2.3.1.157: glucosamine-1-phosphate N-acetyltransferase
This is an abbreviated version!
For detailed information about glucosamine-1-phosphate N-acetyltransferase, go to the full flat file.
Word Map on EC 2.3.1.157
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2.3.1.157
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peptidoglycan
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utp
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drug development
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tokodaii
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glucosamine-6-phosphate
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left-hand
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udp-sugars
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glmm
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nucleotidylyltransferase
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utase
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diphosphate-n-acetylglucosamine
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medicine
- 2.3.1.157
- peptidoglycan
- utp
- drug development
- tokodaii
- glucosamine-6-phosphate
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left-hand
- udp-sugars
- glmm
-
nucleotidylyltransferase
- utase
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diphosphate-n-acetylglucosamine
- medicine
Reaction
Synonyms
amino-sugar-1-P AcTase, amino-sugar-1-phosphate acetyltransferase, bifunctional GlmU protein, bifunctional N-acetyltransferase/uridylyltransferase, bifunctional protein GlmU, bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase, galactosamine-1-phosphate acetyltransferase, GalN-1-P AcTase, GlcN-1-P acetyltransferase, GlcN-1-P AcTase, GlcNAc-1-P uridyltransferase, GlmU, GlmU acetyltransferase, GlmU enzyme, GlmU uridyltransferase, glucosamine 1-phosphate N-acetyltransferase/N-acetylglucosamine-1-phosphate uridyltransferase, glucosamine-1-phosphate acetyltransferase, glucosamine-1-phosphate acetyltransferase/N-acetylglucosamine-1-phosphate uridyltransferase, More, MtbGlmU, MtGlmU, N-acetylglucosamine-1-phosphate pyrophosphorylase, N-acetylglucosamine-1-phosphate uridyltransferase, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase, N-acetylglucosamine-1-phosphate-uridylyltransferase/glucosamine-1-phosphate-acetyltransferase, Rv1018c, Rxn-1, ST0452, ST0452 protein, STK_04520, UDP-GlcNAc pyrophosphorylase, UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase
ECTree
2.3.1.157 glucosamine-1-phosphate N-acetyltransferaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.3.1.157 - glucosamine-1-phosphate N-acetyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C380A
the acetyltransferase activity of the mutant is 2.6fold higher than that of the wild type enzyme
C380A/C405S
the double mutant has an increased kcat/Km value compared to the wild type enzyme
C405A
the mutant shows a slight increase in activity compared to the wild type enzyme
C405S
the mutant has an increased kcat/Km value compared to the wild type enzyme
V385C/C405S
the double mutant has an increased kcat/Km value compared to the wild type enzyme
C380A
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the acetyltransferase activity of the mutant is 2.6fold higher than that of the wild type enzyme
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C380A/C405S
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the double mutant has an increased kcat/Km value compared to the wild type enzyme
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C405A
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the mutant shows a slight increase in activity compared to the wild type enzyme
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C405S
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the mutant has an increased kcat/Km value compared to the wild type enzyme
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V385C/C405S
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the double mutant has an increased kcat/Km value compared to the wild type enzyme
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A451R
site-directed mutagenesis, neither the single mutants A451R and R439T nor the double mutant A451R/R439T affect the acetyltransferase activity significantly
A451R/R439T
site-directed mutagenesis, neither the single mutants A451R and R439T nor the double mutant A451R/R439T affect the acetyltransferase activity significantly
E458A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, 86% of wild-type acetyltransferase activity is remaining
H374A
K362A
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site-directed mutagenesis, the enzyme activity of the mutant is abolished by more than 90% of the wild-type acetyltransferase, and the affinity with the two substrates is completely lost
K403A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, 27% of wild-type acetyltransferase activity is remaining
K464A
K464A/W460A
site-directed mutagenesis, the mutant shows highly compromised activity compared to the wild-type enzyme
N397A
N456A
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site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme, 67% of wild-type acetyltransferase activity is remaining
R439T
site-directed mutagenesis, neither the single mutants A451R and R439T nor the double mutant A451R/R439T affect the acetyltransferase activity significantly
R463A
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site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
S416A
S474A
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site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
T296A
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in vitro kinase assays show that the mutant protein is phosphorylated to the same extent as the wild-type GlmU
T308A/T309A/T311A
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in vitro kinase assays show that the mutant protein is phosphorylated to the same extent as the wild-type GlmU
T324A/T341A/T347A
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in vitro kinase assays show that the mutant protein is phosphorylated to the same extent as the wild-type GlmU
T365A/T368A/T370A
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in vitro kinase assays show that the mutant protein is phosphorylated to the same extent as the wild-type GlmU
T376A/T401A/T406A/T407A
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in vitro kinase assays show that the mutant protein is phosphorylated to the same extent as the wild-type GlmU
T414A/T418A/T425/T432A/T436A
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in vitro kinase assays show that the mutant protein is not phosphorylated as the wild-type GlmU. These results confine PknB-mediated phosphorylation sites to a smaller region between amino acids 414 and 439 that harbors five threonines
T418A
T418E
T418S
site-directed mutagenesis, the acetyltransferase activity of the mutant is compromised as compared with GlmUMtb wild-type, the mutant shows 19% acetyltransferase activity and 108.8% of uridinyltransferase activity compared to the wild-type
T486A/T494A
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in vitro kinase assays show that the mutant protein is phosphorylated to the same extent as the wild-type GlmU
W460A
W460A/K64A
site-directed mutagenesis, the mutant shows 7.8% acetyltransferase activity and 104.7% of uridinyltransferase activity compared to the wild-type
Y398A
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site-directed mutagenesis, the enzyme activity of the mutant is abolished by more than 90% of the wild-type acetyltransferase, and the affinity with the two substrates is completely lost
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
H308A
T80S/Y97N
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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
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Y97A
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mutant enzyme exhibits the highest activity of the single-mutant proteins
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Y97N
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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
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H308A
K340A
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
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specific activity is 147.1% compared to the wild-type enzyme
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C307S
additional information
H374A
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site-directed mutagenesis, the enzyme activity of the mutant is abolished by more than 90% of the wild-type acetyltransferase, and the affinity with the two substrates is completely lost
H374A
site-directed mutagenesis, the mutant shows highly reduced Vmax in acetyltransfer compared to the wild-type enzyme
H374A
site-directed mutagenesis, the acetyltransferase active site mutant shows 1.7% of acetyltransferase activity and 96.7% of uridinyltransferase activity compared to the wild-type
K464A
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
K464A
site-directed mutagenesis, the mutant still shows acetyltransferase activity, the mutant shows 105.6% acetyltransferase activity and 97.9% of uridinyltransferase activity compared to the wild-type
N397A
site-directed mutagenesis, the mutant shows highly reduced Vmax in acetyltransfer compared to the wild-type enzyme
N397A
site-directed mutagenesis, the acetyltransferase active site mutant shows 5.2% of acetyltransferase activity and 113.6% of uridinyltransferase activity compared to the wild-type
S416A
site-directed mutagenesis, the mutant shows kinetics in acetyltransfer similar to the wild-type enzyme, S416 neither plays a role in catalysis nor in substrate binding
S416A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, 65% of wild-type acetyltransferase activity is remaining
S416A
site-directed mutagenesis, the acetyltransferase active site mutant shows 100.9% of acetyltransferase activity and 96.4% of uridinyltransferase activity compared to the wild-type
T418A
site-directed mutagenesis, T418 is the most abundant phosphorylation site on GlmUMtb, acetyltransferase activity is completely abolishe
T418A
site-directed mutagenesis, the acetyltransferase activity of mutant is severely compromised as compared with GlmUMtb wild-type, the mutant shows 2.4% acetyltransferase activity and 100.4% of uridinyltransferase activity compared to the wild-type
T418E
site-directed mutagenesis, acetyltransferase activity of T418E mutant that mimics a phosphorylated Thr, is severely compromised compared to wild-type GlmUMtb
T418E
site-directed mutagenesis, the acetyltransferase activity of the T418E mutant that mimics a phosphorylated Thr, is severely compromised as compared with GlmUMtb wild-type, the mutant shows 2.2% acetyltransferase activity and 109.2% of uridinyltransferase activity compared to the wild-type
W460A
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site-directed mutagenesis, the enzyme activity of the mutant is abolished by more than 90% of the wild-type acetyltransferase, and the affinity with the two substrates is completely lost
W460A
site-directed mutagenesis, the mutant shows highly compromised activity compared to the wild-type enzyme
W460A
site-directed mutagenesis, the mutant displays almost complete loss in acetyltransferase activity, the mutant shows 8.4% acetyltransferase activity and 99.8% of uridinyltransferase activity compared to the wild-type
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
H308A
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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
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H308A
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
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specific activity is 0.7% compared to the wild-type enzyme
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H308A
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
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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
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additional information
construction of Mycobacterium tuberculosis mutant strains overproducing GlmU allows determination of the contribution of the protein to mycobacterial entry into human neutrophils
additional information
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construction of Mycobacterium tuberculosis mutant strains overproducing GlmU allows determination of the contribution of the protein to mycobacterial entry into human neutrophils
additional information
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construction of Mycobacterium tuberculosis mutant strains overproducing GlmU allows determination of the contribution of the protein to mycobacterial entry into human neutrophils
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additional information
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construction of Mycobacterium tuberculosis mutant strains overproducing GlmU allows determination of the contribution of the protein to mycobacterial entry into human neutrophils
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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
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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
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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
-
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
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additional information
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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
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additional information
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
-
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
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
-
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
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