5.1.3.8: N-acylglucosamine 2-epimerase
This is an abbreviated version!
For detailed information about N-acylglucosamine 2-epimerase, go to the full flat file.
Word Map on EC 5.1.3.8
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5.1.3.8
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n-acetylneuraminic
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neu5ac
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n-acetyl-d-neuraminic
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anabaena
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mannac
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takahashi
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n-acetyl-d-mannosamine
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renbp
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nal
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n-acetylmannosamine
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synthesis
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biotechnology
- 5.1.3.8
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n-acetylneuraminic
- neu5ac
-
n-acetyl-d-neuraminic
- anabaena
- mannac
-
takahashi
- n-acetyl-d-mannosamine
-
renbp
- nal
- n-acetylmannosamine
- synthesis
- biotechnology
Reaction
Synonyms
Acylglucosamine 2-epimerase, AGE, AGE2, anAGE, AvaAGE, bage, bGlcNAc 2-epimerase, Epimerase, acylglucosamine 2-, GlcNAc 2-epimerase, GlcNAc-2-epimerase, N-acetyl-D-glucosamine 2-epimerase, N-acetyl-D-glucosamine-2-epimerase, N-Acetylglucosamine 2-epimerase, N-acyl-D-glucosamine 2-epimerase, N-acylglucosamine 2-epimerase, PhGn2E, renin binding protein, Renin-binding protein, RNBP
ECTree
5.1.3.8 N-acylglucosamine 2-epimeraseAdvanced search results
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results (Activating Compound
Activating Compound on EC 5.1.3.8 - N-acylglucosamine 2-epimerase
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
renin
activates isozyme BoAGE2, unrelatedly with the unique native N-terminal tag, an addiional 27-amino acid tag sequence, detagged enzyme is also activated by renin. BoAGE2 can be considered a renin-binding protein
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additional information
no effects by nucleotides AMP, ADP, GMP, GDP, GTP, CMP, CTP, and UTP at 2 mM each
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ATP
activates isozyme AGE2, incubation with ATP stabilized its structure, raising its melting temperature by about 8 degrees
ATP
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allosteric activation, the enzyme shows 18% of maximal activity without ATP
ATP
stabilizes the dimeric form of the enzyme, inhibits the heterocomplex with renin, prevents inhibition by NEM, inhibits degradation of the enzyme by thermolysin
ATP
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allosteric activation, ATP has a more pronounced effect on the Km for the substrate than on the enzyme activity. The enzyme shows 20% of maximal activity without ATP. At high substrate concentrations of 200 mM and without ATP, the enzyme reaches up to 32% of the activity measured with ATP in excess
ATP
ATP is an allosteric activator of the epimerase, the binding of the nucleotide is crucial for its catalytic properties, binding kinetics of wild-type and mutant enzymes, overview
