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Literature summary extracted from

  • Tsuchiya, Y.; Morioka, K.; Yoshida, K.; Shirai, J.; Kokuho, T.; Inumaru, S.
    Effect of N-terminal mutation of human lysozyme on enzymatic activity (2007), Nucleic Acids Symp. Ser., 51, 465-466.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.17 _K1insA the pH-profile is almost the same as that of native enzyme Homo sapiens
3.2.1.17 _K1insK the optimal pH-range is extended to higher pH-values in comparison to wild-type enzyme and mutant enzyme _K1insN. The mutant enzyme has significantly higher activity than native enzyme and _K1insN in higher ionic strength and in 150 mM NaCl. The mutant enzyme may be a useful antimicrobial agent Homo sapiens
3.2.1.17 _K1insL the pH-profile is almost the same as that of native enzyme Homo sapiens
3.2.1.17 _K1insN the pH-profile is almost the same as that of native enzyme Homo sapiens
3.2.1.17 _K1insV the pH-profile is almost the same as that of native enzyme Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.17 Homo sapiens
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.17 peptidoglycan + H2O Micrococcus lysodeikticus cells Homo sapiens ?
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.17 6
-
 native enzyme and mutant enzyme _K1insN Homo sapiens
3.2.1.17 7
-
 mutant _K1insK Homo sapiens

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.17 6.5 8.5 from pH 6.5-8.5, the rising of the pH results in decrease in lytic activity of native enzyme and mutant _K1insK, but not _K1insK Homo sapiens