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Comparative Study
. 1990 Jun 15;169(2):751-7.
doi: 10.1016/0006-291x(90)90395-4.

Action of endo-alpha-N-acetylgalactosaminidase from Alcaligenes sp. on amino acid-O-glycans: comparison with the enzyme from Diplococcus pneumoniae

J Q Fan  1 , K Yamamoto, Y Matsumoto, Y Hirabayashi, H Kumagai, T Tochikura
Affiliations
Comparative Study

Action of endo-alpha-N-acetylgalactosaminidase from Alcaligenes sp. on amino acid-O-glycans: comparison with the enzyme from Diplococcus pneumoniae

J Q Fan et al. Biochem Biophys Res Commun. .

Abstract

Endo-alpha-N-acetylgalactosaminidase from Alcaligenes sp. released the disaccharide, Gal beta 1----3GalNAc, from both dansylated serine-GalNAc-Gal and threonine-GalNAc-Gal, and showed higher activity on the former than the latter. The Km values were 0.17 mM and 1.43 mM with DNS-Ser-GalNAc-Gal and DNS-Thr-GalNAc-Gal, respectively. The optimum pHs were found to be 4.5-7.5 and 4.5-6.0 on DNS-Ser-GalNAc-Gal and DNS-Thr-GalNAc-Gal, respectively. On the contrary, the enzyme from Diplococcus pneumoniae had low activity to release the disaccharide from the amino acid-O-glycans. The possibility that the same O-glycoside but linked to different aglycon amino acids may play a different biological role in glycoproteins is discussed.

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