Protein Variants | Comment | Organism |
---|---|---|
R114A | decrease in activity toward substrate glycol chitin to 80.5%. Reduction of binding free enrgies of E-F sites and the rate constant of transglycosylation for substrate GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta is about 50% of wild-type. Structural changes induced by the mutation are extended to aromatic side chains of F34 and W123 | Gallus gallus |
R114H | decrease in activity toward substrate glycol chitin to 79%. Reduction of binding free enrgies of E-F sites and the rate constant of transglycosylation for substrate GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta. Structural changes induced by the mutation are extended to aromatic side chains of F34 and W123 | Gallus gallus |
R114L | no decrease in activity toward substrate glycol chitin. Reduction of binding free enrgies of E-F sites and the rate constant of transglycosylation for substrate GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta | Gallus gallus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Gallus gallus | P00698 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + H2O | - |
Gallus gallus | GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + ? | - |
? | |
glycol chitin + H2O | - |
Gallus gallus | ? | - |
? |