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2 - 231.9
N-acetyl-D-glucosamine
1.7 - 211
N-acetyl-D-mannosamine
2 - 2.2
N-acetyl-D-glucosamine
-
pH 9.0, 30°C
3.4
N-acetyl-D-glucosamine
-
-
5.2
N-acetyl-D-glucosamine
E242Q, reverse conversion in the presence of 1 mM ATP
6.94
N-acetyl-D-glucosamine
-
-
7.4
N-acetyl-D-glucosamine
-
7.4
N-acetyl-D-glucosamine
R375K, reverse conversion in the presence of 1 mM ATP
9.5
N-acetyl-D-glucosamine
pH 7.5, 30°C, recombinant His6-tagged mutant K155A
13.4
N-acetyl-D-glucosamine
E218D, reverse conversion in the presence of 1 mM ATP
16.1
N-acetyl-D-glucosamine
pH 7.5, 30°C, recombinant His6-tagged mutant K157L
16.3
N-acetyl-D-glucosamine
-
pH 7.5, 30°C
16.3
N-acetyl-D-glucosamine
pH 7.5, 30°C, recombinant His6-tagged wild-type enzyme
16.6
N-acetyl-D-glucosamine
-
pH 7.5, 30°C
16.7
N-acetyl-D-glucosamine
C370A, reverse conversion in the presence of 1 mM ATP
16.7
N-acetyl-D-glucosamine
R375A, reverse conversion in the presence of 1 mM ATP
18.8
N-acetyl-D-glucosamine
-
pH 7.5, 37°C
18.8
N-acetyl-D-glucosamine
-
pH 8.0, 30°C
21.3
N-acetyl-D-glucosamine
-
37°C, pH 7.5
24.4
N-acetyl-D-glucosamine
E218A, reverse conversion in the presence of 1 mM ATP
24.6
N-acetyl-D-glucosamine
-
pH 7.5, 30°C
25.4
N-acetyl-D-glucosamine
wild type, reverse conversion in the presence of 1 mM ATP
26.1
N-acetyl-D-glucosamine
-
pH 7.0, 30°C
44.2
N-acetyl-D-glucosamine
pH 7.5, 30°C, recombinant His6-tagged mutant K151V
45.7
N-acetyl-D-glucosamine
N179A, reverse conversion in the presence of 1 mM ATP
62.5
N-acetyl-D-glucosamine
-
pH 6.0, 30°C
113.9
N-acetyl-D-glucosamine
-
pH 7.5, 30°C, without ATP
129
N-acetyl-D-glucosamine
pH 7.5, 30°C, recombinant His6-tagged mutant K160P
231.9
N-acetyl-D-glucosamine
-
pH 7.5, 37°C, without ATP
1.7
N-acetyl-D-mannosamine
-
in presence of saturating concentrations of ATP
3
N-acetyl-D-mannosamine
-
-
4.76
N-acetyl-D-mannosamine
-
-
6.3
N-acetyl-D-mannosamine
-
9
N-acetyl-D-mannosamine
-
in absence of ATP
9.2
N-acetyl-D-mannosamine
R375K, in the presence of 1 mM ATP
12.8
N-acetyl-D-mannosamine
-
37°C, pH 7.5
13.9
N-acetyl-D-mannosamine
R375A, in the presence of 1 mM ATP
14.8
N-acetyl-D-mannosamine
wild type, at pH 7, in the presence of 1 mM ATP
15.5
N-acetyl-D-mannosamine
E218A, in the presence of 1 mM ATP
15.6
N-acetyl-D-mannosamine
wild type, at pH 8, in the presence of 1 mM ATP
16.6
N-acetyl-D-mannosamine
-
pH 7.5, 30°C
16.7
N-acetyl-D-mannosamine
-
pH 7.5, 30°C
16.7
N-acetyl-D-mannosamine
pH 7.5, 30°C, recombinant His6-tagged wild-type enzyme
19.7
N-acetyl-D-mannosamine
-
pH 7.5, 30°C
21
N-acetyl-D-mannosamine
E218D, in the presence of 1 mM ATP
21.3
N-acetyl-D-mannosamine
C370A, in the presence of 1 mM ATP
25.4
N-acetyl-D-mannosamine
-
27.2
N-acetyl-D-mannosamine
N179A, in the presence of 1 mM ATP
30.1
N-acetyl-D-mannosamine
pH 7.5, 30°C, recombinant His6-tagged mutant K157L
31.6
N-acetyl-D-mannosamine
pH 7.5, 30°C, recombinant His6-tagged mutant K151V
32.7
N-acetyl-D-mannosamine
wild type, at pH 9, in the presence of 1 mM ATP
53.8
N-acetyl-D-mannosamine
E242Q, in the presence of 1 mM ATP
57.33
N-acetyl-D-mannosamine
wild type, at pH 6 in the presence of 1 mM ATP
67.9
N-acetyl-D-mannosamine
pH 7.5, 30°C, recombinant His6-tagged mutant K155A
211
N-acetyl-D-mannosamine
pH 7.5, 30°C, recombinant His6-tagged mutant K160P
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0.07818
AGE, immobilized recombinant enzyme, the activity yield of immobilized enzyme is approximately 30% of the free enzyme, activity is determined in 1 ml of reaction solution (100 mM Tris-HCl, pH 7.5, 100 mM GlcNAc, 10 mM MgCl2, and 2.5 mM ATP)
0.49
specific activity in crude extract after expression in Escherichia coli cells, activity is determined in 1 ml of reaction solution (100 mM Tris-HCl, pH 7.5, 100 mM GlcNAc, 10 mM MgCl2, and 2.5 mM ATP)
117
-
with N-acetyl-D-glucosamine, pH 7.5, 30°C
123.8
wild type, reverse conversion in the presence of 1 mM ATP
124
in the presence of 1 mM ATP
131
-
with 430 mM N-acetyl-D-glucosamine, pH 9.0, 30°C
22.8
E218A, in the presence of 1 mM ATP
256.4
E218D, in the presence of 1 mM ATP
258.5
N179A, in the presence of 1 mM ATP
29.13
recombinant enzyme after purification, activity is determined in 1 ml of reaction solution (100 mM Tris-HCl, pH 7.5, 100 mM GlcNAc, 10 mM MgCl2, and 2.5 mM ATP)
32
in the presence of 1 mM ATP
351
C370A, in the presence of 1 mM ATP
46.5
E218D, reverse conversion in the presence of 1 mM ATP
5.6
E242Q, reverse conversion in the presence of 1 mM ATP
50.8
N179A, reverse conversion in the presence of 1 mM ATP
525.8
wild type, in the presence of 1 mM ATP
54.8
R375A, in the presence of 1 mM ATP
6.2
R375A, reverse conversion in the presence of 1 mM ATP
6.6
E218A, reverse conversion in the presence of 1 mM ATP
79.2
-
with N-acetyl-D-glucosamine, pH 6.0, 30°C
8.1
E242Q, in the presence of 1 mM ATP
8.9
R375K, reverse conversion in the presence of 1 mM ATP
82.1
-
with N-acetyl-D-glucosamine, pH 7.0, 30°C
82.4
-
with 250 mM N-acetyl-D-glucosamine, pH 9.0, 30°C
85.9
C370A, reverse conversion in the presence of 1 mM ATP
90.8
-
with N-acetyl-D-glucosamine, pH 8.0, 30°C
94.3
R375K, in the presence of 1 mM ATP
additional information
-
-
additional information
Escherichia coli cells harboring the recombinant plasmid are grown at 37°C in TB medium and induced by adding lactose to a final concentration of 1% lactose, samples are taken every 2 h, and the highest activity is 0.825 U/ml after fermentation for 22 h, activity is determined in 1 ml of reaction solution (100 mM Tris-HCl, pH 7.5, 100 mM GlcNAc, 10 mM MgCl2, and 2.5 mM ATP)
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C370A
site directed mutagenesis
E218A
site directed mutagenesis
E218D
site directed mutagenesis
E242Q
site directed mutagenesis
E308A
site directed mutagenesis
E308D
site directed mutagenesis
H239A
site directed mutagenesis
H239N
site directed mutagenesis
H372A
site directed mutagenesis
H372I
site directed mutagenesis
H372N
site directed mutagenesis
N179A
site directed mutagenesis
R375A
site directed mutagenesis
R375K
site directed mutagenesis
R57A
site directed mutagenesis
R57K
site directed mutagenesis
C104S
-
specific activity in the extract is 25% of that of the wild-type enzyme
C125S/C210S
-
mutant enzyme shows 54.8% of the activity relative to the wild-type enzyme
C125S/C210S/C239S
-
mutant enzyme shows 49.3% of the activity relative to the wild-type enzyme
C125S/C210S/C239S/C203S
-
mutant enzyme shows 28.7% of the activity relative to the wild-type enzyme
C125S/C210S/C239S/C203S/C386S
-
mutant enzyme shows 23.8% of the activity relative to the wild-type enzyme
C125S/C210S/C302S/C390S
-
no activity detected
C125S/C386S
-
mutant enzyme shows 68.7% of the activity relative to the wild-type enzyme
C125S/C390S
-
mutant enzyme shows 5.1% of the activity relative to the wild-type enzyme
C210S
-
relative specific activity in the extract is nearly the same to that of the wild-type enzyme
C210S/C386S
-
mutant enzyme shows 88.7% of the activity relative to the wild-type enzyme
C210S/C390S
-
mutant enzyme shows 30.9% of the activity relative to the wild-type enzyme
C239S
-
relative specific activity in the extract is nearly the same to that of the wild-type enzyme
C239S/C386S
-
mutant enzyme shows 116% of the activity relative to the wild-type enzyme
C239S/C390S
-
mutant enzyme shows 27.8% of the activity relative to the wild-type enzyme
C302S
-
relative specific activity in the extract is nearly the same to that of the wild-type enzyme
C302S/C386S
-
mutant enzyme shows 65.8% of the activity relative to the wild-type enzyme
C302S/C390S
-
mutant enzyme shows 7.4% of the activity relative to the wild-type enzyme
C380S
-
no enzyme activity detected in the extract
C41S/C125S
-
mutant enzyme shows 17.7% of the activity relative to the wild-type enzyme
C41S/C125S/C210S
-
mutant enzyme shows 28.1% of the activity relative to the wild-type enzyme
C41S/C125S/C210S/C239S
-
mutant enzyme shows 9.7% of the activity relative to the wild-type enzyme
C41S/C125S/C210S/C239S/C302S
-
no activity detected
C41S/C125S/C210S/C239S/C302S/C386S
-
no activity detected
C41S/C125S/C210S/C239S/C302S/C390S
-
no activity detected
C41S/C386S
-
mutant enzyme shows 0.7% of the activity relative to the wild-type enzyme
C41S/C390S
-
no activity detected
C66S/C125S
-
mutant enzyme shows 39.4% of the activity relative to the wild-type enzyme
C66S/C125S/C210S
-
mutant enzyme shows 23.9% of the activity relative to the wild-type enzyme
C66S/C125S/C210S/C239S
-
mutant enzyme shows 58.4% of the activity relative to the wild-type enzyme
C66S/C125S/C210S/C239S/C302S
-
mutant enzyme shows 15.5% of the activity relative to the wild-type enzyme
C66S/C125S/C210S/C302S/C386S
-
no activity detected
C66S/C125S/C210S/C302S/C390S
-
no activity detected
C66S/C386S
-
mutant enzyme shows 113% of the activity relative to the wild-type enzyme
C66S/C390S
-
mutant enzyme shows 14.4% of the activity relative to the wild-type enzyme
DELTA380-417
-
mutant enzyme has no activity
DELTA386-417
-
mutant enzyme has no activity
DELTA390-417
-
mutant enzyme has no activity
DELTA400-417
-
C-terminal deletion mutant has approximately 50% activity relative to the wild-type enzyme
K151V
site-directed mutagenesis, the mutation within the ATP-binding site leads to biphasic enzyme inactivation in the presence of 400 mM pyruvate
K155A
site-directed mutagenesis, the mutation within the ATP-binding site leads to biphasic enzyme inactivation in the presence of 400 mM pyruvate
K157L
site-directed mutagenesis, the mutation within the ATP-binding site leads to biphasic enzyme inactivation in the presence of 400 mM pyruvate
K160I
site-directed mutagenesis, within the ATP-binding site, the mutant shows no inactivation by pyruvate, in contrast to the wild-type enzyme, but significantly impaired kinetic parameters compared to wild-type
K160L
site-directed mutagenesis, within the ATP-binding site, the mutant shows no inactivation by pyruvate, in contrast to the wild-type enzyme, but significantly impaired kinetic parameters compared to wild-type
K160N
site-directed mutagenesis, within the ATP-binding site, the mutant shows no inactivation by pyruvate, in contrast to the wild-type enzyme, but significantly impaired kinetic parameters compared to wild-type
K160P
site-directed mutagenesis, within the ATP-binding site
C125S
-
no loss of activity compared to wild-type enzyme
C125S
-
relative specific activity in the extract is nearly the same to that of the wild-type enzyme
C386S
-
no loss of activity compared to wild-type enzyme
C386S
-
relative specific activity in the extract is nearly the same to that of the wild-type enzyme
C390S
-
no loss of activity compared to wild-type enzyme
C390S
-
relative specific activity in the extract is nearly the same to that of the wild-type enzyme
C41S
-
no loss of activity compared to wild-type enzyme
C41S
-
relative specific activity in the extract is nearly the same to that of the wild-type enzyme
C66S
-
no loss of activity compared to wild-type enzyme
C66S
-
relative specific activity in the extract is nearly the same to that of the wild-type enzyme
additional information
metabolic channeling enables efficient transfer of the intermediates by forming a multienzyme complex. To leverage the metabolic channeling for improved biosynthesis, N-acetylneuraminic acid lyase from Corynebacterium glutamicum ATCC 13032 (CgNal, EC 4.1.3.3) and N-acetylglucosamine-2-epimerase from Anabaena sp. CH1 (anAGE) are coexpressed in Escherichia coli and the whole cell are used to synthesize N-acetylneuraminic acid (Neu5Ac) from N-acetylglucosamine (GlcNAc) and pyruvate. To get the multienzyme complex, a polycistronic plasmid with high levels of CgNal and anAGE expression is constructed by tuning the orders of the genes. The Shine-Dalgarno (SD) sequence and aligned spacing (AS) distance are optimized. The Escherichia coli strain Rosetta harboring the polycistronic plasmid pET-28a-SD2-AS1-CgNal-SD-AS-anAGE increases the production of Neu5Ac by 58.7% to 92.5 g/l in 36 h by whole-cell catalysis and by 21.9% up to 112.8 g/l in 24 h with the addition of Triton X-100
additional information
production of N-acetyl-D-neuraminic acid by recombinant single whole cells co-expressing N-acetyl-D-glucosamine-2-epimerase and N-acetyl-D-neuraminic acid aldolase in Escherichia coli. Method development and evaluation, overview
additional information
-
construction of a series of chimeric enzymes successively replacing the three domains of the human enzyme - N-terminal, middle, and C-terminal - with the corresponding domains of the rat enzyme. Chimerae are expressed in Escherichia coli JM109 under the control of the Taq promoter. Chimeric enzymes of HHR, RHH and RHR - where H is a human type domain and R is a rat type domain - have nearly the same nucleotide specificity as the human enzyme. HRR, HRH, and RRH chimeras have the same nucleotide specificity as the rat enzyme. These results indicate that the middle domain of the enzyme molecule participates in the specificity for and binding of nucleotides
additional information
-
mutational analysis of multi-cysteine/serine mutants reveals that Cys41 and Cys390 are critical for the activity or stabilization of the enzyme, while cysteine residues in the middle of the enzyme, Cys125, Cys210, Cys239, and Cys302 have no essential function in relation to the activity
additional information
-
construction of a series of chimeric enzymes successively replacing the three domains of the human enzyme - N-terminal, middle, and C-terminal - with the corresponding domains of the rat enzyme. Chimeras are expressed in Escherichia coli JM109 under the control of the Taq promoter. Chimeric enzymes of HHR, RHH and RHR - where H is a human type domain and R is a rat type domain - have nearly the same nucleotide specificity as the human enzyme. HRR, HRH, and RRH chimeras have the same nucleotide specificity as the rat enzyme. These results indicate that the middle domain of the enzyme molecule participates in the specificity for and binding of nucleotides
additional information
the majority of biocatalytic approaches for Neu5Ac synthesis involve an N-acylglucosamine 2-epimerase (AGE, EC 5.3.1.8) in combination with an N-acetylneuraminate lyase (NAL, EC 4.1.3.3)
additional information
two-step enzymatic synthesis of N-acetylneuraminic acid (Neu5Ac) using an N-acyl-D-glucosamine 2-epimerase from Anabaena variabilis ATCC 29413 (AvaAGE) in combination with an N-acetylneuraminate lyase (NAL) from Escherichia coli. AvaAGE epimerizes N-acetyl-D-glucosamine (GlcNAc) to N-acetyl-D-mannosamine (ManNAc), which then reacts with pyruvate in a NAL-catalyzed aldol condensation to form Neu5Ac. AvaAGE is inactivated by high pyruvate concentrations, which are used to push the NAL reaction toward the product side. A biphasic inactivation is observed in the presence of 50-800 mM pyruvate resulting in activity losses of the AvaAGE of up to 60% within the first hour. Site-directed mutagenesis reveals that pyruvate modifies one of the four lysine residues in the ATP-binding site of AvaAGE
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2 recombinant Escherichia coli strains capable of expressing N-acetyl-D-glucosamine 2-epimerase and N-acetyl-D-neuraminic acid aldolase are constructed based on a highly efficient temperature-responsive expression system which is safe compared to chemical-induced systems and coupled in N-acetyl-D-neuraminic acid production
-
construction of a series of chimeric enzymes successively replacing the three domains of the human enzyme - N-terminal, middle, and C-terminal - with the corresponding domains of the rat enzyme. Chimeras are expressed in Escherichia coli JM109 under the control of the Taq promoter
construction of several C-terminal deletion and multi-cysteine/serine mutants and expression in Escherichia coli
-
expressed in Escherichia coli JM109 under the transcriptional control of taq promoter
-
expression in Escherichia coli
expression in Jurkat cells
-
expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) in inclusion bodies, subcloning in Escherichia coli strain DH5alpha
-
expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
expression of wild-type enzyme and mutant enzymes C41S, C66S, C104S, C125S, C210S, C239S, C302S, C380S, C386S and C390S in Escherichia coli
-
gene age, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) at 37°C with coexpression of chaperones GroEL/GroES, 264fold increased AGE activity and maximum yield of 22.5 mg isolated AvaAGE per liter shake flask culture, compared to the starting conditions, method optimization, enhancement of soluble expression via chaperones, temperature dependence of soluble expression, and enhancement of soluble expression via fusion tags, overview
gene BACOVA_01816, expression of His-tagged enzyme in Escherichia coli strain Rosetta (DE3)pLys
gene bage, recombinant expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3), coexpression with N-acetyl-D-neuraminic acid aldolase gene nanA from Escherichia coli
recombinant enzyme expression in Escherichia coli, coexpression with N-acetylneuraminic acid lyase from Corynebacterium glutamicum ATCC 13032 (CgNal, EC 4.1.3.3)
recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain NovaBlue (DE3)
construction of a series of chimeric enzymes successively replacing the three domains of the human enzyme - N-terminal, middle, and C-terminal - with the corresponding domains of the rat enzyme. Chimeras are expressed in Escherichia coli JM109 under the control of the Taq promoter
-
construction of a series of chimeric enzymes successively replacing the three domains of the human enzyme - N-terminal, middle, and C-terminal - with the corresponding domains of the rat enzyme. Chimeras are expressed in Escherichia coli JM109 under the control of the Taq promoter
-
expression in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli
expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
-
expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
-
expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
-
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Van Rinsum, J.; van Dijk, W.; Hooghwinkel, G.J.M.; Ferwerda, W.
Subcellular localization and tissue distribution of sialic acid precursor-forming enzymes
Biochem. J.
210
21-28
1983
Rattus norvegicus
brenda
Corfield, A.P.; Clamp, J.R.; Wagner, S.A.
The metabolism of sialic acids in isolated rat colonic mucosal cells
Biochem. Soc. Trans.
11
767-768
1983
Rattus norvegicus
-
brenda
Corfield, A.P.; Rainey, J.B.; Clamp, J.R.; Wagner, S.A.
Rat colonic mucosal cell sialic acid metabolism in azoxymethane-induced tumours
Biochim. Biophys. Acta
840
264-270
1985
Rattus norvegicus
brenda
Corfield, A.P.; Clamp, J.R.; Wagner, S.A.
The metabolism of sialic acids in isolated rat colonic mucosal cells
Biochem. J.
226
163-174
1985
Rattus norvegicus
brenda
Datta, A.
N-Acetylglucosamine 2-epimerase from hog kidney
Methods Enzymol.
41
407-412
1975
Sus scrofa
brenda
Ghosh, S.; Roseman, S.
N-Acetylglucosamine 2-epimerase from hog kidney
Methods Enzymol.
8
191-195
1966
Sus scrofa
-
brenda
Ghosh, S.; Roseman, S.
The sialic acids. V. N-Acyl-D-glucosamine 2-epimerase
J. Biol. Chem.
240
1531-1536
1965
Sus scrofa
brenda
Maru, I.; Ohta, Y.; Murata, K.; Tsukada, Y.
Molecular cloning and identification of N-acetyl-D-glucosamine 2-epimerase from porcine kidney as a renin-binding protein
J. Biol. Chem.
271
16294-16299
1996
Sus scrofa (P17560), Sus scrofa
brenda
Maru, I.; Ohnishi, J.; Ohta, Y.; Hashimoto, W.; Tsukada, Y.; Murata, K.; Mikami, B.
Crystallization and preliminary X-ray diffraction studies of N-acetyl-D-glucosamine 2-epimerase from porcine kidney
J. Biochem.
120
481-482
1996
Sus scrofa
brenda
Maru, I.; Ohnishi, J.; Ohta, Y.; Tsukada, Y.
Simple and large-scale production of N-acetylneuraminic acid from N-acetyl-D-glucosamine and pyruvate using N-acyl-D-glucosamine 2-epimerase and N-acetylneuraminate lyase
Carbohydr. Res.
306
575-578
1998
Escherichia coli
brenda
Corfield, A.P.; Rainey, J.B.; Clamp, J.R.; Wagner, S.A.
Changes in the activity of the enzymes involved in sialic acid metabolism in isolated rat colonic mucosal cells on administration of azoxymethane
Biochem. Soc. Trans.
11
766-767
1983
Rattus norvegicus
-
brenda
Tabata, K.; Koizumi, S.; Endo, T.; Ozaki, A.
Production of N-acetyl-D-neuraminic acid by coupling bacteria expressing N-acetyl-D-glucosamine 2-epimerase and N-acetyl-D-neuraminic acid synthetase
Enzyme Microb. Technol.
30
327-333
2002
Synechocystis sp.
-
brenda
Takahashi, S.; Takahashi, K.; Kaneko, T.; Ogasawara, H.; Shindo, S.; Kobayashi, M.
Human renin-binding protein is the enzyme N-acetyl-D-glucosamine 2-epimerase
J. Biochem.
125
348-353
1999
Homo sapiens
brenda
Takahashi, S.; Takahashi, K.; Kaneko, T.; Ogasawara, H.; Shindo, S.; Saito, K.; Kobayashi, M.
Identification of cysteine-380 as the essential residue for the human N-acetyl-D-glucosamine 2-epimerase (renin binding protein)
J. Biochem.
126
639-642
1999
Homo sapiens
brenda
Takahashi, S.; Kumagai, M.; Shindo, S.; Saito, K.; Kawamura, Y.
Renin inhibits N-acetyl-D-glucosamine 2-epimerase (renin-binding protein)
J. Biochem.
128
951-956
2000
Homo sapiens
brenda
Takahashi, S.; Takahashi, K.; Kaneko, T.; Ogasawara, H.; Shindo, S.; Saito, K.; Kawamura, Y.
Identification of functionally important cysteine residues of the human renin-binding protein as the enzyme N-acetyl-D-glucosamine 2-epimerase
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2001
Homo sapiens
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Takahashi, S.; Ogasawara, H.; Takahashi, K.; Hori, K.; Saito, K.; Mori, K.
Identification of a domain conferring nucleotide binding to the N-acetyl-D-glucosamine 2-epimerase (renin binding protein)
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2002
Homo sapiens, Rattus norvegicus
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Luchansky, S.J.; Yarema, K.J.; Takahashi, S.; Bertozzi, C.R.
GlcNAc 2-epimerase can serve a catabolic role in sialic acid metabolism
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Homo sapiens
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Itoh, T.; Mikami, B.; Maru, I.; Ohta, Y.; Hashimoto, W.; Murata, K.
Crystal structure of N-acyl-D-glucosamine 2-epimerase from porcine kidney at 2.0 A resolution
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2000
Sus scrofa
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Lee, J.O.; Yi, J.K.; Lee, S.G.; Takahashi, S.; Kim, B.G.
Production of N-acetylneuraminic acid from N-acetylglucosamine and pyruvate using recombinant human renin binding protein and sialic acid aldolase in one pot
Enzyme Microb. Technol.
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2004
Homo sapiens
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brenda
Takahashi, S.; Hori, K.; Ogasawara, H.; Hiwatashi, K.; Sugiyama, T.
Effects of nucleotides on the interaction of renin with GlcNAc 2-epimerase (renin binding protein, RnBP)
J. Biochem.
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725-730
2006
Sus scrofa (P17560), Sus scrofa
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Lee, Y.C.; Chien, H.C.; Hsu, W.H.
Production of N-acetyl-D-neuraminic acid by recombinant whole cells expressing Anabaena sp. CH1 N-acetyl-D-glucosamine 2-epimerase and Escherichia coli N-acetyl-D-neuraminic acid lyase
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2007
Anabaena sp. CH1 (A4UA16), Sus scrofa (P17560), Sus scrofa
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Lee, Y.C.; Wu, H.M.; Chang, Y.N.; Wang, W.C.; Hsu, W.H.
The central cavity from the (alpha/alpha)6 barrel structure of Anabaena sp. CH1 N-acetyl-D-glucosamine 2-epimerase contains two key histidine residues for reversible conversion
J. Mol. Biol.
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2007
Anabaena sp. CH1 (A4UA16)
brenda
Hu, S.; Chen, J.; Yang, Z.; Shao, L.; Bai, H.; Luo, J.; Jiang, W.; Yang, Y.
Coupled bioconversion for preparation of N-acetyl-D-neuraminic acid using immobilized N-acetyl-D-glucosamine-2-epimerase and N-acetyl-D-neuraminic acid lyase
Appl. Microbiol. Biotechnol.
85
1383-1391
2010
Sus scrofa (P17560)
brenda
Zhang, Y.; Tao, F.; Du, M.; Ma, C.; Qiu, J.; Gu, L.; He, X.; Xu, P.
An efficient method for N-acetyl-D-neuraminic acid production using coupled bacterial cells with a safe temperature-induced system
Appl. Microbiol. Biotechnol.
86
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2010
Synechocystis sp. PCC 6803
brenda
Sola-Carvajal, A.; Sanchez-Carron, G.; Garcia-Garcia, M.I.; Garcia-Carmona, F.; Sanchez-Ferrer, A.
Properties of BoAGE2, a second N-acetyl-D-glucosamine 2-epimerase from Bacteroides ovatus ATCC 8483
Biochimie
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222-230
2012
Bacteroides ovatus (A7LVG6), Bacteroides ovatus ATCC 8483 (A7LVG6), Bacteroides ovatus ATCC 8483
brenda
Klermund, L.; Groher, A.; Castiglione, K.
New N-acyl-D-glucosamine 2-epimerases from cyanobacteria with high activity in the absence of ATP and low inhibition by pyruvate
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2013
Acaryochloris marina, Acaryochloris marina MBIC 11017, Nostoc punctiforme, Nostoc sp., Nostoc sp. PCC 7120, Trichormus variabilis
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Wang, S.; Laborda, P.; Lu, A.; Duan, X.; Ma, H.; Liu, L.; Voglmeir, J.
N-acetylglucosamine 2-epimerase from Pedobacter heparinus First experimental evidence of a deprotonation/reprotonation mechanism
Catalysts
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212-228
2016
Pedobacter heparinus (C6Y403), Homo sapiens (P51606), Pedobacter heparinus ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3 (C6Y403)
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Klermund, L.; Riederer, A.; Hunger, A.; Castiglione, K.
Protein engineering of a bacterial N-acyl-D-glucosamine 2-epimerase for improved stability under process conditions
Enzyme Microb. Technol.
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2016
Trichormus variabilis (Q3M763)
brenda
Wang, Z.; Zhuang, W.; Cheng, J.; Sun, W.; Wu, J.; Chen, Y.; Ying, H.
In vivo multienzyme complex coconstruction of N-acetylneuraminic acid lyase and N-acetylglucosamine-2-epimerase for biosynthesis of N-acetylneuraminic acid
J. Agric. Food Chem.
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2017
Anabaena sp. CH1 (A4UA16)
brenda
Kao, C.H.; Chen, Y.Y.; Wang, L.R.; Lee, Y.C.
Production of N-acetyl-D-neuraminic acid by recombinant single whole cells co-expressing N-acetyl-D-glucosamine-2-epimerase and N-acetyl-D-neuraminic acid aldolase
Mol. Biotechnol.
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427-434
2018
Anabaena sp. CH1 (A4UA16)
brenda
Klermund, L.; Riederer, A.; Groher, A.; Castiglione, K.
High-level soluble expression of a bacterial N-acyl-D-glucosamine 2-epimerase in recombinant Escherichia coli
Protein Expr. Purif.
111
36-41
2015
Trichormus variabilis (Q3M763)
brenda