Papaya (Carica papaya) lysozyme is a member of the family 19 (basic, class II) chitinases.
The most comprehensive studies on a plant lysozyme (EC 3.2.1.17) are those on the enzyme from papaya (Carica papaya) latex, published in 1967 and 1969. However, the N-terminal amino acid sequence of five amino acid sequence of this enzyme, determined by manual Edman degradation, did not allow assignment to any of the much later-classified families of glycosyl hydrolases. N-Terminal sequence analysis of 22 residues of papaya lysozyme now shows unambiguously that the enzyme belongs to the family 19 chitinases. It has properties similar to those of basic class I chitinases with lysozyme activity, such as cleavage specificity at the C-1 of N-acetylmuramic acid with inversion of configuration, but as it lacks an N-terminal hevein domain, it should be classified as a class II chitinase.
Subroto
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Sufiati
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Beintema
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D000595:Amino Acid Sequence; D002688:Chitinases / Q000737:chemistry* / Q000145:classification* / Q000302:isolation & purification; D016208:Databases, Factual; D019143:Evolution, Molecular; D019684:Magnoliopsida / Q000201:enzymology; D008969:Molecular Sequence Data; D009113:Muramidase / Q000737:chemistry* / Q000145:classification* / Q000302:isolation & purification; D019685:Rosales / Q000201:enzymology*; D020539:Sequence Analysis, Protein; D017386:Sequence Homology, Amino Acid
D002688:Chitinases; D009113:Muramidase