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Lysozyme-like protein 6 (LYZL6) is a member of the c-type lysozyme/alpha-lactalbumin family, which are enzymes primarily known for their bacteriolytic function by hydrolyzing peptidoglycan in bacterial cell walls. LYZL6 displays the canonical catalytic residues that confer lysozyme activity (Glu35 and Asp52), and has been demonstrated to possess in vitro antibacterial activity against Gram-positive bacteria, with maximal activity at acidic pH. Expression studies in mice and humans indicate that LYZL6 is localized in the testis and epididymis and is present on the post-acrosomal area and midpiece of mature spermatozoa, suggesting roles in sperm-egg binding, mitochondrial function, and innate immunity in the male reproductive tract. There is no evidence to suggest it is a receptor, druggable target, or associated with any human disease as a biomarker or therapeutic safety concern. Protein sequence and phylogenetic analysis confirm that LYZL6 shares structural motifs and substrate binding residues with other c-type lysozyme family members, while displaying distinct tissue-specific functions.
Not applicable; no drugs target LYZL6.
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