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Literature summary for 3.2.1.17 extracted from

  • Nonaka, Y.; Aizawa, T.; Akieda, D.; Yasui, M.; Watanabe, M.; Watanabe, N.; Tanaka, I.; Kamiya, M.; Mizuguchi, M.; Demura, M.; Kawano, K.
    Spontaneous asparaginyl deamidation of canine milk lysozyme under mild conditions (2008), Proteins, 72, 313-322.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of mutant N44Q/N47Q/N49Q/N68Q/N103Q is substantially identical to that of the wild type, and the substitutions of Asn to Gln are appropriate for the folding and structural analyses of this protein Canis lupus familiaris

Protein Variants

Protein Variants Comment Organism
N44Q/N47Q/N49Q/N103Q mutant construcuted for study of charge heterogeneity caused by asparaginyl deamidation. Residues Asn 44, 47, 49, and 68 are the deamidation sites Canis lupus familiaris
N44Q/N47Q/N49Q/N68Q mutant construcuted for study of charge heterogeneity caused by asparaginyl deamidation. Residues Asn 44, 47, 49, and 68 are the deamidation sites Canis lupus familiaris
N44Q/N47Q/N49Q/N68Q/N103Q mutant construcuted for study of charge heterogeneity caused by asparaginyl deamidation. Residues Asn 44, 47, 49, and 68 are the deamidation sites. Decrease in lytic activity by a factor 20 compared with wild-type Canis lupus familiaris
N44Q/N47Q/N68Q/N103Q mutant construcuted for study of charge heterogeneity caused by asparaginyl deamidation. Residues Asn 44, 47, 49, and 68 are the deamidation sites Canis lupus familiaris
N44QN49Q/N68Q/N103Q mutant construcuted for study of charge heterogeneity caused by asparaginyl deamidation. Residues Asn 44, 47, 49, and 68 are the deamidation sites Canis lupus familiaris
N47Q/N49Q/N68Q/N103Q mutant construcuted for study of charge heterogeneity caused by asparaginyl deamidation. Residues Asn 44, 47, 49, and 68 are the deamidation sites Canis lupus familiaris

Organism

Organism UniProt Comment Textmining
Canis lupus familiaris
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Purification (Commentary)

Purification (Comment) Organism
canine milk lysozyme exhibits charge heterogeneity after sample purification. Four Asn residues deamidate rapidly under mild conditions of pH 8.0 and 30°C. One Asn residue, which is stable in the native state, is labile to deamidation in the unfolded state Canis lupus familiaris

Source Tissue

Source Tissue Comment Organism Textmining
milk
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Canis lupus familiaris
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