EC Number |
Substrates |
Products |
Reversibility |
---|
5.1.3.7 | more |
two genes, galEsp1 and galEsp2, are responsible for galactose metabolism in pathogenic Streptococcus pneumoniae TIGR4. Both GalESp1 and GalESp2 catalyze the epimerization of UDP-Glc/UDP-Gal, EC 5.1.3.2, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc. Enzyme GalESp2 has a 3fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1. GalESp2 can convert both UDP-Glc/UDP-Gal and UDP-GlcNAc/UDP-GalNAc with conversion ratios of 29% and 28% for the UDP-Glc and UDP-GlcNAc substrates |
? |
- |
? |
5.1.3.7 | UDP-alpha-D-galactose |
- |
UDP-alpha-D-glucose |
- |
r |
5.1.3.7 | UDP-alpha-D-glucose |
epimerization at 36.2% compared to the activity with UDP-alpha-D-galactose |
UDP-alpha-D-galactose |
- |
r |
5.1.3.7 | UDP-D-glucose |
- |
UDP-D-galactose |
- |
r |
5.1.3.7 | UDP-D-glucose |
the achieved reasonable conversion rates the amount of enzyme used is increased 200fold comparted to UDP-N-acetyl-D-glucosamine as substrate. Substrate conversions reach 20% for UDP-Glc and 65% for UDP-Gal |
UDP-D-galactose |
- |
r |
5.1.3.7 | UDP-D-glucose |
the enzyme provides Gal and galNAc residues for the synthesis of the cell-surface carbohydrates in Campylobacter jejuni NCTC 11168 |
UDP-D-galactose |
- |
r |
5.1.3.7 | UDP-D-glucose |
unlike the wild-type enzyme the mutant enzyme is more efficient in catalyzing the reaction with the non-acetylated hexoses UDP-Glc and UDP-Gal than in catalyzing epimerization of UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine |
UDP-D-galactose |
- |
r |
5.1.3.7 | UDP-GlcNAc |
- |
UDP-GalNAc |
- |
r |
5.1.3.7 | UDP-glucose |
- |
UDP-galactose |
- |
r |
5.1.3.7 | UDP-N-acetyl-alpha-D-galactosamine |
epimerization at 48.5% compared to the activity with UDP-alpha-D-galactose |
UDP-N-acetyl-alpha-D-glucosamine |
- |
r |