ISSN:
0739-4462
Keywords:
intra- and extracellular enzymes
;
kinetic properties
;
inhibition
;
Chemistry
;
Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
Notes:
Kc-cells from Drosophila melanogaster, grown under serum-free conditions, produce two β-hexosaminidases and secrete these enzymes into the medium. The two enzymes were separated by DEAE-exchange chromatography. According to their substrate specificities one enzyme is a β-N-acetyl-D-glucosaminidase (E.C.3.2.1.30), the other one a β-N-acetyl-D-hexosaminidase (E.C.3.2.1.52). The β-N-acetyl-D-glucosaminidase is predominant in the medium, the β-N-acetyl-D-hexosaminidase within the cells. The Km values for the substrates pNP-GlcNAc, pNP-GalNAc, and (GlcNAc)2 are 0.8, 16.73, and 1.67 mM for the β-N-acetyl-D-glucosaminidase and 0.24, 0.44, and 0.2 mM for the β-N-acetyl-D-hexosaminidase. Both enzymes are inhibited by the products and the β-N-acetyl-D-glucosaminidase is also inhibited stereospecifically by the substrates pNP-GlcNAc and (GlcNAc)2. Both enzymes are inhibited in a partial competitive way by acetamidolactones, the Kis being as low as 0.1 μM.
Additional Material:
4 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/arch.940170103
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