(DE3), phylogenetic analysis
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