PMID: 42541Dec 1, 1979

A pathway of polygalactosamine formation in Aspergillus parasiticus: enzymatic deacetylation of N-acetylated polygalactosamine

European Journal of Biochemistry
Y ArakiE Ito

Abstract

1. An enzyme which hydrolyzes the acetamido groups of N-acetylgalactosamine residues in N-acetylated polygalactosamine was found in the supernatant fraction of Aspergillus parasiticus AHU 7165, a polygalactosamine-producing strain. 2. N-Acetylated polygalactosamine was used as a substrate in the purification and characterization of this enzyme. A 140-fold purification was obtained by means of ammonium sulfate fractionation followed by chromatography on carboxymethylcellulose and DEAE-cellulose. 3. The enzyme releases about 60-70% of the acetyl groups of N-acetylated polygalactosamine, giving a product with free amino groups. Whereas the enzyme also deacetylates oligosaccharides with 14 or more N-acetylgalactosamine units at a rate similar to that of deacetylation of the polymer, it deacetylates shorter oligosaccharides (trimer to hexamer of N-acetylgalactosamine) much more slowly and is virtually inactive toward disaccharide. Deacetylation can not be detected with bacterial cell wall peptidoglycan, N-acetylated heparin, partially O-hydroxyethylated chitin or monomeric N-acetylgalactosamine derivatives as substrates. 4. This enzyme shows double pH optima of 5.3 and 9.3. The Km value for N-acetylated poly-galactosamine is 0.15 g/...Continue Reading

Citations

Jun 16, 1975·European Journal of Biochemistry·Y Araki, E Ito
Jun 1, 1971·Journal of Bacteriology·J L Reissig, J E Glasgow
Nov 5, 1971·Biochemical and Biophysical Research Communications·Y ArakiE Ito
Feb 4, 1974·Biochemical and Biophysical Research Communications·Y Araki, E Ito
Mar 26, 1962·Biochimica Et Biophysica Acta·S BARTNICKI-GARCIA, W J NICKERSON

Related Concepts

Biochemical Pathway
Heparin
Derivatives
Aspergillus parasiticus
Chromatography
Disaccharides
Acetylgalactosamine
Supernatant
DEAE-Cellulose
Substrate Specificity

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