Literature summary for 3.2.1.17 extracted from

Kawamura, S.; Ohkuma, M.; Chijiiwa, Y.; Kohno, D.; Nakagawa, H.; Hirakawa, H.; Kuhara, S.; Torikata, T.
Role of disulfide bonds in goose-type lysozyme (2008), FEBS J., 275, 2818-2830.

Search for more literature for 3.2.1.17

Cloned(Commentary)

Cloned (Comment)	Organism
amino acid Ser at the N-terminus	Struthio camelus

Protein Variants

Protein Variants	Comment	Organism
C18S/C29S	deletion of disulfide bond. No rearkable difference to wild-type in secondary structure or catalytic activity, but decrease in stability	Struthio camelus
C4S/C18S/C29S/C60S	deletion of both disulfide bonds. No rearkable difference to wild-type in secondary structure or catalytic activity, but decrease in stability. Optimum temperature of catalytic activity is dow-shifted by about 20 degrees	Struthio camelus
C4S/C60S	deletion of disulfide bond. No rearkable difference to wild-type in secondary structure or catalytic activity, but decrease in stability	Struthio camelus

Organism

Organism	UniProt	Comment	Textmining
Struthio camelus	-	ostrich	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
egg white	-	Struthio camelus	-

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	-	Struthio camelus	GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + (GlcNAc)2	main products	?

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
45.3	-	melting temperature, mutant C4S/C18S/C29S/C60S	Struthio camelus
46.2	-	melting temperature, reduced wild-type	Struthio camelus
51.1	-	melting temperature, mutant C4S/C60S	Struthio camelus
54.3	-	melting temperature, mutant C18S/C29S	Struthio camelus
60.6	-	melting temperature, wild-type	Struthio camelus

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Release 2023.1 (January 2023)