EC Number   |
General Information |
Reference |
|---|
   3.2.1.140 | more |
three realistic mechanistic alternatives exist for lacto-N-biosidases: substrate-assisted catalytic mechanism, or a mechanism involving the formation and breakdown of a covalent aglycosyl enzyme intermediate, or an inverting mechanism, overview. A key difference between these mechanistic alternatives is the involvement of the 2-acetamido group of the substrate. The lacto-N-biosidase-type enzyme uses a mechanism involving substrate-assisted catalysis from the 2-acetamido group of the substrate. Decrease in second-order rate constant, the carbonyl oxygen acts as a nucleophile, attacking the anomeric centre |
731652 |
| 3.2.1.140 | physiological function |
lacto-N-biosidase (LNBase), a beta-N-acetyl-hexosaminidase that liberates lacto-N-biose (LNB) from human milk oligosaccharides (HMOs), is important to the LNB pathway |
753245 |
| 3.2.1.140 | physiological function |
lacto-N-biosidase is a key enzyme that degrades lacto-N-tetraose, a main component of human milk oligosaccharides (HMOs, the third-most abundant solid component in human milk), into lacto-N-biose I and lactose. . Enzymatic release of beta-linked GNB from natural substrates, these unique activities may play a role in modulating the microbial composition in the gut ecosystem |
753153 |
| 3.2.1.140 | physiological function |
lacto-N-biosidase is a key enzyme that degrades lacto-N-tetraose, a main component of human milk oligosaccharides (HMOs, the third-most abundant solid component in human milk), into lacto-N-biose I and lactose. Enzymatic release of beta-linked Galbeta1-3GalNAc from natural substrates, these unique activities may play a role in modulating the microbial composition in the gut ecosystem |
753153 |
| 3.2.1.140 | physiological function |
the enzyme liberates lacto-N-biose I, the major core structure, from the nonreducing end of human milk oligosaccharides and plays a key role in the metabolic pathway of these compounds |
732092 |
