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Information on EC 2.7.7.23 - UDP-N-acetylglucosamine diphosphorylase and Organism(s) Sulfurisphaera tokodaii and UniProt Accession Q975F9

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EC Tree
IUBMB Comments
Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. 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 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase [3,4,6]. The enzyme from plants and animals is also active toward N-acetyl-alpha-D-galactosamine 1-phosphate (cf. EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase) [5,7], while the bacterial enzyme shows low activity toward that substrate .
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This record set is specific for:
Sulfurisphaera tokodaii
UNIPROT: Q975F9
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The taxonomic range for the selected organisms is: Sulfurisphaera tokodaii
Synonyms
acetylglucosamine 1-phosphate uridylyltransferase, AGX1, AGX2, CL6EHI_021200, CL6EHI_039830, EcGlmU, EnhiA.01126.a, EnhiA.01126.b, GlcNAc-1-P uridyltransferase, GlcNAc-1-P UTase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylglucosamine 1-phosphate uridylyltransferase
-
-
-
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GlcNAc-1-P uridyltransferase
299945
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GlcNAc-1-P UTase
299945
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GlcNAc-1-phosphate nucleotidylyltransferase
299945
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GlmU
-
-
-
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N-acetyl-D-glucosamine-1-phosphate uridylyltransferase
299945
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ST0452
UDP-GlcNAc pyrophosphorylase
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-
-
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UDP-HexNAc pyrophosphorylase
-
-
-
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UDPacetylglucosamine pyrophosphorylase
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-
-
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uridine diphosphate-N-acetylglucosamine pyrophosphorylase
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-
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uridine diphosphoacetylglucosamine phosphorylase
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uridine diphosphoacetylglucosamine pyrophosphorylase
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-
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UTP:2-acetamido-2-deoxy-alpha-D-glucose-1-phosphate uridylyltransferase
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-
-
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Ydl103c protein
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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-
-
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SYSTEMATIC NAME
IUBMB Comments
UTP:N-acetyl-alpha-D-glucosamine-1-phosphate uridylyltransferase
Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. 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 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase [3,4,6]. The enzyme from plants and animals is also active toward N-acetyl-alpha-D-galactosamine 1-phosphate (cf. EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase) [5,7], while the bacterial enzyme shows low activity toward that substrate [4].
CAS REGISTRY NUMBER
COMMENTARY hide
9023-06-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
show the reaction diagram
-
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-alpha-D-glucose
show the reaction diagram
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the activity with N-acetyl-D-glucosamine-1-phosphate is 3.4 times higher, respectively, than the corresponding activity with alpha-D-glucose-1-phosphate
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-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
show the reaction diagram
additional information
?
-
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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
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.016
diphosphate
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pH 7.5, 80C
0.008 - 0.861
N-acetyl-alpha-D-glucosamine 1-phosphate
0.016
UDP-N-acetyl-alpha-D-glucosamine
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pH 7.5, 80C
0.0017
UTP
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pH 7.5, 80C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.21
diphosphate
-
pH 7.5, 80C
2.54 - 49.75
N-acetyl-alpha-D-glucosamine 1-phosphate
8.4
UDP-N-acetyl-alpha-D-glucosamine
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pH 7.5, 80C
3.53
UTP
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pH 7.5, 80C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
380
diphosphate
-
pH 7.5, 80C
56.9 - 338.4
N-acetyl-alpha-D-glucosamine 1-phosphate
530
UDP-N-acetyl-alpha-D-glucosamine
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pH 7.5, 80C
2120
UTP
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pH 7.5, 80C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2
-
N-acetyl-alpha-D-glucosamine 1-phosphate substrate, pH 7.5, 80C, recombinant mutant D005 protein
2.2
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N-acetyl-alpha-D-glucosamine 1-phosphate substrate, pH 7.5, 80C, recombinant wild-type ST0452 protein
2.6
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N-acetyl-alpha-D-glucosamine 1-phosphate substrate, pH 7.5, 80C, recombinant mutant D011 protein
6.42
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pH 7.5, 80C, substrates: UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
16.34
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pH 7.5, 80C, substrates: diphosphate + UDP-N-acetyl-alpha-D-glucosamine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
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pH 6.0: about 50% of maximal activity, pH 10.0: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70 - 100
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70C: about 40% of maximal activity, 100C: about 80% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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the enzyme is involved in biosyntheis of UDP-N-acetylglucosamine
physiological function
additional information
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the ST0452 protein contains only two Cys residues, it is unlikely that CysCys bonds contribute to its thermostability
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
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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
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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
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method at 22C, crystallization of the Y97N protein
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D208A
D99A
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no GlcNAc-1-P UTase activity
E146A
G9A/K147A
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specific GlcNAc-1-P UTase activity of the mutant enzyme is 71.8fold lower compared to specific activity of the wild-type enzyme
G9A/T80A
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specific GlcNAc-1-P UTase activity of the mutant enzyme is 35fold lower compared to specific activity of the wild-type enzyme
G9A/Y97A
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no activity
G9A/Y97F
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specific GlcNAc-1-P UTase activity of the mutant enzyme is 14.5fold lower compared to specific activity of the wild-type enzyme
H308A
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site-directed mutagenesis
K147A
K23A
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no GlcNAc-1-P UTase activity
K337A
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site-directed mutagenesis
K340A
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site-directed mutagenesis
N331A
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site-directed mutagenesis
T80A/K147A
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specific GlcNAc-1-P UTase activity of the mutant enzyme is 11.09fold lower compared to specific activity of the wild-type enzyme
T80A/Y97A
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specific GlcNAc-1-P UTase activity of the mutant enzyme is 31.4fold lower compared to specific activity of the wild-type enzyme
T80A/Y97F
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specific GlcNAc-1-P UTase activity of the mutant enzyme is 25.1fold lower compared to specific activity of the wild-type enzyme
T80L
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no GlcNAc-1-P UTase activity
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
Y311A
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site-directed mutagenesis
Y97A/K147A
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specific GlcNAc-1-P UTase activity of the mutant enzyme is 11.9fold lower compared to specific activity of the wild-type enzyme
Y97F/K147A
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specific GlcNAc-1-P UTaseactivity of the mutant enzyme is 5.7fold lower compared to specific activity of the wild-type enzyme
Y97V
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3.56fold increase in GlcNAc-1-P UTase activity compared to that of the wild-type enzyme
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
-
half-life: 180 min
95
-
half-life: 60 min
additional information
-
N-acetyl-D-glucosamine-1-phosphate uridylyltransferase activity of the mutant enzyme deletion mutant lacking the 170-residue C-terminal domain remains in the truncated enzyme after 5 min of heating at 65 C but is completely removed by treatment over 70C
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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expression in Escherichia coli BL21-Codon Plus (DE3)-RIL cells
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expression in Escherichia coli, wild-type and truncated enzyme form lacking the 170-residues C-terminal domain
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expression of mutant enzymes in Escherichia coli
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gene ST0452, recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21-Codon Plus(DE3)-RIL
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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biosynthesis of UDP-N-acetyl-alpha-D-glucosamine. As glycosylation is the most important modification for activating peptide drugs, the activated form of N-acetyl-alpha-D-glucosamine is thought to be important for future development of effective drugs
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhang, Z.; Tsujimura, M.; Akutsu, J.; Sasaki, M.; Tajima, H.; Kawarabayasi, Y.
Identification of an extremely thermostable enzyme with dual sugar-1-phosphate nucleotidylyltransferase activities from an acidothermophilic archaeon, Sulfolobus tokodaii strain 7
J. Biol. Chem.
280
9698-9705
2005
Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii 7 (Q975F9)
Manually annotated by BRENDA team
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 7 (Q975F9)
Manually annotated by BRENDA team
Zhang, Z.; Akutsu, J.; Tsujimura, M.; Kawarabayasi, Y.
Increasing in archaeal GlcNAc-1-P uridyltransferase activity by targeted mutagenesis while retaining its extreme thermostability
J. Biochem.
141
553-562
2007
Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii 7 (Q975F9)
Manually annotated by BRENDA team
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 DSM 16993 / JCM 10545 / NBRC 100140 / 7 (Q975F9)
Manually annotated by BRENDA team
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
2017
Escherichia coli (P0ACC7), Escherichia coli K12 (P0ACC7), Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii DSM 16993 (Q975F9)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Dadashipour, M.; Iwamoto, M.; Hossain, M.M.; Akutsu, J.I.; Zhang, Z.; Kawarabayasi, Y.
Identification of a direct biosynthetic pathway for UDP-N-acetylgalactosamine from glucosamine-6-phosphate in thermophilic crenarchaeon Sulfolobus tokodaii
J. Bacteriol.
200
e00048-18
2018
Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii DSM 16993 (Q975F9)
Manually annotated by BRENDA team
Zhang, Z.; Akutsu, J.; Tsujimura, M.; Kawarabayasi, Y.
Increasing in archaeal GlcNAc-1-P uridyltransferase activity by targeted mutagenesis while retaining its extreme thermostability
J. Biochem.
141
553-562
2007
Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii DSM 16993 (Q975F9)
Manually annotated by BRENDA team
Zhang, Z.; Tsujimura, M.; Akutsu, J.; Sasaki, M.; Tajima, H.; Kawarabayasi, Y.
Identification of an extremely thermostable enzyme with dual sugar-1-phosphate nucleotidylyltransferase activities from an acidothermophilic archaeon, Sulfolobus tokodaii strain 7
J. Biol. Chem.
280
9698-9705
2005
Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii DSM 16993 (Q975F9)
Manually annotated by BRENDA team
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