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Literature summary for 3.2.1.17 extracted from

  • Kawamura, S.; Chijiiwa, Y.; Minematsu, T.; Fukamizo, T.; Varum, K.M.; Torikata, T.
    The role of Arg114 at subsites E and F in reactions catalyzed by hen egg-white lysozyme (2008), Biosci. Biotechnol. Biochem., 72, 823-832.
    View publication on PubMed

Protein Variants

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

Organism UniProt Comment Textmining
Gallus gallus P00698
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-

Substrates and Products (Substrate)

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 ?
-
?