Information on EC 2.3.1.B28 - galactosamine-1-phosphate N-acetyltransferase

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The expected taxonomic range for this enzyme is: Sulfolobus tokodaii

EC NUMBER
COMMENTARY hide
2.3.1.B28
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
galactosamine-1-phosphate N-acetyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + alpha-D-galactosamine 1-phosphate = CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
show the reaction diagram
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-
-
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:alpha-D-galactosamine-1-phosphate N-acetyltransferase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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 + alpha-D-galactosamine 1-phosphate
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
show the reaction diagram
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
acetyl-CoA + alpha-D-galactosamine 1-phosphate
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
2 mM, enhances galactosamine-1-phosphate N-acetyltransferase activity 2.1fold
Co2+
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2 mM, enhances galactosamine-1-phosphate N-acetyltransferase activity 1.2fold
Mg2+
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2 mM, enhances galactosamine-1-phosphate N-acetyltransferase activity 1.4fold
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Mn2+
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2 mM, 80% inhibition
Zn2+
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2 mM, 75% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.52 - 1.55
acetyl-CoA
0.66 - 1.71
alpha-D-galactosamine 1-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12.6 - 69.7
alpha-D-galactosamine 1-phosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19.6 - 40.8
alpha-D-galactosamine 1-phosphate
19761
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.23
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pH 7.5, 80°C, mutant enzyme N331A
1.31
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pH 7.5, 80°C, mutant enzyme Y311A
3
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pH 7.5, 80°C, mutant enzyme H308A
25.3
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pH 7.5, 80°C, mutant enzyme K340A
33
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pH 7.5, 80°C, mutant enzyme K337A
38.4
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pH 7.5, 80°C, substrates: acetyl-CoA + alpha-D-galactosamine 1-phosphate
40
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pH 7.5, 80°C, wild-type enzyme enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
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mutant enzyme DC005 shows the same thermostability as wild-type ST0452 protein, whereas mutant enzyme DC011 denatures and becomes insoluble form by 5-min treatment at 80 °C. The C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain BL21-Codon Plus(DE3)-RIL
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H308A
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specific activity is 7.7% compared to the wild-type enzyme
K340A
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specific activity is 63.3% compared to the wild-type enzyme
K377A
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specific activity is 82.6% compared to the wild-type enzyme
N331A
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specific activity is 3.1% compared to the wild-type enzyme
Y311A
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specific activity is 3.3% compared to the wild-type enzyme
additional information
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C-terminal deletion mutants DC005 and DC011 (deletion of the C-terminal 5 or 11 residues of the ST0452 protein) shows 20% and 38% less galactosamine-1-phosphate acetyltransferase activity than the wild-type ST0452 protein. The mutant enzyme DC011 (deletion of the C-terminal 11 residues of the ST0452 protein) shows little thermal stability at 80°C. The C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein. The deletion mutant enzymes DC021, DC031, DC041, DC071 and DC121, are produced in an insoluble form or aggregated immediately after purification. Mutant enzymes DC051 and DC171 can be expressed in a soluble form. Mutant enzyme DC051 becomes completely insoluble after 5 min treatment at 60°C, while mutant enzyme DC171 is insoluble after 5 min treatment at 70 °C