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EC Tree
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
glcnac 2-epimerase, renin-binding protein, anage, n-acetyl-d-glucosamine 2-epimerase, n-acyl-d-glucosamine 2-epimerase, renin binding protein, n-acetylglucosamine 2-epimerase, avaage, bglcnac 2-epimerase, n-acylglucosamine 2-epimerase,
more
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bGlcNAc 2-epimerase
recombinant protein
N-acetyl-D-glucosamine-2-epimerase
-
N-acyl-D-glucosamine 2-epimerase
-
N-acylglucosamine 2-epimerase
-
Acylglucosamine 2-epimerase
-
-
-
-
Epimerase, acylglucosamine 2-
-
-
-
-
GlcNAc 2-epimerase
-
-
-
-
N-acetyl-D-glucosamine 2-epimerase
-
-
-
-
N-Acetylglucosamine 2-epimerase
-
-
-
-
Renin-binding protein
-
-
-
-
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N-Acyl-D-glucosamine 2-epimerase
Requires catalytic amounts of ATP.
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N-acetyl-D-glucosamine
N-acetyl-D-mannosamine
-
-
-
r
N-acetyl-D-mannosamine
N-acetyl-D-glucosamine
-
-
-
r
N-Acyl-D-glucosamine
N-Acyl-D-mannosamine
-
-
-
r
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N-acetyl-D-glucosamine
N-acetyl-D-mannosamine
-
-
-
r
N-Acyl-D-glucosamine
N-Acyl-D-mannosamine
-
-
-
r
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pyruvate
50% reduced activity at 0.2 M pyruvate
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ADP
20 fold increase in activity
AMPPNP
20 fold increase in activity
ATP
20 fold increase in activity, 0.020 mM for maximal activity
dATP
20 fold increase in activity
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Essential Hypertension
Association of Renin Binding Protein (RnBP) Gene Polymorphisms with Essential Hypertension in the Hani Minority of Southwestern China.
Hypertension
The expression of renin-binding protein and renin in the kidneys of rats with two-kidney one-clip hypertension.
Neoplasms
Modulation of active renin secretion by renin-binding protein (RnBP) in mouse pituitary AtT-20 cells transfected with human renin and RnBP cDNAs.
Neoplasms
Properties of renin-binding protein.
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5.2 - 45.7
N-acetyl-D-glucosamine
9.2 - 57.33
N-acetyl-D-mannosamine
5.2
N-acetyl-D-glucosamine
E242Q, reverse conversion in the presence of 1 mM ATP
7.4
N-acetyl-D-glucosamine
R375K, reverse conversion in the presence of 1 mM ATP
13.4
N-acetyl-D-glucosamine
E218D, reverse conversion in the presence of 1 mM ATP
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
24.4
N-acetyl-D-glucosamine
E218A, reverse conversion in the presence of 1 mM ATP
25.4
N-acetyl-D-glucosamine
wild type, reverse conversion in the presence of 1 mM ATP
45.7
N-acetyl-D-glucosamine
N179A, reverse conversion in the presence of 1 mM ATP
9.2
N-acetyl-D-mannosamine
R375K, in the presence of 1 mM ATP
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
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
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
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123.8
wild type, reverse conversion in the presence of 1 mM ATP
124
in the presence of 1 mM ATP
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
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
8.1
E242Q, in the presence of 1 mM ATP
8.9
R375K, reverse conversion in the presence of 1 mM ATP
85.9
C370A, reverse conversion in the presence of 1 mM ATP
94.3
R375K, in the presence of 1 mM ATP
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7 - 9.5
-
7 - 9.5
more than 90% of maximal activity
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35 - 55
more than 90% of maximal activity
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-
SWISSPROT
brenda
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A4UA16_9NOST
388
0
45062
TrEMBL
-
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42000
calculated, SDS-PAGE
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?
x * 42000, recombinant His-tagged enzyme, SDS-PAGE
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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
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
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of the recombinant protein by immobilized nickel-ion chromatography
of the recombinant proteins, wild type and mutants by immobilized nickel-ion chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, copurification with recombinant Escherichia coli N-acetyl-D-neuraminic acid aldolase
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expression in Escherichia coli
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)
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synthesis
recombinant Escherichia coli cells synchronously expressing N-acetyl-D-glucosamine-2-epimerase and N-acetyl-D-neuraminic acid aldolase as biocatalysts can potentially be used in the industrial mass production of Neu5Ac
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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
J. Biotechnol.
129
453-460
2007
Anabaena sp. CH1 (A4UA16), Sus scrofa (P17560), Sus scrofa
brenda
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.
367
895-908
2007
Anabaena sp. CH1 (A4UA16)
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.
65
7467-7475
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.
60
427-434
2018
Anabaena sp. CH1 (A4UA16)
brenda