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Literature summary extracted from

  • Hakulinen, N.; Tenkanen, M.; Rouvinen, J.
    Three-dimensional structure of the catalytic core of acetylxylan esterase from Trichoderma reesei: insights into the deacetylation mechanism (2000), J. Struct. Biol., 132, 180-190.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.1.72 purified catalytic core of the enzyme at 10 mg/ml, hanging drop vapour diffusion method, room temperature, protein solution: sodium acetate, pH 5.0, reservoir solution: potassium/sodium tartrate 1.1 M, TES buffer 0.1 M, pH 8.2, in the ratio 2:1:1 with a Trixton X-100 solution, few weeks, X-ray diffraction structure determination and analysis at 1.9 A, structure model Trichoderma reesei

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.72 Trichoderma reesei Q99034
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Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.1.72 acetylxylan + 3 H2O = 3 acetic acid + xylan catalyses the hydrolysis of acetyl groups from polymeric xylan, acetylated xylose, acetylated glucose, alpha-naphthyl acetate, p-nitrophenyl acetate but not from triacetylglycerol. Does not act on acetylated mannan or pectin, reaction mechanism, enzyme is a serine esterase containing an oxyanion hole and a catalytic triad build of Ser90, His187, and Asp175, substrate binding model Trichoderma reesei
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.72 acetylated xylan + H2O catalytic mechanism, substrate with mono- and double acetylated residues, the enzyme cannot remove acetyl groups located close to large side groups such as 4-O-methylglucuronic acid Trichoderma reesei xylan + acetate
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