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Information on EC 2.3.1.197 - dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose 3-N-acetyltransferase and Organism(s) Aneurinibacillus thermoaerophilus and UniProt Accession Q6T1W7

for references in articles please use BRENDA:EC2.3.1.197
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IUBMB Comments
The product, dTDP-3-acetamido-3,6-dideoxy-alpha-D-galactose, is a component of the glycan chain of the crystalline bacterial cell surface layer protein (S-layer glycoprotein) of Aneurinibacillus thermoaerophilus.
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This record set is specific for:
Aneurinibacillus thermoaerophilus
UNIPROT: Q6T1W7
The expected taxonomic range for this enzyme is: Aneurinibacillus thermoaerophilus
The taxonomic range for the selected organisms is: Aneurinibacillus thermoaerophilus
Synonyms
dTDP-D-Fucp3N acetylase, FdtC, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dTDP-D-Fucp3N acetylase
293978
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose 3-N-acetyltransferase
The product, dTDP-3-acetamido-3,6-dideoxy-alpha-D-galactose, is a component of the glycan chain of the crystalline bacterial cell surface layer protein (S-layer glycoprotein) of Aneurinibacillus thermoaerophilus.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose
CoA + dTDP-3-acetamido-3,6-dideoxy-alpha-D-galactopyranose
show the reaction diagram
the enzyme is involved in the biosynthesis of dTDP-3-acetamido-3,6-dideoxy-alpha-D-galactose. The reverse reaction cannot be detected
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.061
acetyl-CoA
pH 7.4, 37°C
0.0667
dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose
pH 7.4, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.1
acetyl-CoA
pH 7.4, 37°C
2.3
dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose
pH 7.4, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
50.8
acetyl-CoA
pH 7.4, 37°C
3.4
dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose
pH 7.4, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
FDTC_ANETH
192
0
21003
Swiss-Prot
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
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
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pfoestl, A.; Hofinger, A.; Kosma, P.; Messner, P.
Biosynthesis of dTDP-3-acetamido-3,6-dideoxy-alpha-D-galactose in Aneurinibacillus thermoaerophilus L420-91T
J. Biol. Chem.
278
26410-26417
2003
Aneurinibacillus thermoaerophilus (Q6T1W7)
Manually annotated by BRENDA team
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