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Literature summary for 3.1.1.73 extracted from

  • Schubot, F.D.; Kataeva, I.A.; Blum, D.L.; Shah, A.K.; Ljungdahl, L.G.; Rose, J.P.; Wang, B.C.
    Structural basis for the substrate specificity of the feruloyl esterase domain of the cellulosomal xylanase Z from Clostridium thermocellum (2001), Biochemistry, 40, 12524-12532.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
native and mutant enzyme expressed in Escherichia coli Acetivibrio thermocellus

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method, cocrystals of the native enzyme with the substrate O-(5-O-[(E)-feruloyl]-alpha-L-arabinofuranosyl)-(1-3)-O-beta-D-xylopyranosyl-(1-4)-D-xylopyranose and of the S172A mutant with 5-O-[(E)-feruloyl]-[O-beta-D-xylopyranosyl-(1-2)]-O-R-L-arabino-furanosyl-[1-3]-O-beta-D-xylopyranosyl-(1-4)-D-xylopyranose Acetivibrio thermocellus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular a domain of the Clostridium thermocellum’s cellulosomal xylanase Z displays feruloyl esterase activity Acetivibrio thermocellus
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-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5-O-[(E)-feruloyl]-[O-beta-D-xylopyranosyl-(1-2)]-O-alpha-L-arabino-furanosyl-[1-3]-O-beta-D-xylopyranosyl-(1-4)-D-xylopyranose + H2O Acetivibrio thermocellus
-
ferulic acid + [O-beta-D-xylopyranosyl-(1-2)]-O-alpha-L-arabino-furanosyl-[1-3]-O-beta-D-xylopyranosyl-(1-4)-D-xylopyranose
-
?
feruloyl polysaccharide + H2O Acetivibrio thermocellus involved in the degradation of plant cell wall material, breaks ferulic acid cross-links between cell wall components ferulic acid + ?
-
?
hemicellulose + H2O Acetivibrio thermocellus involved in the degradation of plant cell wall material, breaks ferulic acid cross-links between cell wall components ferulic acid + arabinoxylan + pectin + ?
-
?
O-(5-O-[(E)-feruloyl]-alpha-L-arabinofuranosyl)-(1-3)-O-beta-D-xylopyranosyl-(1-4)-D-xylopyranose + H2O Acetivibrio thermocellus
-
ferulic acid + alpha-L-arabinofuranosyl-(1-3)-O-beta-D-xylopyranosyl-(1-4)-D-xylopyranose
-
?

Organism

Organism UniProt Comment Textmining
Acetivibrio thermocellus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzymes Acetivibrio thermocellus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5-O-[(E)-feruloyl]-[O-beta-D-xylopyranosyl-(1-2)]-O-alpha-L-arabino-furanosyl-[1-3]-O-beta-D-xylopyranosyl-(1-4)-D-xylopyranose + H2O
-
Acetivibrio thermocellus ferulic acid + [O-beta-D-xylopyranosyl-(1-2)]-O-alpha-L-arabino-furanosyl-[1-3]-O-beta-D-xylopyranosyl-(1-4)-D-xylopyranose
-
?
feruloyl polysaccharide + H2O involved in the degradation of plant cell wall material, breaks ferulic acid cross-links between cell wall components Acetivibrio thermocellus ferulic acid + ?
-
?
hemicellulose + H2O involved in the degradation of plant cell wall material, breaks ferulic acid cross-links between cell wall components Acetivibrio thermocellus ferulic acid + arabinoxylan + pectin + ?
-
?
O-(5-O-[(E)-feruloyl]-alpha-L-arabinofuranosyl)-(1-3)-O-beta-D-xylopyranosyl-(1-4)-D-xylopyranose + H2O
-
Acetivibrio thermocellus ferulic acid + alpha-L-arabinofuranosyl-(1-3)-O-beta-D-xylopyranosyl-(1-4)-D-xylopyranose
-
?

Synonyms

Synonyms Comment Organism
FAE_XynZ
-
Acetivibrio thermocellus
xylanase Z a domain of the Clostridium thermocellum’s cellulosomal xylanase Z displays feruloyl esterase activity Acetivibrio thermocellus