Molecular basis for the functional diversity of enzyme forms of the LMW (Mr 38,000) acid phosphatase of the frog liver.
Recent studies on the structure and function of the tartrate-resistant acid phosphatase (Mr 38,000) of the frog liver are reviewed. The nature of the enzyme heterogeneity is elucidated on a molecular and physiological basis. The following structure-activity relationship is proposed: the enzyme protein is modified by glycosylation processes leading to formation of the different enzyme forms. The oligosaccharide chain stabilizes the final structure of the enzyme forms with altered conformation causing different exposure of the essential functional groups (e.g. sulfhydryl residues, antigen determinants). This leads to different physiological events necessary for fulfillment of metabolic requirements of the cell.
Kubicz
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Institute of Biochemistry, University of Wrocław.
D000135:Acid Phosphatase / Q000737:chemistry* / Q000302:isolation & purification; D000818:Animals; D002241:Carbohydrates / Q000737:chemistry; D006031:Glycosylation; D007120:Immunochemistry; D007527:Isoenzymes / Q000737:chemistry* / Q000302:isolation & purification; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D011506:Proteins / Q000737:chemistry; D011898:Ranidae; D013329:Structure-Activity Relationship
D002241:Carbohydrates; D007527:Isoenzymes; D011506:Proteins; D000135:Acid Phosphatase