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Literature summary for 5.4.99.9 extracted from

  • Poulin, M.B.; Shi, Y.; Protsko, C.; Dalrymple, S.A.; Sanders, D.A.; Pinto, B.M.; Lowary, T.L.
    Specificity of a UDP-GalNAc pyranose-furanose mutase: a potential therapeutic target for Campylobacter jejuni infections (2014), ChemBioChem, 15, 47-56.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-alpha-D-galactopyranose Campylobacter jejuni
-
UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose Campylobacter jejuni 11168
-
UDP-alpha-D-galactofuranose
-
r
UDP-N-acetyl-2-deoxy-2-amino-alpha-D-galactopyranose Campylobacter jejuni
-
UDP-N-acetyl-2-deoxy-2-amino-alpha-D-galactofuranose
-
r
UDP-N-acetyl-2-deoxy-2-amino-alpha-D-galactopyranose Campylobacter jejuni 11168
-
UDP-N-acetyl-2-deoxy-2-amino-alpha-D-galactofuranose
-
r

Organism

Organism UniProt Comment Textmining
Campylobacter jejuni
-
-
-
Campylobacter jejuni 11168
-
-
-

Reaction

Reaction Comment Organism Reaction ID
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose catalytic mechanism, overview Campylobacter jejuni

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the bifunctional pyranose-furanose mutase recognizes both UDP-Gal and UDP-GalNAc Campylobacter jejuni ?
-
?
additional information the bifunctional pyranose-furanose mutase recognizes both UDP-Gal and UDP-GalNAc Campylobacter jejuni 11168 ?
-
?
UDP-alpha-D-galactopyranose
-
Campylobacter jejuni UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose
-
Campylobacter jejuni 11168 UDP-alpha-D-galactofuranose
-
r
UDP-N-acetyl-2-deoxy-2-amino-alpha-D-galactopyranose
-
Campylobacter jejuni UDP-N-acetyl-2-deoxy-2-amino-alpha-D-galactofuranose
-
r
UDP-N-acetyl-2-deoxy-2-amino-alpha-D-galactopyranose
-
Campylobacter jejuni 11168 UDP-N-acetyl-2-deoxy-2-amino-alpha-D-galactofuranose
-
r

Synonyms

Synonyms Comment Organism
UNGM
-
Campylobacter jejuni

Cofactor

Cofactor Comment Organism Structure
FAD
-
Campylobacter jejuni

General Information

General Information Comment Organism
evolution the enzyme is a member of the UGM family Campylobacter jejuni
additional information enzyme-substrate binding analysis by combination of UV/visible spectroscopy, X-ray crystallography, saturation transfer difference NMR spectroscopy, molecular dynamics, and CORCEMA-ST calculations. Two arginines in the enzyme, Arg59 and Arg168, play critical roles in the catalytic mechanism of the enzyme and in controlling its specificity to ultimately lead to an N-acetyl-alpha-D-galactofuranose-containing capsular polysaccharides. Substrate-recognition patterns compared to the Eschericia coli enzyme, overview Campylobacter jejuni
physiological function the enzyme is involved in the biosynthesis of capsular polysaccharides in Campylobacter jejuni 11168. These capsular polysaccharides are known virulence factors that are required for adhesion and invasion of human epithelial cells. Production of suitable quantities of the sugar nucleotide substrate required for the assembly of a capsular polysaccharide containing N-acetyl-alpha-D-galactofuranose, which is essential for viability Campylobacter jejuni