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3.1.1.73: feruloyl esterase

This is an abbreviated version!
For detailed information about feruloyl esterase, go to the full flat file.

Word Map on EC 3.1.1.73

Reaction

feruloyl-polysaccharide
+
H2O
=
ferulate
 +
Polysaccharide

Synonyms

4-hydroxy-3-methoxycinnamic acid esterase, A.O.1, A.O.11, A.O.12, A.O.13, A.O.2, A.O.3, A.O.4, A.O.5, A.O.6, A.O.7, A.O.8, A.O.9, acetyl/ferulic acid esterase, AfFaeA, AN1772.2, AnFAE, AnFaeA, AnFAEB, AO090701000884, AoFaeB, AoFaeC, AtFAE-1, AtFAE-2, AtFAE-3, AuFaeA, AusFaeA, AwFAE, AwFAEA, BioH, carboxylic ester hydrolase, CE1, cellulosome multi-enzyme complex, cellulosome xylanase Z feruloyl esterase, CinI, CinII, cinnAE, cinnamic acid esterase, cinnamic acid hydrolase, cinnamic acid hydrolases, cinnamoyl ester hydrolase, Cinnamoyl esterase, CjXYLD, Est1, Est1E, EstA, esterase A, EstF27, FA esterase, FAE, FAE B, Fae-1, FAE-2, FAE-A, FAE-B, FAE-C, FAE-D, FAE-I, FAE-II, FAE-III, FAE-PL, FAE1, FAE125, Fae1A, FAE2, FAE3, FAE4, FAE5, FAE6, FAE68, FAE7, FAE7262, FAEA, FAEA1, FAEA2, FAEB, FaeB1, FAEB2, FaeC, FaeD, FaeD-3.544, FaeD1, FaeD2, FaeI, FaeT, FAE_XynZ, FE, FeE, Fee1B, ferulic acid esterase, ferulic acid esterase A, ferulic acid esterase B, ferulic acid esterase C, ferulic acid esterase D, feruloyl esterase, feruloyl esterase A, feruloyl esterase B, feruloyl/p-coumaroyl esterase, Feruloylesterase, FoFAE, FoFAE-I, FoFAE-II, FoFaeA, FoFaeB, FoFaeI, FoFaeII, hemicellulase acessory enzymes, hydroxycinnamoyl esterase, KX091144, Lp_0796, More, NcFaeB, NcFaeD-3.544, PeFaeA, PfFaeB, phenolic acid esterase, PSHAa enzyme, PSHAa1385, R18, SCHCODRAFT_60993, SCHCODRAFT_61055, StFAE, StFAE-A, StFaeB, StFaeC, TH2-18, TsFaeA, TsFaeB, TsFaeC, Tvms10a, Tvmz2a, type A FAE, type A feruloyl esterase, type B FAE, type B ferulic acid esterase, XLYD, XM 001217492, xylan-degrading enzyme system, xylanase 10, xylanase 10B, xylanase Z, xylanase-ferulic acid esterase, XYLD, XYLD esterase, Xyn10B, Xyn10D-Fae1A, XynZ

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.73 feruloyl esterase

Crystallization

Crystallization on EC 3.1.1.73 - feruloyl esterase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals belong to the orthorhombic space group
-
FAE domains, such as XynY and XynZ of the cellulosomal proteins
-
hanging drop vapor diffusion method
-
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
-
native and mutant protein, hanging drop vapor diffusion method
-
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
by hanging drop vapor diffusion method at 20°C, to 2.5 A resolution. Crystals of recombinant FaeA enzyme and its complex with ferulic acid belong to the triclinic space group P212121, with unit cell dimensions of a = 40.04, b = 48.98, c = 61.98 A and alpha = 98.65, beta = 93.98, gamma = 103.98, and a = 41.04, b = 49.28, c = 62.23 A and alpha = 98.01, beta = 92.12, gamma = 100.11, respectively
hanging drop vapor diffusion method
hanging drop vapor diffusion method, FAEA produced in Aspergillus niger (AnN) and Escherichia coli (EcR)
optimization of crystallization conditions is performed manually using the hanging micro-drop technique. Crystals are optimized using a full factorial screen. Crystals diffracting at 1.7A are obtained in the optimized condition
-
S133A mutant in complex with O-(5-O-[(E)-feruloyl]-alpha-L-arabinofuranosyl)-(1,3)-O-beta-D-xylopyranosyl-(1,4)-D-xylopyranose, hanging drop vapor diffusion method
-
purified recombinant deglycosylated enzyme, untreated or as iodine derivative, mixing of 0.001 ml of 30 mg/ml protein in 5 mM HEPES-NaOH, pH 7.0, with 0.001 ml of reservoir solution containing 20% PEG 1000 and 0.1M Tris-HCl, pH 7.0, hanging drop vapor diffusion method, 20°C, X-ray diffraction structure determination and analysis at 1.5-2.4 A resolution, modeling
-
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
-
homology modeling of structure and docking of substrates
molecular modeling of structure based on PDB entry 3WMT
molecular docking of methyl hydroxycinnamates to wild-type and mutant structures
purified recombinant His-tagged enzyme, hanging drop vapour diffusion, 0.002 ml of 15 mg/ml protein in 200 mM NaCl, 10 mM HEPES, pH 7.5, 5 mM dithiothreitol, 10% glycerol, are mixed with 0.002 ml of reservoir solution containing 0.2 M ammonium sulfate, 26% PEG 4000, 0.1 M sodium cacodylate pH 6.5, 4% w/v benzamidine-HCl, and equilibration against 0.5 ml reservoir solution, 16°C, 2 weeks, method optimization, X-ray diffraction structure determination and analysis at 2.9 A resolution