Catalyses the hydrolysis of acetyl groups from polymeric xylan, acetylated xylose, acetylated glucose, alpha-napthyl acetate, p-nitrophenyl acetate but not from triacetylglycerol. Does not act on acetylated mannan or pectin.
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.
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, catalytic triad consists of Ser90, His187, and Asp175
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.
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SYSTEMATIC NAME
IUBMB Comments
acetylxylan esterase
Catalyses the hydrolysis of acetyl groups from polymeric xylan, acetylated xylose, acetylated glucose, alpha-napthyl acetate, p-nitrophenyl acetate but not from triacetylglycerol. Does not act on acetylated mannan or pectin.
it is proposed that AXE I and II act in succession in xylan degradation, first, xylan is attacked by AXE I and other xylanases possessing CBMs (which facilitate binding to lignocellulose), followed by other enzymes acting mainly on soluble substrates
it is proposed that AXE I and II act in succession in xylan degradation, first, xylan is attacked by AXE I and other xylanases possessing CBMs (which facilitate binding to lignocellulose), followed by other enzymes acting mainly on soluble substrates
it is proposed that AXE I and II act in succession in xylan degradation, first, xylan is attacked by AXE I and other xylanases possessing CBMs (which facilitate binding to lignocellulose), followed by other enzymes acting mainly on soluble substrates
it is proposed that AXE I and II act in succession in xylan degradation, first, xylan is attacked by AXE I and other xylanases possessing CBMs (which facilitate binding to lignocellulose), followed by other enzymes acting mainly on soluble substrates
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
protein solution: ammonium sulfate in 50 mM citrate buffer, pH 5.3, X-ray diffraction structure determination at 0.9 and 1.1 A, analysis of the multiple conformations of the active site residues Ser90 and His187
preparation of a deletion mutant where the amino acid 104-114 are eliminated. This mutant is catalytically active and can hydrolyze long chain fatty acid esters with much greater efficiency than the wild type AXE II
preparation of a deletion mutant where the amino acid 104-114 are eliminated. This mutant is catalytically active and can hydrolyze long chain fatty acid esters with much greater efficiency than the wild type AXE II
Gordillo, F.; Caputo, V.; Peirano, A.; Chavez, R.; Van Beeumen, J.; Vandenberghe, I.; Claeyssens, M.; Bull, P.; Ravanal, M.C.; Eyzaguirre, J.
Penicillium purpurogenum produces a family 1 acetyl xylan esterase containing a carbohydrate-binding module: characterization of the protein and its gene