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 | UniProt | Comment | Textmining |
---|---|---|---|
Campylobacter jejuni | - |
- |
- |
Campylobacter jejuni 11168 | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose | catalytic mechanism, overview | Campylobacter jejuni |
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 | Comment | Organism |
---|---|---|
UNGM | - |
Campylobacter jejuni |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Campylobacter jejuni |
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 |