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Information on EC 5.1.3.8 - N-acylglucosamine 2-epimerase and Organism(s) Sus scrofa and UniProt Accession P17560
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5.1.3.8 N-acylglucosamine 2-epimeraseIUBMB Comments
Requires catalytic amounts of ATP.
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Word Map
- 5.1.3.8
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n-acetylneuraminic
- neu5ac
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n-acetyl-d-neuraminic
- anabaena
- mannac
-
takahashi
- n-acetyl-d-mannosamine
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renbp
- nal
- n-acetylmannosamine
- synthesis
- biotechnology
The taxonomic range for the selected organisms is: Sus scrofa
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
RNBP
inhibits activity of renin, forms heterocomplex with renin, high molecular weight renin, HMW
Acylglucosamine 2-epimerase
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-
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Epimerase, acylglucosamine 2-
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-
-
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GlcNAc 2-epimerase
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-
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N-acetyl-D-glucosamine 2-epimerase
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-
-
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N-Acetylglucosamine 2-epimerase
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-
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Renin-binding protein
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-
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RNBP
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
epimerization
epimerization
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SYSTEMATIC NAME
IUBMB Comments
N-Acyl-D-glucosamine 2-epimerase
Requires catalytic amounts of ATP.
CAS REGISTRY NUMBER
COMMENTARY
37318-34-6
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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
N-Acyl-D-glucosamine
N-Acyl-D-mannosamine
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also catalyzes epimerization of the corresponding N-glycolyl derivatives
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?
additional information
?
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involved in biosynthesis of N-acetylneuraminic acid
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-
?
additional information
?
-
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involved in biosynthesis of N-acetylneuraminic acid
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-
?
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
additional information
?
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involved in biosynthesis of N-acetylneuraminic acid
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-
?
additional information
?
-
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involved in biosynthesis of N-acetylneuraminic acid
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
not essential for reaction, but 20fold enhancement of activity, Km: 0.018 mM
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-ethylmaleimide
NEM, strong inhibitor in absence of ATP at 0.1-0.3 mM, at 5mM inhibition also in presence of ATP
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
stabilizes the dimeric form of the enzyme, inhibits the heterocomplex with renin, prevents inhibition by NEM, inhibits degradation of the enzyme by thermolysin
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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)
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)
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)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.3 - 8.3
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6.3: about 50% of maximal activity, 8.3: about 80% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). RENBP_PIG
402
0
46402
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, structure determination by the multiple isomorphous replacement method
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20 mM potassium phosphate buffer, pH 7.6, 1.0 mM EDTA, 0.05% 2-mercaptoethanol, 5.0% sucrose, stable for at least 6 months
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
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, a two-step enzymatic system involving immobilized both enzymes is used for the conversion of GlcNAc to NeuAc in a single reactor, optimum ratio is 3-6.25 U/ml of N-acetyl-D-glucosamine-2-epimerase and 12.5-25 U/ml of N-acetyl-D-neuraminic acid lyase
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Datta, A.
N-Acetylglucosamine 2-epimerase from hog kidney
Methods Enzymol.
41
407-412
1975
Sus scrofa
Ghosh, S.; Roseman, S.
N-Acetylglucosamine 2-epimerase from hog kidney
Methods Enzymol.
8
191-195
1966
Sus scrofa
-
Ghosh, S.; Roseman, S.
The sialic acids. V. N-Acyl-D-glucosamine 2-epimerase
J. Biol. Chem.
240
1531-1536
1965
Sus scrofa
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
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
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
J. Mol. Biol.
303
733-744
2000
Sus scrofa
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.
140
725-730
2006
Sus scrofa (P17560), Sus scrofa
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
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)
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