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Literature summary for 3.2.1.17 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)

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

Organism

Organism UniProt Comment Textmining
Anser anser P00718
-
-

Reaction

Reaction Comment Organism Reaction ID
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

Source Tissue

Source Tissue Comment Organism Textmining
egg white
-
Anser anser
-

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(1-4)GlcNAcbeta + H2O
-
Anser anser GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta
-
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