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Literature summary for 3.1.1.72 extracted from

  • Kool, M.M.; Schols, H.A.; Wagenknecht, M.; Hinz, S.W.; Moerschbacher, B.M.; Gruppen, H.
    Characterization of an acetyl esterase from Myceliophthora thermophila C1 able to deacetylate xanthan (2014), Carbohydr. Polym., 111, 222-229.
    View publication on PubMed
Search for more literature for 3.1.1.72

Organism

Organism UniProt Comment Textmining
Thermothelomyces thermophilus
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Thermothelomyces thermophilus C1
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Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0013
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 substrate xanthan, pH 5.6, 40°C Thermothelomyces thermophilus
8.3
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 substrate acetylated xylooligosaccharides, pH 5.6, 40°C Thermothelomyces thermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetylated xylooligosaccharides + H2O
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 Thermothelomyces thermophilus ?
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 ?
acetylated xylooligosaccharides + H2O
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 Thermothelomyces thermophilus C1 ?
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 ?
xanthan + H2O bacterial polysaccharide xanthan is a polymer having a (1->4)-linked beta-D-glucopyranosyl backbone, with a beta-D-mannopyranosyl-(1->4)-beta-D-glucopyranosyluronic acid-(1->2)-alpha-D-mannopyranosyl side chain substituted to every other glucopyranosyl residue at the O-3 position. Enzyme activity towards xanthan is only observed when xanthan molecules are in the disordered conformation in complete absence of salt. The enzyme specifically removes the acetyl groups positioned on the inner mannose, acetyl groups positioned on the outer mannose are not removed at all. After a prolonged incubation at optimal conditions, 57% of all acetyl groups, representing 70% of all acetyl groups on the inner mannose units, are hydrolyzed Thermothelomyces thermophilus ?
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 ?
xanthan + H2O bacterial polysaccharide xanthan is a polymer having a (1->4)-linked beta-D-glucopyranosyl backbone, with a beta-D-mannopyranosyl-(1->4)-beta-D-glucopyranosyluronic acid-(1->2)-alpha-D-mannopyranosyl side chain substituted to every other glucopyranosyl residue at the O-3 position. Enzyme activity towards xanthan is only observed when xanthan molecules are in the disordered conformation in complete absence of salt. The enzyme specifically removes the acetyl groups positioned on the inner mannose, acetyl groups positioned on the outer mannose are not removed at all. After a prolonged incubation at optimal conditions, 57% of all acetyl groups, representing 70% of all acetyl groups on the inner mannose units, are hydrolyzed Thermothelomyces thermophilus C1 ?
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 ?

Synonyms

Synonyms Comment Organism
acetyl xylan esterase
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 Thermothelomyces thermophilus
Axe3
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 Thermothelomyces thermophilus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
53
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 with xanthan Thermothelomyces thermophilus

General Information

General Information Comment Organism
evolution the enzyme belongs to the carbohydrate esterase family 1, CE1 Thermothelomyces thermophilus