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
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3.1.1.73
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aspergillus
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esterases
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wheat
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niger
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bran
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xylans
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arabinoxylans
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hydroxycinnamic
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p-coumaric
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thermocellum
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hemicellulose
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destarched
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caffeate
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fermentum
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degradation
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synthesis
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talaromyces
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xylanolytic
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xylanases
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diferulic
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psycinfo
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sinapinate
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nutrition
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spelt
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arabinofuranosidase
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ester-linked
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ensile
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lignocellulolytic
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awamori
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acetylxylan
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neocallimastix
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fibrolytic
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food industry
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agriculture
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paper production
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biotechnology
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pharmacology
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biofuel production
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industry
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medicine
- 3.1.1.73
- aspergillus
- esterases
- wheat
- niger
- bran
- xylans
- arabinoxylans
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hydroxycinnamic
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p-coumaric
- thermocellum
- hemicellulose
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destarched
- caffeate
- fermentum
- degradation
- synthesis
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talaromyces
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xylanolytic
- xylanases
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diferulic
-
psycinfo
- sinapinate
- nutrition
- spelt
- arabinofuranosidase
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ester-linked
-
ensile
-
lignocellulolytic
- awamori
- acetylxylan
- neocallimastix
-
fibrolytic
- food industry
- agriculture
- paper production
- biotechnology
- pharmacology
- biofuel production
- industry
- medicine
Reaction
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
3.1.1.73 feruloyl esteraseAdvanced search results
results (
results (Engineering
Engineering on EC 3.1.1.73 - feruloyl esterase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
S954A
D77I
higher catalytic efficiency towards alpha-naphtylbutyrate and alpha-naphtylcaprylate, some activity towards long-acyl chain esters, no activity towards phenolic acid methyl esters and feruloylated arabinoxylan, increased pH-optimum
N79A
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glycosylation-free mutant enzyme has lower activity than that of the recombinant wild-type enzyme towards alpha-naphthylbutyrate, alpha-naphthylcaprylate, and phenolic acid methyl esters. The lower catalytic efficiency is due to a combination of increased KM and decreased kcat. the mutant enzyme exhibits considerably reduced thermostaility relative to wild-type
N79Q
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glycosylation-free mutant enzyme has lower activity than that of the recombinant wild-type enzyme towards alpha-naphthylbutyrate, alpha-naphthylcaprylate, and phenolic acid methyl esters. The lower catalytic efficiency is due to a considerably decreased kcat. the mutant enzyme exhibits considerably reduced thermostability relative to wild-type
Y80F
higher catalytic efficiency towards alpha-naphtylbutyrate and alpha-naphtylcaprylate, increased pH-optimum
Y80F
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higher catalytic efficiency towards alpha-naphtylbutyrate and alpha-naphtylcaprylate, increased pH-optimum
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N79A
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glycosylation-free mutant enzyme has lower activity than that of the recombinant wild-type enzyme towards alpha-naphthylbutyrate, alpha-naphthylcaprylate, and phenolic acid methyl esters. The lower catalytic efficiency is due to a combination of increased KM and decreased kcat. the mutant enzyme exhibits considerably reduced thermostaility relative to wild-type
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N79Q
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glycosylation-free mutant enzyme has lower activity than that of the recombinant wild-type enzyme towards alpha-naphthylbutyrate, alpha-naphthylcaprylate, and phenolic acid methyl esters. The lower catalytic efficiency is due to a considerably decreased kcat. the mutant enzyme exhibits considerably reduced thermostability relative to wild-type
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A140T
random mutagenesis, the mutant shows 2.4fold increased thermostability compared to the mutant D93G/S187F
C235S
random mutagenesis, the mutant shows 3.2fold increased thermostability compared to the mutant D93G/S187F
D174A
site-directed mutagenesis, the mutant does not show changes in thermal stability compared to the wild-type enzyme
D93G
D93G/S187F
D93G/S187F/C235I
specific activity similar to wild-type, significant increase in thermal stability
D93G/S187F/C235N
specific activity similar to wild-type, significant increase in thermal stability
D93G/S187F/C235R
specific activity similar to wild-type, significant increase in thermal stability
D93G/S187F/C235S
specific activity similar to wild-type, significant increase in thermal stability
D93G/S187F/C235V
specific activity similar to wild-type, significant increase in thermal stability
G69A
random mutagenesis, the mutant shows unaltered thermostability compared to the mutant D93G/S187F
K37I
random mutagenesis, the mutant shows 2.5fold increased thermostability compared to the mutant D93G/S187F
K37I/G69A
random mutagenesis, the mutant shows 2.5fold increased thermostability compared to the mutant D93G/S187F
L14F
random mutagenesis, the mutant shows 2.0fold increased thermostability compared to the mutant D93G/S187F
L14F/T35I/K37I/T57I/T63I/A140T/Q121H/S163T/Q177H/V178A/Q185R
the mutant shows altered kinetics compared to the mutant D93G/S187F
L14F/T35I/K37I/T57I/T63I/A140T/Q121H/S163T/Q177H/V178A/Q185R/C235S
the mutant shows altered kinetics compared to the mutant D93G/S187F
Q121H
random mutagenesis, the mutant shows 1.8fold increased thermostability compared to the mutant D93G/S187F
Q177H
random mutagenesis, the mutant shows 2.0fold increased thermostability compared to the mutant D93G/S187F
Q185R
random mutagenesis, the mutant shows 2.5fold increased thermostability compared to the mutant D93G/S187F
S163T
random mutagenesis, the mutant shows 3.6fold increased thermostability compared to the mutant D93G/S187F
S187F
S92A
site-directed mutagenesis, the mutant does not show changes in thermal stability compared to the wild-type enzyme
T35I
random mutagenesis, the mutant shows 3.4fold increased thermostability compared to the mutant D93G/S187F
T57I
random mutagenesis, the mutant shows 1.4fold increased thermostability compared to the mutant D93G/S187F
T57I/V178A
random mutagenesis, the mutant 2.3fold shows increased thermostability compared to the mutant D93G/S187F
T63I
random mutagenesis, the mutant shows 2.5fold increased thermostability compared to the mutant D93G/S187F
V178A
random mutagenesis, the mutant shows 1.6fold increased thermostability compared to the mutant D93G/S187F
W260S
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significantly reduced turnover, increase in alpha-helix content, broadening of substrate specificity allowing the hydrolysis of methyl caffeate
W260V
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significantly reduced turnover, increase in alpha-helix content, broadening of substrate specificity allowing the hydrolysis of methyl caffeate
Y80S
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significantly reduced turnover, increase in alpha-helix content, broadening of substrate specificity allowing the hydrolysis of methyl caffeate
Y80V
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significantly reduced turnover, increase in alpha-helix content, broadening of substrate specificity allowing the hydrolysis of methyl caffeate
C235S
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random mutagenesis, the mutant shows 3.2fold increased thermostability compared to the mutant D93G/S187F
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D174A
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site-directed mutagenesis, the mutant does not show changes in thermal stability compared to the wild-type enzyme
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D93G
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site-directed mutagenesis, the mutant shows slightly increased thermal stability compared to the wild-type enzyme
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G69A
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random mutagenesis, the mutant shows unaltered thermostability compared to the mutant D93G/S187F
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Q185R
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random mutagenesis, the mutant shows 2.5fold increased thermostability compared to the mutant D93G/S187F
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S187F
S92A
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site-directed mutagenesis, the mutant does not show changes in thermal stability compared to the wild-type enzyme
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W142F
contrary to wild type, mutant is active against methyl esters of ferulic acid, p-coumaric acid, caffeic acid, and sinapic acid and ethyl ester of ferulic acid and exhibits enhanced production of ferulic acid from wheat arabinoxylan
W144Y
contrary to wild type, mutant is active against methyl esters of ferulic acid, p-coumaric acid, caffeic acid, and sinapic acid and ethyl ester of ferulic acid and exhibits enhanced production of ferulic acid from wheat arabinoxylan
W142F
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contrary to wild type, mutant is active against methyl esters of ferulic acid, p-coumaric acid, caffeic acid, and sinapic acid and ethyl ester of ferulic acid and exhibits enhanced production of ferulic acid from wheat arabinoxylan
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W144Y
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contrary to wild type, mutant is active against methyl esters of ferulic acid, p-coumaric acid, caffeic acid, and sinapic acid and ethyl ester of ferulic acid and exhibits enhanced production of ferulic acid from wheat arabinoxylan
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A126C/N152C
introduction of a disulfide bridge, increase of temperature optimum by 6°C and increase in thermal inactivation half-live
E280S
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the ferulic acid esterase activity increases 3fold. Capacity for Xyn10D-Fae1A to depolymerize oat spelt xylan is attenuated
S629A
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the ferulic acid esterase activity for Xyn10D-Fae1A is attenuated. Depolymerizes xylan to an extent similar to the that of wild-type
E280S
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the ferulic acid esterase activity increases 3fold. Capacity for Xyn10D-Fae1A to depolymerize oat spelt xylan is attenuated
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S629A
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the ferulic acid esterase activity for Xyn10D-Fae1A is attenuated. Depolymerizes xylan to an extent similar to the that of wild-type
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D214A
mutation within catalytic triad, complete loss of activity
H268A
mutation within catalytic triad, complete loss of activity
S191A
mutation within catalytic triad, complete loss of activity
D214A
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mutation within catalytic triad, complete loss of activity
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H268A
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mutation within catalytic triad, complete loss of activity
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S191A
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mutation within catalytic triad, complete loss of activity
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F251L/H105Y
mutant displays improved activity and thermostability
G49A
mutant displays improved activity and thermostability
G49D
mutant displays improved activity and thermostability
H105Y
mutant displays improved activity and thermostability
F251L/H105Y
Thermothelomyces thermophilus DSM 1799
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mutant displays improved activity and thermostability
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G49A
Thermothelomyces thermophilus DSM 1799
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mutant displays improved activity and thermostability
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G49D
Thermothelomyces thermophilus DSM 1799
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mutant displays improved activity and thermostability
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H105Y
Thermothelomyces thermophilus DSM 1799
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mutant displays improved activity and thermostability
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T27I/S84L/V161I/G243C
mutant displays significantly improved thermostability
T27I/S84L/V161I/H195L/G243C/A259V
mutant displays significantly improved thermostability
additional information
D93G
site-directed mutagenesis, the mutant shows slightly increased thermal stability compared to the wild-type enzyme
D93G
site-directed mutagenesis, the mutant shows increased thermostability compared to the wild-type enzyme
D93G/S187F
site-directed mutagenesis, the mutant shows 10fold increased activity compared to the wild-type enzyme
S187F
site-directed mutagenesis, the mutant shows highly increased thermal stability compared to the wild-type enzyme. The substitution of S187F reduces three possible hydrogen bonds
S187F
site-directed mutagenesis, the mutant shows increased thermostability compared to the wild-type enzyme
S187F
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site-directed mutagenesis, the mutant shows highly increased thermal stability compared to the wild-type enzyme. The substitution of S187F reduces three possible hydrogen bonds
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S187F
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site-directed mutagenesis, the mutant shows increased thermostability compared to the wild-type enzyme
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additional information
exprression in Escherichia coli with and without its putative signal peptide. The truncated form has less than 10% relative activity compared to the full length and is more prone to aggregation after purification
additional information
Actinomyces sp. oral taxon 448 F0400
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exprression in Escherichia coli with and without its putative signal peptide. The truncated form has less than 10% relative activity compared to the full length and is more prone to aggregation after purification
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additional information
deletion of the beta-clamp region, residues 185-199, complete loss of activity
additional information
generation of a chimeric library from four homologous FAEs originated from fungi by a DNA shuffling strategy. Chimeras contain DNA fragments encoding the wild-type FaeA from Aspergillus terreus, FaeA from Penicillium chrysogenum and FaeA from Aspergillus flavus, as well as the M11 mutant of FaeA from Aspergillus niger. Chimeras with enhanced thermal stability contain segments from 3 or 4 of the parental enzymes. The half-lives of inactivation of the chimeras at 65°C are increased by up to 22 fold when compared to the most stable parental FAE. The release of ferulic acid from steam-exploded corn stalk using the best chimera is enhanced by 12.8fold when compared to the best parental FAE
additional information
production of a fusion protein of the Trichoderma reesei swollenin I (SWOI) and Aspergillus niger feruloyl esterase A (FAEA). The release of ferulic acid from wheat bran during a period of 24 h of enzymatic hydrolysis with the SWOI-FAEA improved the efficiency of ferulic acid release by 50% compared with the results obtained using the free FAEA and SWOI
additional information
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production of a fusion protein of the Trichoderma reesei swollenin I (SWOI) and Aspergillus niger feruloyl esterase A (FAEA). The release of ferulic acid from wheat bran during a period of 24 h of enzymatic hydrolysis with the SWOI-FAEA improved the efficiency of ferulic acid release by 50% compared with the results obtained using the free FAEA and SWOI
additional information
identification of mutations beneficial to the thermostability of the nezyme, screening a random mutagenesis library constructed in Pichia pastoris
additional information
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identification of mutations beneficial to the thermostability of the nezyme, screening a random mutagenesis library constructed in Pichia pastoris
additional information
transgenic alflafa plants expressing the enzyme possess modified cell wall morphology and composition with a reduction in ester linkages and elevated lignin content, they are more recalcitrant to digestion by mixed ruminal microorganisms, phenotypes, detailed overview
additional information
generation of a chimeric library from four homologous FAEs originated from fungi by a DNA shuffling strategy. Chimeras contain DNA fragments encoding the wild-type FaeA from Aspergillus terreus, FaeA from Penicillium chrysogenum and FaeA from Aspergillus flavus, as well as the M11 mutant of FaeA from Aspergillus niger. Chimeras with enhanced thermal stability contain segments from 3 or 4 of the parental enzymes. The half-lives of inactivation of the chimeras at 65°C are increased by up to 22 fold when compared to the most stable parental FAE. The release of ferulic acid from steam-exploded corn stalk using the best chimera is enhanced by 12.8fold when compared to the best parental FAE
additional information
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identification of mutations beneficial to the thermostability of the nezyme, screening a random mutagenesis library constructed in Pichia pastoris
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additional information
generation of a chimeric library from four homologous FAEs originated from fungi by a DNA shuffling strategy. Chimeras contain DNA fragments encoding the wild-type FaeA from Aspergillus terreus, FaeA from Penicillium chrysogenum and FaeA from Aspergillus flavus, as well as the M11 mutant of FaeA from Aspergillus niger. Chimeras with enhanced thermal stability contain segments from 3 or 4 of the parental enzymes. The half-lives of inactivation of the chimeras at 65°C are increased by up to 22 fold when compared to the most stable parental FAE. The release of ferulic acid from steam-exploded corn stalk using the best chimera is enhanced by 12.8fold when compared to the best parental FAE
additional information
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generation of a chimeric library from four homologous FAEs originated from fungi by a DNA shuffling strategy. Chimeras contain DNA fragments encoding the wild-type FaeA from Aspergillus terreus, FaeA from Penicillium chrysogenum and FaeA from Aspergillus flavus, as well as the M11 mutant of FaeA from Aspergillus niger. Chimeras with enhanced thermal stability contain segments from 3 or 4 of the parental enzymes. The half-lives of inactivation of the chimeras at 65°C are increased by up to 22 fold when compared to the most stable parental FAE. The release of ferulic acid from steam-exploded corn stalk using the best chimera is enhanced by 12.8fold when compared to the best parental FAE
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additional information
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generation of a truncated Feel1B variant with reduced enzyme activity
additional information
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generation of a truncated Feel1B variant with reduced enzyme activity
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additional information
introduction of mutations to provide hydrophobic environment for increased hydrolysis of sinapate substrates
additional information
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introduction of mutations to provide hydrophobic environment for increased hydrolysis of sinapate substrates
additional information
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immobilization of feruloyl esterase on mesoporous silica as support. Immobilization in mesoporous silica with larger pore size of 9 nm shows higher protein loading and higher specific activity compared to immobilization with smaller pore size of 5 nm. Adsorption into mesoporous silica changes the product specificity of the enzymes to favor transesterification and decrease the rate of hydrolysis compared to free enzymes, overview. The immobilized enzyme has a butyl ferulate yield of up to 90%, significantly higher compared to free enzyme. Additionally, the immobilized enzymes shows an excellent operational stability and reusability, retaining 70% or more of the initial activity after 6 sequential runs, each lasting 6 days
additional information
generation of a chimeric library from four homologous FAEs originated from fungi by a DNA shuffling strategy. Chimeras contain DNA fragments encoding the wild-type FaeA from Aspergillus terreus, FaeA from Penicillium chrysogenum and FaeA from Aspergillus flavus, as well as the M11 mutant of FaeA from Aspergillus niger. Chimeras with enhanced thermal stability contain segments from 3 or 4 of the parental enzymes. The half-lives of inactivation of the chimeras at 65°C are increased by up to 22 fold when compared to the most stable parental FAE. The release of ferulic acid from steam-exploded corn stalk using the best chimera is enhanced by 12.8fold when compared to the best parental FAE
additional information
expression in Pichia pastoris with an N-terminal alpha-mating factor pre-pro sequence and under the control of a methanol inducible alcohol oxidase 1 promotor
additional information
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expression in Pichia pastoris with an N-terminal alpha-mating factor pre-pro sequence and under the control of a methanol inducible alcohol oxidase 1 promotor
additional information
construction of chimeric proteins by RIBS in vivo DNA shuffling of the feruloyl esterase genes of strains Streptomyces cinnamoneus NBRC 12852 and Streptomyces cinnamoneus TH-2. A domain comprised of residues 140 to 154 is crucial for the catalytic activity of isoform EstA
additional information
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construction of chimeric proteins by RIBS in vivo DNA shuffling of the feruloyl esterase genes of strains Streptomyces cinnamoneus NBRC 12852 and Streptomyces cinnamoneus TH-2. A domain comprised of residues 140 to 154 is crucial for the catalytic activity of isoform EstA
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additional information
construction of chimeric proteins by RIBS in vivo DNA shuffling of the feruloyl esterase genes of strains Streptomyces cinnamoneus NBRC 12852 and Streptomyces cinnamoneus TH-2. insertion of residues Pro and Gly between residues Asn-152 and Ala-153, i.e. mutant 18PG, leads to increased activity with substrates methyl ferulate and methyl sinapinate
additional information
Q70Y21
additional amino acids at the N-terminus do not influence the activity
additional information
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additional amino acids at the N-terminus do not influence the activity
additional information
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additional amino acids at the N-terminus do not influence the activity
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