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Information on EC 2.3.1.157 - glucosamine-1-phosphate N-acetyltransferase and Organism(s) Sulfurisphaera tokodaii and UniProt Accession Q975F9
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2.3.1.157 glucosamine-1-phosphate N-acetyltransferaseIUBMB Comments
The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase.
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Word Map
- 2.3.1.157
- peptidoglycan
- utp
- drug development
- tokodaii
- glucosamine-6-phosphate
-
left-hand
- udp-sugars
- glmm
-
nucleotidylyltransferase
- utase
-
diphosphate-n-acetylglucosamine
- medicine
The taxonomic range for the selected organisms is: Sulfurisphaera tokodaii
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
n-acetylglucosamine-1-phosphate uridyltransferase, st0452 protein, udp-glcnac pyrophosphorylase, glmu acetyltransferase, glmu enzyme, st0452, glucosamine-1-phosphate acetyltransferase, glmu uridyltransferase, glcnac-1-p uridyltransferase, glcn-1-p actase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
the multifunctional enzyme from Sulfolobus tokodaii {7} is also active with acetyl-CoA + alpha-D-galactosamine 1-phosphate (galactosamine-1-phosphate N-acetyltransferase), UTP + N-acetylglucosamine 1-phosphate (EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase) and UTP + N-acetyl-alpha-D-galactosamine 1-phosphate (EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase)
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:alpha-D-glucosamine-1-phosphate N-acetyltransferase
The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase.
CAS REGISTRY NUMBER
COMMENTARY
9023-06-7
-
9031-91-8
-
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
acetyl-CoA + alpha-D-galactosamine 1-phosphate
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
because the ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
no activity with alpha-D-glucosamine 6-phosphate. The multifunctional enzyme is also active with acetyl-CoA + alpha-D-galactosamine 1-phosphate (galactosamine-1-phosphate N-acetyltransferase), UTP + N-acetylglucosamine 1-phosphate (EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase) and UTP + N-acetyl-alpha-D-galactosamine 1-phosphate (EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase)
-
-
?
additional information
?
-
the enzyme has multiple sugar-1-phosphate nucleotidylyltransferase, EC 2.7.7.37, and amino-sugar-1-phosphate acetyltransferase, EC 2.3.1.157, activities, overview. In addition to glucosamine-1-phosphate acetyltransferase activity, it possesses unique galactosamine-1-phosphate acetyltransferase activity. Also, the enzyme possesses GlcNAc-1-phosphate nucleotidylyltransferase, EC 2.7.7.23, and N-acetyl-D-galactosamine-1-phosphate uridyltransferase, EC 2.7.7.83, activities, as well as the expected glucose-1-phosphate thymidylyltransferase, EC 2.7.7.24, activity. The ST0452 protein can catalyze the acetylation of both GlcN-1-P and GalN-1-P, while GalN-1-P AcTase activity is not detected in bacterial enzymes
-
-
?
additional information
?
-
-
the enzyme has multiple sugar-1-phosphate nucleotidylyltransferase, EC 2.7.7.37, and amino-sugar-1-phosphate acetyltransferase, EC 2.3.1.157, activities, overview. In addition to glucosamine-1-phosphate acetyltransferase activity, it possesses unique galactosamine-1-phosphate acetyltransferase activity. Also, the enzyme possesses GlcNAc-1-phosphate nucleotidylyltransferase, EC 2.7.7.23, and N-acetyl-D-galactosamine-1-phosphate uridyltransferase, EC 2.7.7.83, activities, as well as the expected glucose-1-phosphate thymidylyltransferase, EC 2.7.7.24, activity. The ST0452 protein can catalyze the acetylation of both GlcN-1-P and GalN-1-P, while GalN-1-P AcTase activity is not detected in bacterial enzymes
-
-
?
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
acetyl-CoA + alpha-D-galactosamine 1-phosphate
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
because the ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ca2+
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
Co2+
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
Mg2+
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
Mn2+
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
Zn2+
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
additional information
residues Tyr311, Lys337 and Lys340 plus C-terminal 11-residue region of the ST0452 protein enhance its GalN-1-P AcTase activity and suppress its GlcN-1-P AcTase activity, this function might be lost in bacterial enzymes
-
additional information
-
residues Tyr311, Lys337 and Lys340 plus C-terminal 11-residue region of the ST0452 protein enhance its GalN-1-P AcTase activity and suppress its GlcN-1-P AcTase activity, this function might be lost in bacterial enzymes
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.52
acetyl-CoA
pH 7.5, 80°C, mutant enzyme DC005 with a deletion of the C-terminal 5 residues of the ST0452 protein
0.52
acetyl-CoA
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein
1.55
acetyl-CoA
pH 7.5, 80°C, mutant enzyme DC011 with a deletion of the C-terminal 11 residues of the ST0452 protein
1.55
acetyl-CoA
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein
0.66
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein
0.84
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein
1.71
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, wild-type ST0452 protein
0.56
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, mutant enzyme DC005 with a deletion of the C-terminal 5 residues of the ST0452 protein
0.56
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein
0.59
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, wild-type enzyme
0.59
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, wild-type ST0452 protein
1.69
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, mutant enzyme DC011 with a deletion of the C-terminal 11 residues of the ST0452 protein
1.69
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
12.6
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein
17.9
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein
69.7
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, wild-type ST0452 protein
123.2
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, wild-type enzyme
123.2
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, wild-type ST0452 protein
490.6
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, mutant enzyme DC005 with a deletion of the C-terminal 5 residues of the ST0452 protein
490.6
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein
2311
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, mutant enzyme DC011 with a deletion of the C-terminal 11 residues of the ST0452 protein
2311
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
19.6
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein
21.5
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein
40.8
alpha-D-galactosamine 1-phosphate
pH 7.5, 80°C, wild-type ST0452 protein
211
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, wild-type enzyme
211
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, wild-type ST0452 protein
869.2
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, mutant enzyme DC005 with a deletion of the C-terminal 5 residues of the ST0452 protein
869.2
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein
1489
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, mutant enzyme DC011 with a deletion of the C-terminal 11 residues of the ST0452 protein
1489
alpha-D-glucosamine 1-phosphate
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1131
alpha-D-glucosamine 1-phosphate aubstrate, pH 7.5, 80°C, recombinant mutant D011 protein
29.6
alpha-D-galactosamine 1-phosphate aubstrate, pH 7.5, 80°C, recombinant mutant D011 protein
3 - 8
alpha-D-galactosamine 1-phosphate substrate, pH 7.5, 80°C, recombinant mutant D005 protein
323.5
alpha-D-glucosamine 1-phosphate substrate, pH 7.5, 80°C, recombinant mutant D005 protein
47.6
alpha-D-galactosamine 1-phosphate aubstrate, pH 7.5, 80°C, recombinant wild-type ST0452 protein
67.4
alpha-D-glucosamine 1-phosphate substrate, pH 7.5, 80°C, recombinant wild-type ST0452 protein
75.34
pH 7.5, 80°C, substrates: acetyl-CoA + alpha-D-glucosamine 1-phosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
physiological function
because the ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
physiological function
the archaeal enzyme's high GalN-1-P AcTase activity, which is not detected on the bacterial and eukaryotic similar enzymes, supports the production of the UDP-GalNAc in archaeal cells
additional information
the C-terminal tail region of the ST0452 protein might be important for recognition of the multiple substrates for amino-sugar-1-P AcTase activity. The ST0452 protein contains only two Cys residues, it is unlikely that Cys-Cys bonds contribute to its thermostability. Residue Asn331 in the ST0452 protein is essential for the GalN-1-P AcTase activity, but it is much less important and not essential for the GlcN-1-P AcTase activity. The C-terminal residues of the ST0452 protein enhance the turnover rate of its GalN-1-P AcTase catalytic activity and slightly suppress substrate binding. Residue H308 is essential for both amino-sugar-1-P AcTase activities of the ST0452 protein
additional information
-
the C-terminal tail region of the ST0452 protein might be important for recognition of the multiple substrates for amino-sugar-1-P AcTase activity. The ST0452 protein contains only two Cys residues, it is unlikely that Cys-Cys bonds contribute to its thermostability. Residue Asn331 in the ST0452 protein is essential for the GalN-1-P AcTase activity, but it is much less important and not essential for the GlcN-1-P AcTase activity. The C-terminal residues of the ST0452 protein enhance the turnover rate of its GalN-1-P AcTase catalytic activity and slightly suppress substrate binding. Residue H308 is essential for both amino-sugar-1-P AcTase activities of the ST0452 protein
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
trimer
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
additional information
additional information
the enzyme contains the the N-terminal nucleotidylyltransferase domain (residues 1210) and the C-terminal acetyltransferase domain (residues 211401), respectively. Comparisons of the crystal structures of the ST0452 protein, PDB ID GGO, and Escherichia coli protein EcGlmU2, PDB ID 2OI5, comparison with ST0452 mutant enzymes, overview. Despite the structural similarities between the N- and C-termini of the ST0452 protein and those of Escherichia coli EcGlmU, the thermostabilities of the two proteins differ greatly, as EcGlmU is a mesophilic enzyme. The structures of these proteins do not correlate directly with their thermostability. The distance between the GlcN-1-P AcTase and GlcNAc-1-P UTase catalytic centers is smaller in the ST0452 protein than the mesophilic bacterial GlmU
additional information
-
the enzyme contains the the N-terminal nucleotidylyltransferase domain (residues 1210) and the C-terminal acetyltransferase domain (residues 211401), respectively. Comparisons of the crystal structures of the ST0452 protein, PDB ID GGO, and Escherichia coli protein EcGlmU2, PDB ID 2OI5, comparison with ST0452 mutant enzymes, overview. Despite the structural similarities between the N- and C-termini of the ST0452 protein and those of Escherichia coli EcGlmU, the thermostabilities of the two proteins differ greatly, as EcGlmU is a mesophilic enzyme. The structures of these proteins do not correlate directly with their thermostability. The distance between the GlcN-1-P AcTase and GlcNAc-1-P UTase catalytic centers is smaller in the ST0452 protein than the mesophilic bacterial GlmU
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method at 22°C, crystallization of the Y97N protein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H308A
K337A
site-directed mutagenesis, the mutant enzyme shows slightly decreasing GalN-1-P AcTase activity and slightly increasing GlcN-1-P AcTase activity compared to the wild-type enzyme. The mutant shows 82.6% and 137.7% of wild-type GalN-1-P AcTase and GlcN-1-P AcTase activity, respetively
K340A
K377A
specific activity is 137.7% compared to the wild-type enzyme
N331A
T80S/Y97N
the mutant enzyme shows 6.5times-higher activity, compared to that of the wild-type ST0452 protein, revealing that these two substituted residues function cooperatively to increase N-acetylglucosamine-1-phosphate uridyltransferase activity
Y311A
Y97A
mutant enzyme exhibits the highest activity of the single-mutant proteins
Y97N
the mutant enzyme exhibits over 4 times higher N-acetylglucosamine-1-phosphate uridyltransferase activity, compared with that of the wild-type ST0452 protein. The three-dimensional structure of the Y97N protein is not changed by this substitution but the interactions with the substrate are slightly modified, which might cause the activity to increase. The crystal structure of the Y97N protein shows that positions 146 (Glu) and 80 (Thr) form interactions with GlcNAc, and an engineering strategy is applied to these residues to increase activity
additional information
H308A
specific activity is 0.7% compared to the wild-type enzyme
H308A
site-directed mutagenesis, the mutation diminishes both amino-sugar-1-P AcTase activities of the ST0452 protein. The mutant shows 7.7% and 0.7% of wild-type GalN-1-P AcTase and GlcN-1-P AcTase activity, respetively
K340A
specific activity is 147.1% compared to the wild-type enzyme
K340A
site-directed mutagenesis, the mutant enzyme shows moderately decreasing GalN-1-P AcTase activity and moderately increasing GlcN-1-P AcTase activity compared to the wild-type enzyme. The mutant shows 63.3% and 147.1% of wild-type GalN-1-P AcTase and GlcN-1-P AcTase activity, respetively
N331A
specific activity is 46.1% compared to the wild-type enzyme
N331A
site-directed mutagenesis, the mutant enzyme shows highly decreasing GalN-1-P AcTase activity and decreasing GlcN-1-P AcTase activity compared to the wild-type enzyme. The mutant shows 3.1% and 46.1% of wild-type GalN-1-P AcTase and GlcN-1-P AcTase activity, respetively
Y311A
specific activity is 118.4% compared to the wild-type enzyme
Y311A
site-directed mutagenesis, the mutant enzyme shows highly decreasing GalN-1-P AcTase activity and increasing GlcN-1-P AcTase activity compared to the wild-type enzyme. The mutant shows 3.3% and 118.4% of wild-type GalN-1-P AcTase and GlcN-1-P AcTase activity, respetively
additional information
glucosamine-1-phosphate acetyltransferase activity of C-terminal deletion mutants DC005 and DC011 (deletion of the C-terminal 5 or 11 residues of the ST0452 protein) are respectively, 4.8 and 16.8 times higher than that of 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
additional information
-
glucosamine-1-phosphate acetyltransferase activity of C-terminal deletion mutants DC005 and DC011 (deletion of the C-terminal 5 or 11 residues of the ST0452 protein) are respectively, 4.8 and 16.8 times higher than that of 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
additional information
construction of expression vectors encoding a series of ST0452 C-terminal deletion mutants with hexahistidine tags at their C-termini, designated pST0452(DC005)H, pST0452(DC011)H, pST0452(DC021)H, pST0452(DC031)H, pST0452(DC041) H, pST0452(DC051)H, pST0452(DC071)H, pST0452 (DC121)H and pST0452(DC171)H. The deletion mutants retain the same tertiary structures as the wild-type ST0452 protein, but some show an altered thermostability, overview
additional information
-
construction of expression vectors encoding a series of ST0452 C-terminal deletion mutants with hexahistidine tags at their C-termini, designated pST0452(DC005)H, pST0452(DC011)H, pST0452(DC021)H, pST0452(DC031)H, pST0452(DC041) H, pST0452(DC051)H, pST0452(DC071)H, pST0452 (DC121)H and pST0452(DC171)H. The deletion mutants retain the same tertiary structures as the wild-type ST0452 protein, but some show an altered thermostability, overview
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
mutant enzyme DC005 shows the same thermostability as wild-type ST0452 protein, whereas mutant enzyme DC011 denatures and becomes insoluble 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
gene ST0452, recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21-Codon Plus(DE3)-RIL
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the increase in activity induced by some substitutions and truncations may be a useful feature that can be exploited for commercial application of this enzyme
additional information
-
the increase in activity induced by some substitutions and truncations may be a useful feature that can be exploited for commercial application of this enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhang, Z.; Akutsu, J.; Kawarabayasi, Y.
Identification of novel acetyltransferase activity on the thermostable protein ST0452 from Sulfolobus tokodaii strain 7
J. Bacteriol.
192
3287-3293
2010
Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7 (Q975F9)
Zhang, Z.; Shimizu, Y.; Kawarabayasi, Y.
Characterization of the amino acid residues mediating the unique amino-sugar-1-phosphate acetyltransferase activity of the archaeal ST0452 protein
Extremophiles
19
417-427
2015
Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7 (Q975F9), Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7 (Q975F9)
Honda, Y.; Nakano, S.; Ito, S.; Dadashipour, M.; Zhang, Z.; Kawarabayasi, Y.
Improvement of ST0452 N-acetylglucosamine-1-phosphate uridyltransferase activity by the cooperative effect of two single mutations identified through structure-based protein engineering
Appl. Environ. Microbiol.
84
e002213-18
2018
Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii DSM 16993 (Q975F9)
Honda, Y.; Zang, Q.; Shimizu, Y.; Dadashipour, M.; Zhang, Z.; Kawarabayasi, Y.
Increasing the thermostable sugar-1-phosphate nucleotidylyltransferase activities of the archaeal ST0452 protein through site saturation mutagenesis of the 97th amino acid position
Appl. Environ. Microbiol.
83
e02291-16
2017
Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii DSM 16993 (Q975F9)
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