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Literature summary for 3.1.1.72 extracted from

  • Biely, P.; Cziszarova, M.; Uhliarikova, I.; Agger, J.W.; Li, X.L.; Eijsink, V.G.; Westereng, B.
    Mode of action of acetylxylan esterases on acetyl glucuronoxylan and acetylated oligosaccharides generated by a GH10 endoxylanase (2013), Biochim. Biophys. Acta, 1830, 5075-5086.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Acetivibrio thermocellus
-
-
-
Orpinomyces sp.
-
-
-
Schizophyllum commune
-
-
-
Streptomyces lividans
-
-
-
Trichoderma reesei
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme Schizophyllum commune

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation recombinant enzyme Orpinomyces sp.
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-O-methyl-D-glucuronosyl-alpha-1,2-D-xylopyranosyl-beta-1,4-xylopyranosyl-beta-1,4-xylopyranosyl-beta-1,4-xylopyranosyl-beta-1,4-xylopyranose + H2O
-
Schizophyllum commune 4-O-methyl-D-glucuronosyl-alpha-1,2-D-xylopyranosyl-beta-1,4-xylopyranosyl-beta-1,4-xylopyranose + beta-1,4-xylopyranosyl-beta-1,4-xylopyranose
-
?
aspen acetyl glucuronoxylan + H2O
-
Trichoderma reesei ?
-
?
aspen acetyl glucuronoxylan + H2O
-
Streptomyces lividans ?
-
?
aspen acetyl glucuronoxylan + H2O
-
Schizophyllum commune ?
-
?
aspen acetyl glucuronoxylan + H2O
-
Orpinomyces sp. ?
-
?
aspen acetyl glucuronoxylan + H2O
-
Acetivibrio thermocellus ?
-
?
birch acetyl glucuronoxylan + H2O positional specificity of the enzyme Schizophyllum commune ?
-
?
hardwood acetyl glucuronoxylan no complete deacetylation, complete deacetylation of a hardwood acetyl glucuronoxylan requires additional deacetylating enzyme(s) Trichoderma reesei ?
-
?
hardwood acetyl glucuronoxylan no complete deacetylation, complete deacetylation of a hardwood acetyl glucuronoxylan requires additional deacetylating enzyme(s) Streptomyces lividans ?
-
?
hardwood acetyl glucuronoxylan no complete deacetylation, complete deacetylation of a hardwood acetyl glucuronoxylan requires additional deacetylating enzyme(s) Schizophyllum commune ?
-
?
hardwood acetyl glucuronoxylan no complete deacetylation, complete deacetylation of a hardwood acetyl glucuronoxylan requires additional deacetylating enzyme(s) Orpinomyces sp. ?
-
?
hardwood acetyl glucuronoxylan no complete deacetylation, complete deacetylation of a hardwood acetyl glucuronoxylan requires additional deacetylating enzyme(s) Acetivibrio thermocellus ?
-
?
additional information inability of CE4 AcXEs to catalyze deacetylation of 2,3-di-O-acetylated xylopyranosyl residues. Substrate specificity together with endo-beta-1,4-xylanase of GH10 family from Clostridium thermocellum, mode of action of the CE4 family enzyme, overview. Regardless of the polymerization degree, each neutral oligosaccharide is converted into three forms: completely deacetylated and mono- and di-O-acetylated Streptomyces lividans ?
-
?
additional information inability of CE4 AcXEs to catalyze deacetylation of 2,3-di-O-acetylated xylopyranosyl residues. Substrate specificity together with endo-beta-1,4-xylanase of GH10 family from Clostridium thermocellum, mode of action of the CE4 family enzyme, overview. Regardless of the polymerization degree, each neutral oligosaccharide is converted into three forms: completely deacetylated and mono- and di-O-acetylated Acetivibrio thermocellus ?
-
?
additional information substrate specificity together with endo-beta-1,4-xylanase of GH10 family from Clostridium thermocellum, mode of action of the CE5 family enzyme, overview. After incubation with the esterase, free and monoacetylated Xyl2, Xyl3, and Xyl4 are detected, with the free oligosaccharides predominating. The complex mixture of acetylated aldouronic acids is converted to a mixture of short free and monoacetylated MeGlcAXylx species (x = 2–6). The mono-acetylated species are clearly more abundant than the corresponding non-acetylated species Trichoderma reesei ?
-
?
additional information substrate specificity together with endo-beta-1,4-xylanase of GH10 family from Clostridium thermocellum, mode of action of the CE6 family enzyme, overview. On aspen glucuronoxylan hydrolysate, all neutral and acidic xylooligosaccharides present in the starting mixture are only partially deacetylated and persist in the reactionmixture mainly as mono- and di-O-acetates. The degree of acetylation is higher with shorter than longer oligosaccharides Orpinomyces sp. ?
-
?
additional information substrate specificity together with endo-beta-1,4-xylanase of GH10 family from Clostridium thermocellum, overview. The enzyme converts acidic oligosaccharides mainly to mono- and di-O-acetyl derivatives, largest amount detected is mono-O-acetate is GlcAXyl8Ac, completely deacetylated MeGlcAXyl3, MeGlcAXyl4 and MeGlcAXyl5 are also observed, mode of action of the CE1 family enzyme, overview Schizophyllum commune ?
-
?

Synonyms

Synonyms Comment Organism
AcXE
-
Trichoderma reesei
AcXE
-
Streptomyces lividans
AcXE
-
Schizophyllum commune
AcXE
-
Orpinomyces sp.
AcXE
-
Acetivibrio thermocellus
CE1 AcXE
-
Schizophyllum commune
CE4 AcXE
-
Streptomyces lividans
CE4 AcXE
-
Acetivibrio thermocellus
CE5 AcXE
-
Trichoderma reesei
CE6 AcXE
-
Orpinomyces sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25 40 assay at Trichoderma reesei
25 40 assay at Streptomyces lividans
25 40 assay at Schizophyllum commune
25 40 assay at Orpinomyces sp.
25 40 assay at Acetivibrio thermocellus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 6.5 assay at Trichoderma reesei
6 6.5 assay at Streptomyces lividans
6 6.5 assay at Schizophyllum commune
6 6.5 assay at Orpinomyces sp.
6 6.5 assay at Acetivibrio thermocellus

General Information

General Information Comment Organism
evolution the enzyme belongs to aspartate-metalloesterase carbohydrate esterase family 4, CE4 Streptomyces lividans
evolution the enzyme belongs to aspartate-metalloesterase carbohydrate esterase family 4, CE4 Acetivibrio thermocellus
evolution the enzyme belongs to serine-type esterase carbohydrate esterase family 1, CE1 Schizophyllum commune
evolution the enzyme belongs to serine-type esterase carbohydrate esterase family 5, CE5 Trichoderma reesei
evolution the enzyme belongs to serine-type esterase carbohydrate esterase family 6, CE6 Orpinomyces sp.