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Literature summary extracted from

  • Goldstone, D.C.; Villas-Boas, S.G.; Till, M.; Kelly, W.J.; Attwood, G.T.; Arcus, V.L.
    Structural and functional characterization of a promiscuous feruloyl esterase (Est1E) from the rumen bacterium Butyrivibrio proteoclasticus (2010), Proteins, 78, 1457-1469.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.1.1.73 industry molecular details of Est1E from the suite of fiber-degrading enzymes from important rumen bacterium is a step toward mapping the complex conversion of plant biomass to valuable products-meat and milk-by ruminants Butyrivibrio proteoclasticus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.73 PCR product cloned in the pDONR221 GATEWAY entry vecto. For protein expression, insert recombined into the pDEST17 GATEWAY expression vector and transformed into Escherichia coli BL21 (DE3) cells Butyrivibrio proteoclasticus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.1.73 crystals of apo-Est1E grown in 17-22% PEG3350, 0.3–0.5 M NaH2PO4, to 1.6 A resolution. Crystals belong to space group P21 with unit cell dimensions a = 52.0, b = 108.8, c = 91.4 A, beta = 102.28, with four Est1E molecules in the asymmetric unit. Overall structure of apo-Est1E is a canonical alpha/beta-hydrolase fold with an insertion in the loop between the 6th and 7th strands of the central beta-sheet. Crystals of Se-Met Est1E, to 2.0 A resolution, belong to space group P21 with cell dimensions a = 41.0, b = 129.6, c = 50.6 A, beta = 106.28, with two molecules in the asymmetric unit. Est1E in complex with ferulic acid, to 2.1 A resolution, crystals belong to space group C2 and with a dimer in the asymmetric unit. Overall structure of Est1E with ferulic acid bound is unchanged from the apostructure Butyrivibrio proteoclasticus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.73 2 3 p-nitrophenyl acetate in 100 mM phosphate buffer, pH 7.2, at 37°C Butyrivibrio proteoclasticus
3.1.1.73 24
-
p-nitrophenyl butyrate in 100 mM phosphate buffer, pH 7.2, at 37°C Butyrivibrio proteoclasticus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.73 75000
-
gel filtration, in solution Butyrivibrio proteoclasticus

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.73 Butyrivibrio proteoclasticus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.73 by centrifugation, immobilized metal affinity chromatography and gel filtration Butyrivibrio proteoclasticus

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.1.73 2.6
-
with ethyl cinnamate as substrate, in 100 mM phosphate buffer, pH 7.2, at 37°C Butyrivibrio proteoclasticus
3.1.1.73 2.9
-
with xylan birchwood as substrate and p-coumaric acid as product, in 100 mM phosphate buffer, pH 7.2, at 37°C Butyrivibrio proteoclasticus
3.1.1.73 4
-
with hemicellulose of ryegrass as substrate and trans-cinnamic acid as product, in 100 mM phosphate buffer, pH 7.2, at 37°C Butyrivibrio proteoclasticus
3.1.1.73 4.1
-
with hemicellulose of ryegrass as substrate and p-coumaric acid as product, in 100 mM phosphate buffer, pH 7.2, at 37°C Butyrivibrio proteoclasticus
3.1.1.73 6.9
-
with hemicellulose of ryegrass as substrate and ferulic acid as product, in 100 mM phosphate buffer, pH 7.2, at 37°C Butyrivibrio proteoclasticus
3.1.1.73 7.1
-
with xylan birchwood as substrate and 3-coumarincarboxylic acid as product, in 100 mM phosphate buffer, pH 7.2, at 37°C Butyrivibrio proteoclasticus
3.1.1.73 7.9
-
with xylan birchwood as substrate and trans-cinnamic acid as product, in 100 mM phosphate buffer, pH 7.2, at 37°C Butyrivibrio proteoclasticus
3.1.1.73 37
-
with ethyl ferulate as substrate, in 100 mM phosphate buffer, pH 7.2, at 37°C Butyrivibrio proteoclasticus
3.1.1.73 199
-
with ethyl 3-coumarincarboxylate as substrate, in 100 mM phosphate buffer, pH 7.2, at 37°C Butyrivibrio proteoclasticus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.73 ethyl 3-coumarincarboxylate + H2O
-
Butyrivibrio proteoclasticus 3-coumarincarboxylic acid + ethanol
-
?
3.1.1.73 ethyl cinnamate + H2O
-
Butyrivibrio proteoclasticus cinnamic acid + ethanol
-
?
3.1.1.73 ethyl ferulate + H2O
-
Butyrivibrio proteoclasticus ferulic acid + ethanol
-
?
3.1.1.73 additional information active site of Est1E is located in a groove at the C-terminus of strand beta5 and is marked in each monomer by the presence of a phosphate molecule. The conserved catalytic triad is formed by the residues Ser105, His225, and Asp197. The nucleophile, Ser105, is located in a tight turn between strand beta5 and alpha3 forming the nucleophile elbow. The histidine residue, His225, is located in a loop prior to alpha8. The catalytic triad is completed by Asp197 located in the loop between beta11 and alpha7 Butyrivibrio proteoclasticus ?
-
?
3.1.1.73 p-nitrophenyl acetate + H2O
-
Butyrivibrio proteoclasticus p-nitrophenol + acetic acid
-
?
3.1.1.73 p-nitrophenyl butyrate + H2O
-
Butyrivibrio proteoclasticus p-nitrophenol + butyric acid
-
?
3.1.1.73 p-nitrophenyl laurate + H2O
-
Butyrivibrio proteoclasticus p-nitrophenol + lauric acid
-
?
3.1.1.73 p-nitrophenyl palmitate + H2O
-
Butyrivibrio proteoclasticus p-nitrophenol + palmitic acid
-
?

Subunits

EC Number Subunits Comment Organism
3.1.1.73 dimer gel filtration, in solution Butyrivibrio proteoclasticus

Synonyms

EC Number Synonyms Comment Organism
3.1.1.73 Est1E
-
Butyrivibrio proteoclasticus
3.1.1.73 FA esterase
-
Butyrivibrio proteoclasticus
3.1.1.73 feruloyl esterase
-
Butyrivibrio proteoclasticus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.1.73 0.19
-
p-nitrophenyl acetate in 100 mM phosphate buffer, pH 7.2, at 37°C Butyrivibrio proteoclasticus
3.1.1.73 0.24
-
p-nitrophenyl butyrate in 100 mM phosphate buffer, pH 7.2, at 37°C Butyrivibrio proteoclasticus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.1.1.73 100
-
p-nitrophenyl butyrate in 100 mM phosphate buffer, pH 7.2, at 37°C Butyrivibrio proteoclasticus
3.1.1.73 120
-
p-nitrophenyl acetate in 100 mM phosphate buffer, pH 7.2, at 37°C Butyrivibrio proteoclasticus