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Literature summary extracted from

  • Araki, Y.; Takada, H.; Fujii, N.; Ito, E.
    A pathway of polygalactosamine formation in Aspergillus parasiticus: enzymatic deacetylation of N-acetylated polygalactosamine (1979), Eur. J. Biochem., 102, 35-42.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.58 Ca2+ stimulates, optimal concentration: 80 mM, pH 9.3: inhibition Aspergillus parasiticus
3.1.1.58 Co2+ pH 5.3: stimulates, optimal concentration: 80 mM, pH 9.3: inhibition Aspergillus parasiticus
3.1.1.58 Mg2+ pH 5.3: stimulates, optimal concentration: 80 mM, pH 9.3: inhibition Aspergillus parasiticus
3.1.1.58 Mn2+ pH 5.3: stimulates, optimal concentration: 80 mM, pH 9.3: inhibition Aspergillus parasiticus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.58 0.54
-
 N-acetylated polygalactosamine 30°C, pH 5.3 and pH 9.3 Aspergillus parasiticus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.1.58 soluble
-
 Aspergillus oryzae
-
-
3.1.1.58 soluble
-
 Aspergillus parasiticus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.58 Ca2+ stimulates, optimal concentration: 80 mM, pH 9.3: inhibition Aspergillus parasiticus
3.1.1.58 Co2+ pH 5.3: stimulates, optimal concentration: 80 mM, pH 9.3: inhibition Aspergillus parasiticus
3.1.1.58 Mg2+ pH 5.3: stimulates, optimal concentration: 80 mM, pH 9.3: inhibition Aspergillus parasiticus
3.1.1.58 Mn2+ pH 5.3: stimulates, optimal concentration: 80 mM, pH 9.3: inhibition Aspergillus parasiticus
3.1.1.58 molybdate ammonium molybdate, pH 5.3: maximal stimulation at 2.5 mM, pH 9.3: slight stimulation Aspergillus parasiticus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.1.58 N-acetylgalactosaminoglycan + H2O Aspergillus parasiticus occurrence of this enzyme may account for the formation of the polygalactosamine with amino groups galactosaminoglycan + acetate
-
 ?
3.1.1.58 N-acetylgalactosaminoglycan + H2O Aspergillus parasiticus AHU 7165 occurrence of this enzyme may account for the formation of the polygalactosamine with amino groups galactosaminoglycan + acetate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.58 Aspergillus oryzae
-
 AHU 7139
-
3.1.1.58 Aspergillus oryzae AHU 7139
-
 AHU 7139
-
3.1.1.58 Aspergillus parasiticus
-
 AHU 7165
-
3.1.1.58 Aspergillus parasiticus AHU 7165
-
 AHU 7165
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.58 140fold, AHU 7165 Aspergillus parasiticus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.1.58 0.529
-
-
 Aspergillus parasiticus

Storage Stability

EC Number Storage Stability Organism
3.1.1.58 -18°C, stable for several months Aspergillus parasiticus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.58 additional information no substrates: bacterial cell wall peptidoglycan, N-acetylated heparin, partially O-hydroxyethylated chitin or monomeric N-acetylgalactosamine derivatives Aspergillus parasiticus ?
-
 ?
3.1.1.58 additional information no substrates: bacterial cell wall peptidoglycan, N-acetylated heparin, partially O-hydroxyethylated chitin or monomeric N-acetylgalactosamine derivatives Aspergillus parasiticus AHU 7165 ?
-
 ?
3.1.1.58 N-acetylated oligogalactosamine + H2O rate of deacetylation increases with the number of monosaccharide units in the oligosaccharides: with 14 or more N-acetylgalactosamine units: at a rate similar to that of deacetylation of the polymer, trimer to hexamer: slowly, inactive towards disaccharide Aspergillus parasiticus ?
-
 ?
3.1.1.58 N-acetylated oligogalactosamine + H2O rate of deacetylation increases with the number of monosaccharide units in the oligosaccharides: with 14 or more N-acetylgalactosamine units: at a rate similar to that of deacetylation of the polymer, trimer to hexamer: slowly, inactive towards disaccharide Aspergillus parasiticus AHU 7165 ?
-
 ?
3.1.1.58 N-acetylated polygalactosamine + H2O
-
 Aspergillus parasiticus polygalactosamine + acetate
-
 ?
3.1.1.58 N-acetylated polygalactosamine + H2O
-
 Aspergillus parasiticus AHU 7165 polygalactosamine + acetate
-
 ?
3.1.1.58 N-acetylgalactosaminoglycan + H2O
-
 Aspergillus oryzae galactosaminoglycan + acetate
-
 ?
3.1.1.58 N-acetylgalactosaminoglycan + H2O
-
 Aspergillus parasiticus galactosaminoglycan + acetate
-
 ?
3.1.1.58 N-acetylgalactosaminoglycan + H2O occurrence of this enzyme may account for the formation of the polygalactosamine with amino groups Aspergillus parasiticus galactosaminoglycan + acetate
-
 ?
3.1.1.58 N-acetylgalactosaminoglycan + H2O
-
 Aspergillus oryzae AHU 7139 galactosaminoglycan + acetate
-
 ?
3.1.1.58 N-acetylgalactosaminoglycan + H2O
-
 Aspergillus parasiticus AHU 7165 galactosaminoglycan + acetate
-
 ?
3.1.1.58 N-acetylgalactosaminoglycan + H2O occurrence of this enzyme may account for the formation of the polygalactosamine with amino groups Aspergillus parasiticus AHU 7165 galactosaminoglycan + acetate
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.58 5.3
-
 and pH 9.3, 2 optima Aspergillus parasiticus
3.1.1.58 9.3
-
 and pH 5.3, 2 optima Aspergillus parasiticus