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Literature summary for 5.1.3.8 extracted from

  • 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 (2016), Catalysts, 6, 212-228 .
No PubMed abstract available
Search for more literature for 5.1.3.8

Activating Compound

Activating Compound Comment Organism Structure
ATP over 4fold activation at 2 mM Pedobacter heparinus
additional information no effects by nucleotides AMP, ADP, GMP, GDP, GTP, CMP, CTP, and UTP at 2 mM each Pedobacter heparinus

Application

Application Comment Organism
additional information the mammalian enzyme is a target for development inhibitors for sialic acid biosynthesis Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
2-mercaptoethanol 30% inhibition at 10 mM, 40% at 100 mM Pedobacter heparinus
SDS 40% inhibition at 1% Pedobacter heparinus
Triton X-100 30% inhibition at 0.1%, 20% at 1% Pedobacter heparinus
Urea 50% inhibition at 2 M, 10% at 1 M Pedobacter heparinus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N-acetyl-D-glucosamine Homo sapiens
-
 N-acetyl-D-mannosamine
-
 r
N-acetyl-D-glucosamine Pedobacter heparinus
-
 N-acetyl-D-mannosamine
-
 r
N-acetyl-D-glucosamine Pedobacter heparinus ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3
-
 N-acetyl-D-mannosamine
-
 r
N-Acyl-D-glucosamine Homo sapiens
-
 N-Acyl-D-mannosamine
-
 r
N-Acyl-D-glucosamine Pedobacter heparinus
-
 N-Acyl-D-mannosamine
-
 r
N-Acyl-D-glucosamine Pedobacter heparinus ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3
-
 N-Acyl-D-mannosamine
-
 r

Organism

Organism UniProt Comment Textmining
Homo sapiens P51606
-
-
Pedobacter heparinus C6Y403
-
-
Pedobacter heparinus ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3 C6Y403
-
-

Reaction

Reaction Comment Organism Reaction ID
N-acyl-D-glucosamine = N-acyl-D-mannosamine various amino acid residues of the enzyme are involved in the reaction mechanism Homo sapiens
a
N-acyl-D-glucosamine = N-acyl-D-mannosamine various amino acid residues of the enzyme are involved in the reaction mechanism Pedobacter heparinus
a

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-acetyl-D-glucosamine
-
 Homo sapiens N-acetyl-D-mannosamine
-
 r
N-acetyl-D-glucosamine
-
 Pedobacter heparinus N-acetyl-D-mannosamine
-
 r
N-acetyl-D-glucosamine
-
 Pedobacter heparinus ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3 N-acetyl-D-mannosamine
-
 r
N-Acyl-D-glucosamine
-
 Homo sapiens N-Acyl-D-mannosamine
-
 r
N-Acyl-D-glucosamine
-
 Pedobacter heparinus N-Acyl-D-mannosamine
-
 r
N-Acyl-D-glucosamine
-
 Pedobacter heparinus ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3 N-Acyl-D-mannosamine
-
 r

Synonyms

Synonyms Comment Organism
GlcNAc 2-epimerase
-
 Homo sapiens
GlcNAc 2-epimerase
-
 Pedobacter heparinus
N-Acetylglucosamine 2-epimerase
-
 Homo sapiens
N-Acetylglucosamine 2-epimerase
-
 Pedobacter heparinus
PhGn2E
-
 Pedobacter heparinus

Cofactor

Cofactor Comment Organism Structure
NTP
-
 Homo sapiens

General Information

General Information Comment Organism
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 Homo sapiens
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 Pedobacter heparinus
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 Homo sapiens