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Literature summary for 3.1.1.72 extracted from

  • Koutaniemi, S.; van Gool, M.P.; Juvonen, M.; Jokela, J.; Hinz, S.W.; Schols, H.A.; Tenkanen, M.
    Distinct roles of carbohydrate esterase family CE16 acetyl esterases and polymer-acting acetyl xylan esterases in xylan deacetylation (2013), J. Biotechnol., 168, 684-692.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information acetyl esterases activate the enzyme Trichoderma reesei
additional information the enzyme is not activated by acetyl esterases Aspergillus niger

Organism

Organism UniProt Comment Textmining
Aspergillus niger
-
-
-
Thermothelomyces thermophilus
-
-
-
Trichoderma reesei
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hardwood acetyl glucuronoxylan mode of action, substrate specifiicity, and role of the family CE1 enzyme during deacetylation of soluble natural substrates, i.e. neutral and acidic O-acetylated xylooligosaccharides Thermothelomyces thermophilus ?
-
?
hardwood acetyl glucuronoxylan the enzyme can act on di-O-acetylated Xylp residues, but may have different activities towards the O-2- and O-3-linked acetyl groups, since the content of monoacetylated Xylp units is high after enzyme action. Mode of action, substrate specifiicity, and role of the family CE5 enzyme during deacetylation of soluble natural substrates, i.e. neutral and acidic O-acetylated xylooligosac-charides, overview Trichoderma reesei ?
-
?
hardwood acetyl glucuronoxylan the enzyme from Aspergillus niger is highly active compared to other acetylxylan esterases independently of the degree of polymerisation of the substrate. Mode of action, substrate specificity, and role of the family CE1 enzyme during deacetylation of soluble natural substrates, i.e. neutral and acidic O-acetylated xylooligosaccharides Aspergillus niger ?
-
?
additional information combined action of acetyl esterases and acetylxylan esterases enhances deacetylation activity Aspergillus niger ?
-
?
additional information combined action of acetyl esterases and acetylxylan esterases enhances deacetylation activity Thermothelomyces thermophilus ?
-
?
additional information the enzyme acts independently of the degree of polymerisation of the substrate. Combined action of acetyl esterases and acetylxylan esterases enhances deacetylation activity Trichoderma reesei ?
-
?

Synonyms

Synonyms Comment Organism
acetyl xylan esterase
-
Aspergillus niger
acetyl xylan esterase
-
Trichoderma reesei
acetyl xylan esterase
-
Thermothelomyces thermophilus
AXE
-
Aspergillus niger
AXE
-
Trichoderma reesei
Axe3
-
Thermothelomyces thermophilus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
assay at Aspergillus niger
40
-
assay at Trichoderma reesei
40
-
assay at Thermothelomyces thermophilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
assay at Aspergillus niger
5.5
-
assay at Trichoderma reesei
5.5
-
assay at Thermothelomyces thermophilus

General Information

General Information Comment Organism
evolution the enzyme belongs to the carbohydrate esterase family CE1 Aspergillus niger
evolution the enzyme belongs to the carbohydrate esterase family CE1 Thermothelomyces thermophilus
evolution the enzyme belongs to the carbohydrate esterase family CE5 Trichoderma reesei
physiological function acetylxylan esterases enhance the hydrolysis of O-acetylated xylan by removing the acetyl substituents that restrict the action of endo-1,4-beta-xylanases and beta-xylosidases Aspergillus niger
physiological function acetylxylan esterases enhance the hydrolysis of O-acetylated xylan by removing the acetyl substituents that restrict the action of endo-1,4-beta-xylanases and beta-xylosidases Trichoderma reesei
physiological function acetylxylan esterases enhance the hydrolysis of O-acetylated xylan by removing the acetyl substituents that restrict the action of endo-1,4-beta-xylanases and beta-xylosidases Thermothelomyces thermophilus