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Lysosomal degradation of heparan sulfate. Dark arrows indicate the site of action of the enzyme, which is listed in italics. Mucopolysaccharidoses due to a deficiency of the indicated enzymes are listed in bold to the right of the enzyme.

Lysosomal degradation of selected glycosphingolipids. The sphingolipid activator proteins necessary for in vivo degradation are indicated. SAP, sphingolipid activator protein.

Lysosomal Digestive Pathways for Glycosaminoglycans. Each structure represents a type of repeating unit in the particular polysaccharide. Enzyme names with corresponding numbers are given in Table 2. A slash between two enzyme numbers indicates either reaction can precede the other.

Lysosomal Digestive Pathways for Sphingolipids. Enzyme names with corresponding numbers are given in Table 3.

Lysosomal handling of cystine . Cys-SH, cysteine CyNH2-SS-CySy mixed disulfide GSH, reduced glutathione G-SS-G, oxidized glutathione

Lysosomal reactions. Most lysosomal enzymes are hydrolases, which cleave peptide, ester, and glycosidic bonds by adding the components of water across the bond. These enzymes are active at the acidic pH of the lysosome and inactive if accidentally released into the cytosol.

Lysosome with lipids.

Lysosomes and phagocytosis. Dead and foreign material are removed via phagocytosis and degradation of macromolecular material using lysosomal enzymes.

Lysosomes in receptor-mediated endocytosis via clathrin-coated pits. 1 Endo-cytotic vesicles fuse to form early endosomes. 2 Vesicle contents are sorted, and receptors, clathrin, and lipids are sent back to the plasma membrane. 3 Transport vesicles from the trans-Golgi carry lysosomal hydrolases to the late endosome. 4 Lysosomes containing concentrated hydrolases digest proteins and other components acquired from endocytotic vesicles.

Lysozyme a. Ball-and-stick model

Lysozyme from hen egg-white showing the amino-acid sequence .

Lysozyme mechanism for hydrolysis of the substrate jS-cel lob iosyl fluoride A is a modified reactive substrate which yields a weakly reactive acylal intermediate.

Lysozyme mechanism.

Lysozyme solubility in aqueous solutions of magnesium chloride at pH 4.1. The solid line rcpresents die prediction based on Eq. are the experimental data from Ref. .

Lysozyme solubility in aqueous solutions of sodium acetate at pH 8.3. The solid line represents the prediction based on Eq. are the experimental data from Ref .

Lysozyme solubility in aqueous solutions of sodium chloride at pH 4.5. The solid line represents the prediction based on Eq. are the experimental data from Refs. , respectively.

Lysozyme solubility in aqueous solutions of sodium chloride at pH 6.5. The solid line represents the prediction based on Eq. are the experimental data from Ref. .

Lysozyme stimulated pinocytosis in Amoeba proteus. Changes in heat output due to different lysozyme concentrations . The baseline is indicated before the arrow, A represents the basic metabolism, B the heat output during pinocytosis ,

Lysozyme surface imprint incorporating lysozyme from solution and analyte re-

Lysozyme synthesis in E. coli Bg. infected with T7 and various T7 gene 1 mutants. E.coli Bg i were grown at 30 in M9 . Dr. Hausmann s mutants were found to be protein kinase negative

Lysozyme, Hydrolysis reaction catalyzed by lysozyme

Lysozyme-morphine conjugation scheme

LysU half-of-sites binding of ATP and half-of-sites reactivity

Lysyl oxidase. The enzyme, lysyl oxidase, appears to seek out lysyl residues in alanyl- and lysyl-rich regions in the pro fibrillar forms of elastin. The presence of an aromatic amino acid residue adjacent to lysine appears to block its oxidation. The product of oxidation is peptidyl a-aminoadipic-S-semialdehyde. Assays for the enzyme against elastin involve first the preparation of an elastin-rich pellet containing 3H-lysyl residues labeled in the 6 or 4,5 position. This is usually accomplished by incubating embryonic chick aortas in medium containing 3H-lysine plus f3-aminopropionitrile to inhibit endogenous lysyl oxidase activity. BAPN is then removed leaving behind an elastin-rich residue in which the profibrillar forms of elastin labelled with 3H-lysine are only partially crosslinked. When lysyl oxidase preparations are added to this residue the release of tritium represents the assay for activity. It has also been demonstrated that tropoelastin, when incubated with lysyl oxidase, forms a-aminoadipic-S-semialdehyde and eventually crosslinks as shown in

Lythraceous quinolizidine alkaloids and analogs.



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