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Literature summary extracted from

  • Hirakawa, H.; Ochi, A.; Kawahara, Y.; Kawamura, S.; Torikata, T.; Kuhara, S.
    Catalytic reaction mechanism of goose egg-white lysozyme by molecular modelling of enzyme-substrate complex (2008), J. Biochem., 144, 753-761.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.17 modeling of complex with GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta Anser anser

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.17 Anser anser P00718
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.17 N,N',N'',N'''-tetraacetylchitotetraose + H2O = N,N',N''-triacetylchitotriose + N-acetyl-D-glucosamine crystallization data and molecular dynamics simulations indicate that lysozyme is an inverting enzyme, and Asp97 acts as a second carboxylate and that the narrow space of the binding cleft at subsites EĀ–G in GEL may prohibit the sugar chain to bind alternative site that might be essential for transglycosylation Anser anser
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.17 egg white
-
 Anser anser
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.17 GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + H2O
-
 Anser anser GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta
-
 ?