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Information on EC 5.1.3.8 - N-acylglucosamine 2-epimerase and Organism(s) Homo sapiens
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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: Homo sapiens
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, renin binding protein, n-acyl-d-glucosamine 2-epimerase, n-acetylglucosamine 2-epimerase, avaage, bglcnac 2-epimerase, n-acylglucosamine 2-epimerase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
N-acetyl-D-glucosamine 2-epimerase
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-
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N-Acetylglucosamine 2-epimerase
Renin-binding protein
RNBP
GlcNAc 2-epimerase
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-
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N-Acetylglucosamine 2-epimerase
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Renin-binding protein
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-
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RNBP
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N-acyl-D-glucosamine = N-acyl-D-mannosamine
various amino acid residues of the enzyme are involved in the reaction mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
epimerization
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-
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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-acetyl-D-mannosamine
N-acetyl-D-glucosamine
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the enzyme can serve a catabolic role, diverting metabolic flux from the sialic acid pathway
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?
additional information
?
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no activity with mannosamine, glucosamine, mannose, glucose and N-acetyl-galactosamine
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?
additional information
?
-
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the enzyme inhibits porcine renin activity through formation of a complex of porcine renin with the recombinant enzyme, the so-called high-molecular-weight renin
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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
N-acetyl-D-mannosamine
N-acetyl-D-glucosamine
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the enzyme can serve a catabolic role, diverting metabolic flux from the sialic acid pathway
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
renin
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the 1:1 renin/enzyme complex has only 2% of the activity of the free enzyme
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
mammalian enzyme requires the presence of nucleotide activators and cofactors, while the bacterial enzyme are activated by nucleotide binding, but do not require them as cofactors
metabolism
the biosynthesis of N-acetyl-D-mannosamine can be regulated in amammals in two different ways. In the liver, UDP-GlcNAc is epimerized to UDP-ManNAc by the bifunctional UDP-GlcNAc 2-epimerase, while in the kidney (mostly), GlcNAc is directly epimerized to ManNac by GlyNAc 2-epimerase
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_HUMAN
427
0
48831
Swiss-Prot
other Location (Reliability: 2)
A6NKZ2_HUMAN
413
0
47066
TrEMBL
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C125S
C125S/C210S
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mutant enzyme shows 54.8% of the activity relative to the wild-type enzyme
C125S/C210S/C239S
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mutant enzyme shows 49.3% of the activity relative to the wild-type enzyme
C125S/C210S/C239S/C203S
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mutant enzyme shows 28.7% of the activity relative to the wild-type enzyme
C125S/C210S/C239S/C203S/C386S
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mutant enzyme shows 23.8% of the activity relative to the wild-type enzyme
C125S/C386S
-
mutant enzyme shows 68.7% of the activity relative to the wild-type enzyme
C125S/C390S
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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
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mutant enzyme shows 88.7% of the activity relative to the wild-type enzyme
C210S/C390S
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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
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mutant enzyme shows 116% of the activity relative to the wild-type enzyme
C239S/C390S
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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
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mutant enzyme shows 65.8% of the activity relative to the wild-type enzyme
C302S/C390S
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mutant enzyme shows 7.4% of the activity relative to the wild-type enzyme
C386S
C390S
C41S
C41S/C125S
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mutant enzyme shows 17.7% of the activity relative to the wild-type enzyme
C41S/C125S/C210S
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mutant enzyme shows 28.1% of the activity relative to the wild-type enzyme
C41S/C125S/C210S/C239S
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mutant enzyme shows 9.7% of the activity relative to the wild-type enzyme
C41S/C386S
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mutant enzyme shows 0.7% of the activity relative to the wild-type enzyme
C66S
C66S/C125S
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mutant enzyme shows 39.4% of the activity relative to the wild-type enzyme
C66S/C125S/C210S
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mutant enzyme shows 23.9% of the activity relative to the wild-type enzyme
C66S/C125S/C210S/C239S
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mutant enzyme shows 58.4% of the activity relative to the wild-type enzyme
C66S/C125S/C210S/C239S/C302S
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mutant enzyme shows 15.5% of the activity relative to the wild-type enzyme
C66S/C386S
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mutant enzyme shows 113% of the activity relative to the wild-type enzyme
C66S/C390S
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mutant enzyme shows 14.4% of the activity relative to the wild-type enzyme
DELTA400-417
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C-terminal deletion mutant has approximately 50% activity relative to the wild-type enzyme
additional information
C125S
-
relative specific activity in the extract is nearly the same to that of the wild-type enzyme
C386S
-
relative specific activity in the extract is nearly the same to that of the wild-type enzyme
C390S
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relative specific activity in the extract is nearly the same to that of the wild-type enzyme
C41S
-
relative specific activity in the extract is nearly the same to that of the wild-type enzyme
C66S
-
relative specific activity in the extract is nearly the same to that of the wild-type enzyme
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
hydrolysis of wild-type and mutant enzymes by thermolysin in absence of ATP, no hydrolysis in presence of ATP
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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construction of several C-terminal deletion and multi-cysteine/serine mutants and expression in Escherichia coli
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expressed in Escherichia coli JM109 under the transcriptional control of taq promoter
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expression of wild-type enzyme and mutant enzymes C41S, C66S, C104S, C125S, C210S, C239S, C302S, C380S, C386S and C390S in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
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production of N-acetylneuraminic acid from N-acetylglucosamine and pyruvate using recombinant human renin binding protein showing GlcNAc-2-epimerase activity and sialic acid aldolase in a coupling reaction
additional information
the mammalian enzyme is a target for development inhibitors for sialic acid biosynthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
J. Biochem.
129
529-535
2001
Homo sapiens
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)
J. Biochem.
131
605-610
2002
Homo sapiens, Rattus norvegicus
Luchansky, S.J.; Yarema, K.J.; Takahashi, S.; Bertozzi, C.R.
GlcNAc 2-epimerase can serve a catabolic role in sialic acid metabolism
J. Biol. Chem.
278
8035-8042
2003
Homo sapiens
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.
35
121-125
2004
Homo sapiens
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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
6
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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