Literature summary for 3.1.1.73 extracted from

Gruninger, R.; Cote, C.; McAllister, T.; Abbott, D.
Contributions of a unique beta-clamp to substrate recognition illuminates the molecular basis of exolysis in ferulic acid esterases (2016), Biochem. J., 473, 839-849.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structure in both the presence and absence of ferulic acid, to 1.55 and 1.6 A resolution, respectively. Fae1A adopts an alpha/beta-hydrolase fold that is structurally conserved with bacterial FAEs, and possesses a unique loop, termed the beta-clamp, that encloses the ligand. The beta-clamp may define the structural basis of exolytic activities	Anaeromyces mucronatus

Protein Variants

Protein Variants	Comment	Organism
D190A	about 10% residual activity with methyl ferulate	Anaeromyces mucronatus
F192A	about 40% residual activity with methyl ferulate	Anaeromyces mucronatus
H196A	about 40% residual activity with methyl ferulate	Anaeromyces mucronatus
additional information	deletion of the beta-clamp region, residues 185-199, complete loss of activity	Anaeromyces mucronatus
Y119A	about 50% residual activity with methyl ferulate	Anaeromyces mucronatus

Organism

Organism	UniProt	Comment	Textmining
Anaeromyces mucronatus	F2YCB6	-	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
2.29	-	substrate methyl 4-coumarate, pH 7.2, 25°C	Anaeromyces mucronatus
7	-	substrate methyl sinapinate, pH 7.2, 25°C	Anaeromyces mucronatus
10.6	-	substrate methyl ferulate, pH 7.2, 25°C	Anaeromyces mucronatus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
methyl 4-coumarate + H2O	-	Anaeromyces mucronatus	methanol + 4-coumaric acid	-	?
methyl ferulate + H2O	-	Anaeromyces mucronatus	methanol + ferulic acid	-	?
methyl sinapinate + H2O	-	Anaeromyces mucronatus	methanol + sinapic acid	-	?

Synonyms

Synonyms	Comment	Organism
Fae1A	-	Anaeromyces mucronatus

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Release 2023.1 (January 2023)