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Information on EC 2.6.1.33 - dTDP-4-amino-4,6-dideoxy-D-glucose transaminase
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2.6.1.33 dTDP-4-amino-4,6-dideoxy-D-glucose transaminaseIUBMB Comments
A pyridoxal-phosphate protein.
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Word Map
- 2.6.1.33
- pyridoxal
-
aldimine
- 5'-phosphate
- aeruginosa
-
plp-dependent
-
o-antigen
- amine
-
phosphate-dependent
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
Synonyms
sugar aminotransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminotransferase, thymidine diphospho-4-amino-4,6-dideoxyglucose
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-
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TDP-4-keto-6-deoxy-D-glucose transaminase
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-
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thymidine diphospho-4-amino-4,6-dideoxyglucose aminotransferase
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-
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thymidine diphospho-4-amino-6-deoxyglucose aminotransferase
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thymidine diphospho-4-keto-6-deoxy-D-glucose transaminase
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thymidine diphospho-4-keto-6-deoxy-D-glucose-glutamic transaminase
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-
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VioA
WecE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dTDP-4-amino-4,6-dideoxy-alpha-D-glucose + 2-oxoglutarate = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + L-glutamate
dTDP-4-amino-4,6-dideoxy-alpha-D-glucose + 2-oxoglutarate = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + L-glutamate
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-
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dTDP-4-amino-4,6-dideoxy-alpha-D-glucose + 2-oxoglutarate = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + L-glutamate
substrate specificity might be related to conserved motifs VLalpha, VLbeta, and VLgamma, around the active site
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
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-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
dTDP-4-amino-4,6-dideoxy-D-glucose:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein.
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CAS REGISTRY NUMBER
COMMENTARY
9023-19-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
dTDP-4-dehydro-6-deoxy-D-glucose + glycine
dTDP-4-amino-4,6-dideoxy-D-galactose + glyoxylate
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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
dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamate
dTDP-4-amino-4,6-dideoxy-D-galactose + 2-oxoglutarate
dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamate
dTDP-4-amino-4,6-dideoxy-D-glucose + 2-oxoglutarate
dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamine
dTDP-4-amino-4,6-dideoxy-D-galactose + 2-oxoglutamine
dTDP-4-dehydro-6-deoxy-D-mannose + L-glutamate
dTDP-4-amino-6-deoxy-D-mannose + 2-oxoglutarate
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-
-
-
?
TDP-4-amino-4,6-dideoxy-alpha-D-glucose + 2-oxoglutarate
TDP-4-dehydro-6-deoxy-alpha-D-glucose + L-glutamate
dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose + L-glutamate
dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose + 2-oxoglutarate
the enzyme is involved in biosynthesis of desosamine
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-
?
dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose + L-glutamate
dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose + 2-oxoglutarate
the two active sites of the enzyme are located in clefts at the subunit/subunit interface. Electron density corresponding to the bound product demonstrates a covalent bond between the amino group of the product and C-4' of the pyridoxal 5'-phosphate cofactor
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-
?
dTDP-4-dehydro-6-deoxy-D-glucose + L-alanine
dTDP-4-amino-4,6-dideoxy-D-galactose + pyruvate
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L-alanine, 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
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L-alanine, 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
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L-alanine, poor amino donor
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-
?
dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamate
dTDP-4-amino-4,6-dideoxy-D-galactose + 2-oxoglutarate
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-
-
-
?
dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamate
dTDP-4-amino-4,6-dideoxy-D-galactose + 2-oxoglutarate
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co-substrate L-glutamate, 85.5% conversion rate
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-
?
dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamate
dTDP-4-amino-4,6-dideoxy-D-galactose + 2-oxoglutarate
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co-substrate L-glutamate, 85.5% conversion rate
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-
?
dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamate
dTDP-4-amino-4,6-dideoxy-D-galactose + 2-oxoglutarate
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co-substrate L-glutamate, 84.9% conversion rate
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-
?
dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamate
dTDP-4-amino-4,6-dideoxy-D-glucose + 2-oxoglutarate
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-
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r
dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamate
dTDP-4-amino-4,6-dideoxy-D-glucose + 2-oxoglutarate
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specific for the substrates
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r
dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamate
dTDP-4-amino-4,6-dideoxy-D-glucose + 2-oxoglutarate
Escherichia coli B / ATCC 11303
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-
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r
dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamate
dTDP-4-amino-4,6-dideoxy-D-glucose + 2-oxoglutarate
Escherichia coli B / ATCC 11303
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specific for the substrates
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r
dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamine
dTDP-4-amino-4,6-dideoxy-D-galactose + 2-oxoglutamine
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co-substrate L-glutamine, 15.9% conversion rate
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-
?
dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamine
dTDP-4-amino-4,6-dideoxy-D-galactose + 2-oxoglutamine
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co-substrate L-glutamine, 15.9% conversion rate
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-
?
dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamine
dTDP-4-amino-4,6-dideoxy-D-galactose + 2-oxoglutamine
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co-substrate L-glutamine, 74.1% conversion rate
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?
TDP-4-amino-4,6-dideoxy-alpha-D-glucose + 2-oxoglutarate
TDP-4-dehydro-6-deoxy-alpha-D-glucose + L-glutamate
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?
TDP-4-amino-4,6-dideoxy-alpha-D-glucose + 2-oxoglutarate
TDP-4-dehydro-6-deoxy-alpha-D-glucose + L-glutamate
Escherichia coli B / ATCC 11303
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?
additional information
?
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DL-glutamine, L-glutamine, D-glutamate, L-asparagine, DL-aspartate and L-alanine are inactive as amino donor, TDP-4-amino-4,6-dideoxy-D-galactose is inactive in the reverse reaction, neither pyruvate nor oxaloacetate can replace 2-oxoglutarate
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?
additional information
?
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no activity with dGDP-4-keto-6-deoxy-D-mannose, the nucleotide moiety is a key determinant for acceptor substrate specificity
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?
additional information
?
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Escherichia coli B / ATCC 11303
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DL-glutamine, L-glutamine, D-glutamate, L-asparagine, DL-aspartate and L-alanine are inactive as amino donor, TDP-4-amino-4,6-dideoxy-D-galactose is inactive in the reverse reaction, neither pyruvate nor oxaloacetate can replace 2-oxoglutarate
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
the enzyme is involved in biosynthesis of desosamine
-
-
?
dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamate
dTDP-4-amino-4,6-dideoxy-D-glucose + 2-oxoglutarate
dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamate
dTDP-4-amino-4,6-dideoxy-D-glucose + 2-oxoglutarate
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-
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r
dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamate
dTDP-4-amino-4,6-dideoxy-D-glucose + 2-oxoglutarate
Escherichia coli B / ATCC 11303
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-
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r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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absolute requirement, Km is 0.00003 mM in reverse reaction, 0.00012 mM in forward reaction
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
activity measurement in a coupled assay with NADH-dependent L-GDH
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Show AA Sequence and Transmembrane Helices (258 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
44000
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4 * 44000, recombinant His6-tagged enzyme, SDS-PAGE, 4 * 44452, recombinant His6-tagged enzyme, nucleotide sequence calculation, 4 * 44465, recombinant His6-tagged enzyme, MALDI-TOF mass spectrometry
44452
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4 * 44000, recombinant His6-tagged enzyme, SDS-PAGE, 4 * 44452, recombinant His6-tagged enzyme, nucleotide sequence calculation, 4 * 44465, recombinant His6-tagged enzyme, MALDI-TOF mass spectrometry
44465
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4 * 44000, recombinant His6-tagged enzyme, SDS-PAGE, 4 * 44452, recombinant His6-tagged enzyme, nucleotide sequence calculation, 4 * 44465, recombinant His6-tagged enzyme, MALDI-TOF mass spectrometry
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
each subunit of the dimeric enzyme contains 12 alpha-helices and 14 alpha-strands
tetramer
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4 * 44000, recombinant His6-tagged enzyme, SDS-PAGE, 4 * 44452, recombinant His6-tagged enzyme, nucleotide sequence calculation, 4 * 44465, recombinant His6-tagged enzyme, MALDI-TOF mass spectrometry
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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
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
engineering of Escherichia coli to divert the flow of carbon flux from glucose-1-phosphate to thymidine diphosphate 4-keto 4,6-dideoxy-D-glucose (dTKDG), an intermediate of various dTDP-sugars. Glucose phosphate isomerase, glucose-6-phosphate dehydrogenase and uridylyltransferase genes are deleted while dTDP-D-glucose synthase and dTDP-Dglucose 4,6-dehydratase are overexpressed to produce a pool of dTKDG in the cell cytosol. The flow of dTKDG is further diverted to dTDP-D-viosamine, dTDP 4-amino 4,6-dideoxy-D-galactose, and dTDP 3-amino 3,6-dideoxy-D-galactose sugars using sugar aminotransferases gerB, wecE, and fdtB, respectively, from different sources. These sugar moieties are transferred to the 3-hydroxyl position of quercetin and kaempferol with the help of Arabidopsis thaliana glycosyltransferase ArGT3
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Matsuhashi, M.; Strominger, J.L.
Thymidine diphosphate 4-acetamido-2,6-dideoxyhexoses. 3. Purification and properties of thymidine diphosphate 4-keto-6-deoxy-D-glucose transaminase from Escherichia coli strain B
J. Biol. Chem.
241
4738-4744
1966
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
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
brenda
Wang, Y.; Xu, Y.; Perepelov, A.V.; Qi, Y.; Knirel, Y.A.; Wang, L.; Feng, L.
Biochemical characterization of dTDP-D-Qui4N and dTDP-D-Qui4NAc biosynthetic pathways in Shigella dysenteriae type 7 and Escherichia coli O7
J. Bacteriol.
189
8626-8635
2007
Escherichia coli, Shigella dysenteriae, Escherichia coli O7
brenda
Burgie, E.S.; Holden, H.M.
Molecular architecture of DesI: a key enzyme in the biosynthesis of desosamine
Biochemistry
46
8999-9006
2007
Streptomyces venezuelae (Q9ZGH0)
brenda
Pandey, R.; Parajuli, P.; Chu, L.; Darsandhari, S.; Sohng, J.
Biosynthesis of amino deoxy-sugar-conjugated flavonol glycosides by engineered Escherichia coli
Biochem. Eng. J.
101
191-199
2015
Escherichia coli (P27833)
-
brenda
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Release 2023.1 (January 2023)
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