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Information on EC 3.1.1.73 - feruloyl esterase and Organism(s) Aspergillus niger and UniProt Accession O42807

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.73 feruloyl esterase
IUBMB Comments
Catalyses the hydrolysis of the 4-hydroxy-3-methoxycinnamoyl (feruloyl) group from an esterified sugar, which is usually arabinose in "natural" substrates. p-Nitrophenol acetate and methyl ferulate are poorer substrates. All microbial ferulate esterases are secreted into the culture medium. They are sometimes called hemicellulase accessory enzymes, since they help xylanases and pectinases to break down plant cell wall hemicellulose.
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Aspergillus niger
UNIPROT: O42807
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Word Map
The taxonomic range for the selected organisms is: Aspergillus niger
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
feruloyl esterase, ferulic acid esterase, cinii, anfaea, feruloyl esterase a, fae-iii, cinnae, type a feruloyl esterase, estf27, xylanase z, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ferulic acid esterase A
-
feruloyl esterase
-
feruloyl esterase A
feruloyl esterase B
FAEA is more active than FAEB towards wheat arabinoxylan, whereas FAEB is more active than FAEA towards sugar-beet pectin
cinnAE
cinnamic acid esterase
-
cinnamoyl ester hydrolase
-
-
-
-
Cinnamoyl esterase
FAE-I
FAE-II
FAE-III
-
-
-
-
ferulic acid esterase
ferulic acid esterase A
-
-
ferulic acid esterase B
-
feruloyl esterase
feruloyl esterase A
FAEA is more active than FAEB towards wheat arabinoxylan, whereas FAEB is more active than FAEA towards sugar-beet pectin
feruloyl esterase B
feruloyl/p-coumaroyl esterase
-
-
-
-
Feruloylesterase
-
-
-
-
hemicellulase acessory enzymes
-
-
-
-
hydroxycinnamoyl esterase
-
-
-
-
phenolic acid esterase
-
-
-
-
type B ferulic acid esterase
-
XYLD esterase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic ester hydrolysis
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
4-hydroxy-3-methoxycinnamoyl-sugar hydrolase
Catalyses the hydrolysis of the 4-hydroxy-3-methoxycinnamoyl (feruloyl) group from an esterified sugar, which is usually arabinose in "natural" substrates. p-Nitrophenol acetate and methyl ferulate are poorer substrates. All microbial ferulate esterases are secreted into the culture medium. They are sometimes called hemicellulase accessory enzymes, since they help xylanases and pectinases to break down plant cell wall hemicellulose.
CAS REGISTRY NUMBER
COMMENTARY hide
134712-49-5
-
224306-54-1
-
224306-55-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+/-)-4-O-(2-chloro-4-nitrophenyl)-1-O-feruloyl-1,2,4-butanetriol + H2O
?
show the reaction diagram
-
-
-
?
(+/-)-4-O-(2-chloro-4-nitrophenyl)-2-O-feruloyl-1,2,4-butanetriol + H2O
?
show the reaction diagram
-
-
-
?
(+/-)-4-O-(2-chloro-4-nitrophenyl)-di-1,2-O-(feruloyl)-1,2,4-butanetriol + H2O
?
show the reaction diagram
-
-
-
?
2-chloro 4-nitrophenyl 5-O-feruloyl-alpha-sc l-arabinofuranoside + H2O
?
show the reaction diagram
-
-
-
?
4-nitrophenyl 2-O-(E)-feruloyl-alpha-D-xylopyranoside + H2O
4-nitrophenyl-alpha-D-xylopyranoside + trans-ferulate
show the reaction diagram
-
-
-
?
4-nitrophenyl 3-O-(E)-feruloyl-alpha-D-xylopyranoside + H2O
4-nitrophenyl-alpha-D-xylopyranoside + trans-ferulate
show the reaction diagram
-
-
-
?
4-nitrophenyl 4-O-(E)-feruloyl-alpha-D-xylopyranoside + H2O
4-nitrophenyl-alpha-D-xylopyranoside + trans-ferulate
show the reaction diagram
-
-
-
?
4-nitrophenyl 5-O-(E)-feruloyl-alpha-L-arabinofuranoside + H2O
4-nitrophenyl alpha-L-arabinofuranoside + ferulate
show the reaction diagram
-
-
-
?
4-nitrophenyl 5-O-acetyl-alpha-L-arabinofuranoside + H2O
4-nitrophenyl-alpha-L-arabinofuranoside + acetate
show the reaction diagram
the enzyme is specialized for deferuloylation of primary hydroxyl groups, with a very strong preference for hydrolyzing 5-O-feruloyl-alpha-L-arabinofuranoside
-
-
?
4-nitrophenyl ferulate + H2O
4-nitrophenol + ferulate
show the reaction diagram
-
-
-
?
5-O-p-coumaroylquinic acid + H2O
p-coumaric acid + quinic acid
show the reaction diagram
-
-
-
?
5-O-trans-feruloyl-alpha-L-Araf + H2O
trans-ferulate + alpha-L-arabinofuranose
show the reaction diagram
-
-
-
?
arabinoxylan + H2O
ferulic acid + ?
show the reaction diagram
from wheat
-
-
?
chlorogenic acid + H2O
?
show the reaction diagram
-
-
-
?
coniferyl p-coumarate + H2O
p-coumaric acid + coniferol
show the reaction diagram
-
-
-
?
ethyl ferulate + H2O
ferulate + ethanol
show the reaction diagram
-
-
-
?
ethyl ferulate + H2O
ferulic acid + ethanol
show the reaction diagram
hydrolyzed by FAEA and not FAEB with FAEA displaying the higher activity
-
-
?
feruloyl polysaccharide + H2O
ferulic acid + ?
show the reaction diagram
involved in the degradation of plant cell wall material, breaks ferulic acid cross-links between cell wall components
-
-
?
feruloyl polysaccharide + H2O
ferulic acid + diferulic acid + arabinoxylan + lignin + ?
show the reaction diagram
involved in the degradation of plant cell wall material, breaks ferulic acid cross-links between cell wall components
-
-
?
methyl 3,5-dimethoxy-4-hydroxy-cinnamate + H2O
3,5-dimethoxy-4-hydroxycinnamic acid + methanol
show the reaction diagram
hydrolyzed only by FAEA and not FAEB
-
-
?
methyl caffeate + H2O
caffeic acid + methanol
show the reaction diagram
methyl cinnamate + H2O
cinnamic acid + methanol
show the reaction diagram
hydrolyzed only by FAEB and not FAEA
-
-
?
methyl ferulate + H2O
ferulate + methanol
show the reaction diagram
-
-
-
?
methyl ferulate + H2O
ferulic acid + methanol
show the reaction diagram
methyl ferulate + H2O
methanol + ferulate
show the reaction diagram
-
-
-
?
methyl p-coumarate + H2O
p-coumaric acid + methanol
show the reaction diagram
methyl sinapate + H2O
sinapic acid + methanol
show the reaction diagram
-
-
-
?
methyl sinapinate + H2O
sinapic acid + methanol
show the reaction diagram
-
-
-
?
n-decyl ferulate + H2O
ferulate + n-decanol
show the reaction diagram
-
-
-
?
n-hexyl ferulate + H2O
ferulate + n-hexanol
show the reaction diagram
-
-
-
?
n-propyl ferulate + H2O
ferulate + n-propanol
show the reaction diagram
-
-
-
?
O-[5-O-(trans-feruloyl)-alpha-L-Araf] + H2O
trans-ferulate + alpha-L-arabinofuranose
show the reaction diagram
-
-
-
?
O-[5-O-(trans-feruloyl)-alpha-L-Araf]-(1,3)D-Xylp + H2O
trans-ferulate + 3-O-alpha-L-arabinofuranosyl-D-xylopyranose
show the reaction diagram
-
-
-
?
pectin + H2O
ferulic acid + ?
show the reaction diagram
from sugar beet
-
-
?
sinapic acid + glycerol
glycerol sinapate + H2O
show the reaction diagram
-
-
-
?
(E)-3-[5'-((E)-2-ethoxycarbonyl-vinyl)-6,2'-dihydroxy-5,3'-dimethoxy-biphenyl-3-yl]-acrylic acid + H2O
(E)-3-[5'-((E)-2-carboxy-vinyl)-6,2'-dihydroxy-5,3'-dimethoxy-biphenyl-3-yl]-acrylic acid + ethanol
show the reaction diagram
-
-
-
-
?
(E,E)-4,4'-dihydroxy-5,5'-dimethoxy-3,3'-bicinnamic acid bis(L-arabinofuran-5-O-yl) ester + H2O
?
show the reaction diagram
-
-
-
-
?
(E,E)-4,4'-dihydroxy-5,5'-dimethoxy-3,3'-bicinnamic acid L-Arg 4-O-yl ester, beta-D-Xylp-(1->2)-L-Ara-5-O-yl ester + H2O
?
show the reaction diagram
-
-
-
-
?
(E,E)-4,4'-dihydroxy-5,5'-dimethoxy-3,3'-bicinnamic acid-bis(L-arabinofuranoside-5-O-yl)ester + H2O
?
show the reaction diagram
-
ara-5-5-ara
-
-
?
(methyl 5-O-trans-feruloyl-alpha-L-arabinofuranoside) + H2O
?
show the reaction diagram
-
chemically synthesized substrate
-
-
?
(O-beta-D-xylopyranosyl-(1-2)-(5-O-trans-feruloyl)-L-arabinofuranoside) + H2O
ferulic acid + beta-D-xylopyranosyl-1,2-L-arabinofuranoside
show the reaction diagram
-
Xyl-Ara-ferulate
-
-
?
(Z)-2-[4-((E)-2-ethoxycarbonylvinyl)-2-methoxyphenoxy]-3-(4-hydroxy-3-methoxyphenyl)-acrylic acid ethyl ester + H2O
(Z)-2-[4-((E)-2-ethoxycarbonylvinyl)-2-methoxyphenoxy]-3-(4-hydroxy-3-methoxyphenyl)-acrylic acid + ethanol
show the reaction diagram
-
-
-
-
?
2-chloro-4-nitrophenyl 5-O-feruloyl alpha-L-arabinofuranoside + H2O
ferulic acid + 2-chloro-4-nitrophenyl-L-arabinofuranoside
show the reaction diagram
-
-
-
-
?
3,4-dimethoxy cinnamic acid + glycerol
?
show the reaction diagram
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl acetate + H2O
acetic acid + 4-nitrophenol
show the reaction diagram
-
FAE-1 and FAE-2
-
-
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
alpha-L-arabinofuranose + 4-nitrophenol
show the reaction diagram
-
FAE-1 and FAE-2
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
beta-D-galactopyranose + 4-nitrophenol
show the reaction diagram
-
FAE-1 and FAE-2
-
-
?
4-nitrophenyl beta-D-mannopyranoside + H2O
beta-D-mannopyranose + 4-nitrophenol
show the reaction diagram
-
FAE-1 and FAE-2
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
beta-D-xylopyranose + 4-nitrophenol
show the reaction diagram
-
FAE-1 and FAE-2
-
-
?
4-nitrophenyl butyrate + H2O
butyric acid + 4-nitrophenol
show the reaction diagram
-
FAE-1 and FAE-2
-
-
?
4-nitrophenyl ferulate + H2O
ferulic acid + 4-nitrophenol
show the reaction diagram
-
best substrate for FAE-1 and FAE-2
-
-
?
5-bromo-4-chloro-3-indolyl 5-O-coumaroyl alpha-L-arabinofuranoside + H2O
coumaric acid + 5-bromo-4-chloro-1H-indol-3-yl-L-arabinofuranoside
show the reaction diagram
-
-
-
-
?
5-bromo-4-chloro-3-indolyl 5-O-feruloyl alpha-L-arabinofuranoside + H2O
ferulic acid + 5-bromo-4-chloro-1H-indol-3-yl-L-arabinofuranoside
show the reaction diagram
-
soluble and stable chromogenic substrates are important to devise enzyme assays that are both specific and simple to implement
-
-
?
5-O-(trans-feruloyl)-L-arabinofuranose + H2O
ferulic acid + L-arabinofuranose
show the reaction diagram
-
FAE-I, CinnAE is not active on this substrate
-
-
?
5-O-(trans-feruloyl)-L-arabinofuranoside + H2O
ferulic acid + L-arabinose
show the reaction diagram
-
ara-ferulate
-
-
?
5-O-(trans-feruloyl)-L-arabinofuranoside + H2O
L-arabinofuranose + ferulic acid
show the reaction diagram
-
-
-
-
?
5-O-caffeoyl quinic acid + H2O
?
show the reaction diagram
-
-
-
?
5-O-p-coumaroylquinic acid + H2O
p-coumaric acid + quinic acid
show the reaction diagram
-
-
-
?
5-O-trans-feruloyl-alpha-L-Araf + H2O
trans-ferulate + alpha-L-arabinofuranose
show the reaction diagram
-
-
-
?
7-hydroxy-1-(4-hydroxy-3-methoxy-phenyl)-6-methoxy-1,2-dihydro-naphthalene-2,3-dicarboxylic acid + H2O
(2S,3S)-5-((E)-2-carboxyvinyl)-2-(4-hydroxy-3-methoxyphenyl)-7-methoxy-2,3-dihydrobenzofuran-3-carboxylic acid ethyl ester + ethanol
show the reaction diagram
-
i.e. 5-(2-ethoxycarbonylvinyl)-2-(4-hydroxy-3-methoxyphenyl)-7-methoxy-2,3-dihydrobenzofuran-3-carboxylic acid ethyl ester
-
-
?
arabinoxylan + H2O
ferulic acid + ?
show the reaction diagram
arabinoxylans + H2O
ferulic acid + ?
show the reaction diagram
barley + H2O
5-5-diferulic acid + ?
show the reaction diagram
-
FAEA, presolubilized substrate
-
-
?
chlorogenic acid + H2O
?
show the reaction diagram
-
-
-
?
cinnamic acid methyl ester + H2O
cinnamic acid + methanol
show the reaction diagram
-
-
-
-
?
coniferyl p-coumarate + H2O
p-coumaric acid + coniferol
show the reaction diagram
-
-
-
?
de-starched wheat bran + H2O
ferulic acid + ?
show the reaction diagram
-
-
-
-
?
diethyl-5,5'-diferulate + 2 H2O
5,5'-diferulate + 2 ethanol
show the reaction diagram
-
-
-
-
?
diethyl-5,5'-diferulate + H2O
ethyl-5,5'-diferulate + ethanol
show the reaction diagram
-
-
-
-
?
ethyl ferulate + H2O
ethanol + ferulate
show the reaction diagram
-
-
-
?
ethyl ferulate + H2O
ferulic acid + ethanol
show the reaction diagram
ferulate + pentanol
pentanyl ferulate + H2O
show the reaction diagram
-
synthesis performed in cetyltrimethylammoniumbromide/hexane/pentanol water-in-oil microemulsion
-
-
r
ferulic acid + D-arabinose
?
show the reaction diagram
-
-
-
-
?
ferulic acid + D-fructose
?
show the reaction diagram
-
-
-
-
?
ferulic acid + D-galactose
?
show the reaction diagram
-
-
-
-
?
ferulic acid + D-glucose
?
show the reaction diagram
-
-
-
-
?
ferulic acid + D-xylose
?
show the reaction diagram
-
-
-
-
?
ferulic acid + glycerol
1-glycerol ferulate
show the reaction diagram
-
-
-
-
?
ferulic acid methyl ester + H2O
ferulic acid + methanol
show the reaction diagram
-
-
-
-
?
feruloyl polysaccharide + H2O
ferulic acid + 5,5'-diferulic acid + arabinoxylan + ?
show the reaction diagram
-
involved in the degradation of plant cell wall material, breaks ferulic acid cross-links between cell wall components
-
-
?
feruloyl polysaccharide + H2O
ferulic acid + ?
show the reaction diagram
feruloyl-polysaccharide + H2O
ferulate + polysaccharide
show the reaction diagram
-
-
-
-
?
glycerol + ferulic acid
glyceryl ferulate + H2O
show the reaction diagram
-
-
-
-
?
hemicellulose + H2O
ferulic acid + lignin + pectin + ?
show the reaction diagram
-
hydrolysis of feruloylated oligosaccharides and diferulate cross-links
-
-
?
methyl 3,5-dimethoxy-4-hydroxy-cinnamate + H2O
3,5-dimethoxy-4-hydroxycinnamic acid + methanol
show the reaction diagram
hydrolyzed only by FAEA and not FAEB
-
-
?
methyl caffeate + H2O
caffeic acid + methanol
show the reaction diagram
methyl caffeate + H2O
methanol + caffeate
show the reaction diagram
77% of the activity with methyl p-coumarate
-
-
?
methyl cinnamate + H2O
cinnamic acid + methanol
show the reaction diagram
hydrolyzed only by FAEB and not FAEA
-
-
?
methyl ferulate + H2O
ferulic acid + methanol
show the reaction diagram
methyl ferulate + H2O
methanol + ferulate
show the reaction diagram
methyl p-coumarate + H2O
4-coumaric acid + methanol
show the reaction diagram
-
-
-
-
?
methyl p-coumarate + H2O
methanol + p-coumarate
show the reaction diagram
-
-
-
?
methyl p-coumarate + H2O
p-coumaric acid + methanol
show the reaction diagram
methyl sinapinate + H2O
sinapic acid + methanol
show the reaction diagram
methyl-3,4-dimethoxy cinnamate + H2O
3,4-dimethoxycinnamic acid + methanol
show the reaction diagram
-
-
-
-
?
O-5-O-(trans-feruloyl)-alpha-L-arabinofuranosyl-(1-3)-O-beta-D-xylopyranosyl-(1-4)-D-xylopyranose + H2O
ferulic acid + alpha-L-arabinofuranosyl-(1-3)-O-beta-D-xylopyranosyl-(1-4)-D-xylopyranose
show the reaction diagram
-
-
-
-
?
O-5-O-(trans-p-coumaroyl)-alpha-L-arabinofuranosyl-(1-3)-O-beta-D-xylopyranosyl-(1-4)-D-xylopyranose + H2O
p-coumaric acid + alpha-L-arabinofuranosyl-(1-3)-O-beta-D-xylopyranosyl-(1-4)-D-xylopyranose
show the reaction diagram
-
-
-
-
?
O-beta-D-Xylp-(1->2)-[(5-O-(trans-feruloyl)-L-Araf] + H2O
?
show the reaction diagram
-
-
-
-
?
O-[5-O-(trans-feruloyl)-alpha-L-Araf] + H2O
trans-ferulate + alpha-L-arabinofuranose
show the reaction diagram
-
-
-
?
O-[5-O-(trans-feruloyl)-alpha-L-Araf]-(1,3)D-Xylp + H2O
trans-ferulate + 3-O-alpha-L-arabinofuranosyl-D-xylopyranose
show the reaction diagram
-
-
-
?
oat spelt xylan + H2O
ferulic acid + ?
show the reaction diagram
-
-
-
-
?
p-coumaric acid methyl ester + H2O
p-coumaric acid + methanol
show the reaction diagram
-
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butyric acid
show the reaction diagram
-
-
-
-
?
pectin + H2O
ferulic acid + ?
show the reaction diagram
pectins + H2O
ferulic acid + ?
show the reaction diagram
-
sugar beet and spinach
-
-
?
sinapic acid + glycerol
?
show the reaction diagram
-
-
-
-
?
sugar beet pulp + H2O
ferulic acid + ?
show the reaction diagram
-
-
-
-
?
sugar beet pulp + H2O
trans,trans-diferulic acid + ?
show the reaction diagram
-
FAEA, presolubilized substrate
-
-
?
trans,trans-diferulic acid diethyl ester + H2O
(E)-3-[5'-((E)-2-ethoxycarbonyl-vinyl)-6,2'-dihydroxy-5,3'-dimethoxy-biphenyl-3-yl]-acrylic acid + ethanol
show the reaction diagram
-
i.e. (E)-3-[5'-((E)-2-ethoxycarbonyl-vinyl)-6,2'-dihydroxy-5,3'-dimethoxy-biphenyl-3-yl]-acrylic acid ethyl ester
-
-
?
wheat bran + H2O
ferulic acid + ?
show the reaction diagram
-
FAEA, presolubilized substrate
-
-
?
wheat bran + H2O
ferulic acid + p-coumaric acid + ?
show the reaction diagram
-
-
-
-
?
xylan polysaccharide + H2O
ferulic acid + p-coumaric acid
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
arabinoxylan + H2O
ferulic acid + ?
show the reaction diagram
from wheat
-
-
?
feruloyl polysaccharide + H2O
ferulic acid + ?
show the reaction diagram
involved in the degradation of plant cell wall material, breaks ferulic acid cross-links between cell wall components
-
-
?
feruloyl polysaccharide + H2O
ferulic acid + diferulic acid + arabinoxylan + lignin + ?
show the reaction diagram
involved in the degradation of plant cell wall material, breaks ferulic acid cross-links between cell wall components
-
-
?
pectin + H2O
ferulic acid + ?
show the reaction diagram
from sugar beet
-
-
?
arabinoxylan + H2O
ferulic acid + ?
show the reaction diagram
arabinoxylans + H2O
ferulic acid + ?
show the reaction diagram
barley + H2O
5-5-diferulic acid + ?
show the reaction diagram
-
FAEA, presolubilized substrate
-
-
?
feruloyl polysaccharide + H2O
ferulic acid + 5,5'-diferulic acid + arabinoxylan + ?
show the reaction diagram
-
involved in the degradation of plant cell wall material, breaks ferulic acid cross-links between cell wall components
-
-
?
feruloyl polysaccharide + H2O
ferulic acid + ?
show the reaction diagram
feruloyl-polysaccharide + H2O
ferulate + polysaccharide
show the reaction diagram
-
-
-
-
?
hemicellulose + H2O
ferulic acid + lignin + pectin + ?
show the reaction diagram
-
hydrolysis of feruloylated oligosaccharides and diferulate cross-links
-
-
?
oat spelt xylan + H2O
ferulic acid + ?
show the reaction diagram
-
-
-
-
?
pectin + H2O
ferulic acid + ?
show the reaction diagram
pectins + H2O
ferulic acid + ?
show the reaction diagram
-
sugar beet and spinach
-
-
?
sugar beet pulp + H2O
ferulic acid + ?
show the reaction diagram
-
-
-
-
?
sugar beet pulp + H2O
trans,trans-diferulic acid + ?
show the reaction diagram
-
FAEA, presolubilized substrate
-
-
?
wheat bran + H2O
ferulic acid + ?
show the reaction diagram
-
FAEA, presolubilized substrate
-
-
?
wheat bran + H2O
ferulic acid + p-coumaric acid + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
the expression of the FAE-encoding gene is regulated by xylose, arabinose and ferulic acid
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diethyl-2-(4-hydroxy-3-methoxyphenyl)ethenephosphonate
-
methyl 5-N-arabinoferulamide
-
aminoethylbenzenesulfonylfluoride
-
-
methanol
-
-
Propanol
-
-
additional information
-
organic solvent inhibition kinetics with recombinant enzyme, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
activity is maximal after 4 days in solid state as well as in submerged fermentations (32.5 and 31.5 U/g dry weight of wheat bran respectively) and the enzyme titers are comparable
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5 - 2
4-nitrophenyl 2-O-(E)-feruloyl-alpha-D-xylopyranoside
-
1.51
4-nitrophenyl 3-O-(E)-feruloyl-alpha-D-xylopyranoside
-
0.24
4-nitrophenyl 4-O-(E)-feruloyl-alpha-D-xylopyranoside
-
0.073
4-nitrophenyl 5-O-(E)-feruloyl-alpha-L-arabinofuranoside
-
1.24
4-nitrophenyl 5-O-acetyl-alpha-L-arabinofuranoside
-
0.237
coniferyl p-coumarate
-
0.611
ethyl ferulate
pH 6.0, 40°C
12.87 - 23.35
ferulate
0.1 - 6.34
methyl ferulate
0.47
methyl p-coumarate
-
0.15 - 1.2
methyl sinapate
0.103
methyl sinapinate
-
0.008
n-decyl ferulate
pH 6.0, 40°C
0.04
n-hexyl ferulate
pH 6.0, 40°C
0.245
n-propyl ferulate
pH 6.0, 40°C
0.061
O-[5-O-(trans-feruloyl)-alpha-L-Araf]
-
0.045
O-[5-O-(trans-feruloyl)-alpha-L-Araf]-(1,3)D-Xylp
-
2
(E)-3-[5'-((E)-2-ethoxycarbonyl-vinyl)-6,2'-dihydroxy-5,3'-dimethoxy-biphenyl-3-yl]-acrylic acid
-
pH 6.1
0.14
(E)-3-[5'-((E)-2-ethoxycarbonylvinyl)-6,2'-dihydroxy-5,3'-dimethoxybiphenyl-3-yl]-acrylic acid ethyl ester
-
pH 3.2
0.08
(E,E)-4,4'-dihydroxy-5,5'-dimethoxy-3,3'-bicinnamic acid bis(L-arabinofuranosyl-5-O-yl) ester
-
pH 6.1
-
0.07 - 0.12
(E,E)-4,4'-dihydroxy-5,5'-dimethoxy-3,3'-bicinnamic acid L-Arg 4-O-yl ester, beta-D-Xylp-(1->2)-L-Ara-5-O-yl ester
-
2 - 3.3
4-nitrophenyl ferulate
0.27
5-O-(trans-feruloyl)-L-arabinofuranoside
-
pH 6.1
0.16
5-O-caffeoyl quinic acid
-
0.163
5-O-p-coumaroylquinic acid
isoenzyme FAEB
0.245
chlorogenic acid
isoenzyme FAEB
0.044
coniferyl p-coumarate
isoenzyme FAEB
0.74
diethyl-5,5'-diferulate
-
pH 6.1
0.69 - 3.4
ethyl ferulate
1.36
methyl 3,4-dimethoxycinnamate
-
-
0.13 - 4.72
methyl caffeate
0.163 - 2.08
methyl ferulate
0.02 - 4.26
methyl p-coumarate
0.24 - 1.44
methyl sinapinate
0.11
O-beta-D-Xylp-(1->2)-[(5-O-(trans-feruloyl)-L-Araf]
-
pH 6.1
-
0.132
O-[5-O-(trans-feruloyl)-alpha-L-Araf]
isoenzyme FAEB
0.044
O-[5-O-(trans-feruloyl)-alpha-L-Araf]-(1,3)D-Xylp
isoenzyme FAEB
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.17
4-nitrophenyl 2-O-(E)-feruloyl-alpha-D-xylopyranoside
-
0.7
4-nitrophenyl 3-O-(E)-feruloyl-alpha-D-xylopyranoside
-
0.24
4-nitrophenyl 4-O-(E)-feruloyl-alpha-D-xylopyranoside
-
175
4-nitrophenyl 5-O-(E)-feruloyl-alpha-L-arabinofuranoside
-
2.33
4-nitrophenyl 5-O-acetyl-alpha-L-arabinofuranoside
-
20
coniferyl p-coumarate
-
29.4
ethyl ferulate
pH 6.0, 40°C
62 - 823
ferulate
0.79 - 32.9
methyl ferulate
61
methyl sinapinate
-
4.6
n-decyl ferulate
pH 6.0, 40°C
9.8
n-hexyl ferulate
pH 6.0, 40°C
44.6
n-propyl ferulate
pH 6.0, 40°C
121
O-[5-O-(trans-feruloyl)-alpha-L-Araf]
-
95
O-[5-O-(trans-feruloyl)-alpha-L-Araf]-(1,3)D-Xylp
-
48
5-O-p-coumaroylquinic acid
isoenzyme FAEB
63
chlorogenic acid
isoenzyme FAEB
140
coniferyl p-coumarate
isoenzyme FAEB
0.01 - 234
methyl caffeate
0.99 - 70.74
methyl ferulate
0.1 - 69
methyl p-coumarate
0.031 - 84.95
methyl sinapinate
2 - 8
O-[5-O-(trans-feruloyl)-alpha-L-Araf]
isoenzyme FAEB
8
O-[5-O-(trans-feruloyl)-alpha-L-Araf]-(1,3)D-Xylp
isoenzyme FAEB
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
48
ethyl ferulate
pH 6.0, 40°C
4.3 - 41
ferulate
0.14 - 29
methyl ferulate
547
n-decyl ferulate
pH 6.0, 40°C
243
n-hexyl ferulate
pH 6.0, 40°C
182
n-propyl ferulate
pH 6.0, 40°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.45 - 2.5
diethyl-2-(4-hydroxy-3-methoxyphenyl)ethenephosphonate
1.4 - 2.9
methyl 5-N-arabinoferulamide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29.5
wild-type enzyme, substrate 4-nitrophenyl ferulate, pH 6.4, 40°C
0.0117
-
purified FAE-2, with 4-nitrophenyl alpha-L-arabinofuranoside, 4-nitrophenyl beta-D-mannopyranoside or 4-nitrophenyl beta-D-xylopyranoside as substrates
0.015
-
in submerged fermentations at 24 h
0.0167
-
purified FAE-1, with 4-nitrophenyl butyrate, 4-nitrophenyl beta-D-galactopyranoside or 4-nitrophenyl beta-D-mannopyranoside as substrates
0.02
-
purified FAE-2, with 4-nitrophenyl beta-D-galactopyranoside as substrate
0.025
-
purified FAE-1, with 4-nitrophenyl alpha-L-arabinofuranoside or 4-nitrophenyl beta-D-xylopyranoside as substrates
0.0317
-
purified FAE-2, with 4-nitrophenyl butyrate as substrate
0.0538
-
crude extract
0.07
-
methyl p-coumarate as substrate
0.102
-
purified FAE-2, with 4-nitrophenyl acetate as substrate
0.103
-
purified FAE-1, with 4-nitrophenyl acetate as substrate
0.15
-
purified FAE-1, with 4-nitrophenyl ferulate as substrate
0.1867
-
purified FAE-2, with 4-nitrophenyl ferulate as substrate
0.195
-
on day 3 in submerged fermentations, remains constant up to 5 days
0.213
-
on day 2 in solid state fermentations, decreases thereafter
0.598
-
11fold purified FAE-1
1.63
-
p-nitrophenyl butyrate
1.91
-
p-nitrophenyl butyrate
156
-
methyl sinapinate as substrate
22.4
-
methyl ferulate as substrate
3
-
de-starched wheat bran as substrate in absence of xylanase
31
-
de-starched wheat bran as substrate in presence of xylanase
38.9
-
methyl 3,4-dimethoxycinnamate as substrate
67.2
-
methyl ferulate as substrate
84.2
-
methyl p-coumarate as substrate
96.9
-
methyl caffeate as substrate
additional information
-
though the feruloyl esterase activity produced in solid state and submerged fermentations are comparable on day 5, specific activity in submerged fermentation conditions is nearly double than that of solid state ones
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
esterification reaction
9
-
purified FAE-1
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 5
-
pH 3.0: about 65% of maximal activity, pH 5.0: about 50% of maximal activity, esterification reaction
3 - 6
-
pH 3.0: about 35% of maximal activity, pH 6.0: about 50% of maximal activity, transesterification and hydrolysis reaction
5 - 10
-
FAE-1 shows about 20% activity at pH 4.0, ca. 70% activity at pH 6.0, ca. 85% activity at pH 8.0 and ca. 50% activity at pH 10.0 and. FAE-2 shows about 10% activity at pH 4.0, ca. 50% activity at pH 6.0 and pH 10, ca. 75% activity at pH 8.0 and retains about 60% at pH 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
substrate: methyl ferulate, FAEA produced in Escherichia coli (EcR)
37 - 70
-
optimum temperature for esterification and transesterification
40
-
purified FAE-1
40 - 50
-
purified FAE-2
55 - 60
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 70
-
37°C: about 55% of maximal activity, 70°C: about 10% of maximal activity, hydrolytic activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.2
calculation from sequence and verification by isoelectric focusing, FAEA produced in Aspergillus niger (AnN)
3.3
-
isoelectric focusing
4.89
calculated from the deduced amino acid sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
up to 23% of the total FAE activity is found in detergent extracts of the residues of leaf tissue of plants transformed with FAEA targeted to the endoplasmic reticulum or Golgi, particularly those plants which show higher activity in soluble extracts such as plants T36 and T38. 50%–60% of the FAEA activity is found in apoplast extracts
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
non-embryogenic cell suspension cultures of Festuca arundinacea expressing Aspergillus niger faeA targeted to the apoplast, or endoplasmic reticulum, or to the vacuole, show both reduced ferulate levels and increased levels of xylanase-mediated release of wall phenolics on autodigestion as well as increased rates of cell wall digestion in a simulated rumen environment
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FAEA_ASPNG
281
0
30537
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28550
FAEA produced in Escherichia coli, mass spectrometry
30250
FAEA produced in Aspergillus niger, mass spectrometry
36000
132000
14500
-
gel filtration, anomalous retardation of the purified enzyme
145000
-
CinnAE, gel filtration
150000
gel filtration
29000
29740
-
FAE-III, mass spectrometry
36000
63000
74000
75000
2 * 75000, SDS-PAGE, native mass by gel filtration
75800
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x *40000, SDS-PAGE
dimer
monomer
-
1* 50000, SDS-PAGE, purified FAE-1. 1* 55000, SDS-PAGE, purified FAE-2
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
glycosylation at Asp79
glycoprotein
18 glycosylation sides
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method
hanging drop vapor diffusion method, FAEA produced in Aspergillus niger (AnN) and Escherichia coli (EcR)
hanging drop vapor diffusion method
-
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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/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
S133A
-
inactive
W260S
-
significantly reduced turnover, increase in alpha-helix content, broadening of substrate specificity allowing the hydrolysis of methyl caffeate
W260V
-
significantly reduced turnover, increase in alpha-helix content, broadening of substrate specificity allowing the hydrolysis of methyl caffeate
Y80S
-
significantly reduced turnover, increase in alpha-helix content, broadening of substrate specificity allowing the hydrolysis of methyl caffeate
Y80V
-
significantly reduced turnover, increase in alpha-helix content, broadening of substrate specificity allowing the hydrolysis of methyl caffeate
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
-
both FAE-1 and FAE-2 are stable at alkaline pH, retaining ca. 50% of their original activity at pH 10 after 2 h of incubation
710685
4 - 9.5
-
30°C, 16 h, more than 80% of the initial activity remains
678379
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
half-lives of wild-type enzyme and mutants S92A and D174A is 8 min, half-life of mutant D93G is 9.4 min, and of mutant S187F 60.5 min
60
wild-type half-life 8.3 min, half-lifes of mutants D93G/S187/C235I, D93G/S187F/C235N, D93G/S187F/C235S, D93G/S187F/C235V, D93G/S187F/C235R 9.8 to 14 min
63
30 min, mutant D93G/S187F shows a loss of around 70-80% activity, mutant C235S shows a loss of about 10% activity
70
wild-type half-life 1.6 min, half-lifes of mutants D93G/S187/C235I, D93G/S187F/C235N, D93G/S187F/C235S, D93G/S187F/C235V, D93G/S187F/C235R 21 to 63 min
30 - 40
-
60% of the activities are retained when FAE-1 and FAE-2 are preincubated at 50°C for 30 min
45 - 50
10-16% loss of activity within 120 min
55
half life: 30 min
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
when enzyme is stored in aqueous solution activity drops to about 50% within 48 h and than remains constant for 40 days
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, stable for at least 2 months after hydrophobic interaction chromatography
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
fusion protein of the Trichoderma reesei swollenin I (SWOI) and Aspergillus niger feruloyl esterase A (FAEA) expressed in Escherichia coli
recombinant enzyme
cinnamoyl esterase FAEA
-
FAE-1 and FAE-2, to homogeneity from the day 5 culture filtrate grown in submerged fermentations, by ammonium sulphate precipitation and ion exchange chromatography, 11fold and 24.8fold, with a recovery of 10 and 8.4%, respectively
-
recombinant enzyme
-
recombinant enzyme using His-tag
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
chimeric enzyme associating FAEA and a dockerin from Clostridium thermocellum expressed in Aspergillus niger
expressed in Aspergillus oryzae
expression in Escherichia coli
expression in Pichia pastoris
expression of of a fusion protein of the Trichoderma reesei swollenin I (SWOI) and Aspergillus niger feruloyl esterase A (FAEA) in Escherichia coli
expression of wild-type and mutant enzymes in Pichia pastoris strain KM71
expressed as His-tag fusion protein in a protease deficient Aspergillus niger strain
expressed in Aspergillus niger strain D15-26 (pyrg-)
-
expressed in Pichia pastoris
-
expression in Escherichia coli
-
expression in Hypocrea jecorina
expression in Triticum aestivum under the control of the endosperm-specific 1DX5 glutenin promoter, with and without the endoplasmic reticulum retention signal (Lys-Asp-Glu-Leu) KDEL, the transgenic plants accumulate recombinant ferulic acid esterase in the endosperm. No qualitative differences are observed whether KDEL is added or not
-
gene faeB, subcloned into pEACH vector without its own N-terminal signal peptide coding region, but containing different signaling peptides to target the enzyme to the apoplast, chloroplast, endoplasmic reticulum, and vacuole. Four constructs harboring faeB are transiently expressed in Nicotiana tabacum leaves, with the enzyme accumulating at high levels in all target sites, except chloroplast. Stable expression in Medicago sativa using Agrobacterium tumefaciens strain LBA4404 transformation method
genetically modified Festuca arundinacea plants are produced expressing an Aspergillus niger ferulic acid esterase (FAEA) targeted to the vacuole. The rice actin promoter proved to be effective for FAEA expression, as does the cauliflower mosaic virus (CaMV) 35S and maize ubiquitin promoters. Higher levels of expression are found with inducible heat-shock and senescence promoters.
-
genetically modified Festuca arundinacea plants are produced expressing an Aspergillus niger ferulic acid esterase targeted to the vacuole. The rice actin promoter proved to be effective for FAEA expression, as did the cauliflower mosaic virus (CaMV) 35S and maize ubiquitin promoters. Higher levels of expression are found with inducible heat-shock and senescence promoters
-
PCR cloning and sequence analysis, gene faeA encoding ferulic acid esterase cloned, the gene product FAEA overexpressed in wild-type Aspergillus tubingensis and protease-deficient Aspergillus niger mutant, gene product is identical with Aspergillus niger FAE-III
-
production of transgenic plants of Lolium multiflorum expressing a ferulic acid esterase gene from Aspergillus niger, targeted to the vacuole under a constitutive rice actin promoter. The level of FAE activity is found to vary with leaf age and is highest in young leaves
-
recombinant expression in Pichia pastoris
-
transgenic Festuca arundinacea lines expressing the faeA gene under the rice actin, heat-shock and senescence promoters
-
Y80 and W260 mutants expressed in Pichia pastoris
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of EstA is controlled by the XlnR transcriptional activator
expression of the faeA gene is much lower with the native fungal Aspergillus apoplast sequence
-
expression of the faeA gene under the control of the rice actin promoter, is highest when FAEA is targeted to the apoplast with the plant-derived N-terminal apoplast targeting motifs from the potato protease inhibitor or with the mutated barley aleurain vacuole signal sequence. Endoplasmic reticulum-targeted and Golgi-targeted plants show intermediate FAE activities. FAE activity varies with leaf age, with the highest activities in young leaves
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
the thermal unfolding of the parental enzyme is irreversible on all the tested conditions, while that of the Cys235 mutants is reversible, and their ability to refold is highly dependent on the denaturing temperature. Mutants denatured at 75°C are able to efficiently reverse the unfolding to regain native structure during the cooling process
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation
feruloyl esterases A is a tool for the release of phenolic compounds from agro-industrial by-products (wheat straw, sugar beet pulp and maize bran)
synthesis
agriculture
biotechnology
-
ability of the enzyme to be active in alkaline pH may be advantageous in biotechnological applications and especially in the treatment of alkaline woodpulp
degradation
industry
-
targeting FAEA expression to the Golgi or apoplast is likely to be an effective strategy for improving wall digestibility in grass species used for fodder or cellulosic ethanol production
nutrition
broad range of application in the agri-food industries, production of ferulic as food preservative and as potential precursor for the production of flavor and photo-active agents
paper production
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Faulds, C.B.; Williamson, G.
The purification and characterization of 4-hydroxy-3-methoxycinnamic (ferulic) acid esterase from Streptomyces olivochromogenes
J. Gen. Microbiol.
137
2339-2345
1991
Aspergillus niger, Neocallimastix sp., Schizophyllum commune, Streptomyces olivochromogenes, Streptomyces olivochromogenes NRCC 2258
Manually annotated by BRENDA team
Borneman, W.S.; Ljungdahl, L.G.; Hartley, R.D.; Akin, D.E.
Purification and partial characterization of two feruloyl esterases from the anaerobic fungus Neocallimastix strain MC-2
Appl. Environ. Microbiol.
58
3762-3766
1992
Aspergillus niger, Neocallimastix sp., Schizophyllum commune, Streptomyces olivochromogenes
Manually annotated by BRENDA team
Faulds, C.B.; Williamson, G.
Purification and characterization of a ferulic acid esterase (FAE-III) from Aspergillus niger: specificity for the phenolic moiety and binding to microcrystalline cellulose
Microbiology
140
779-787
1994
Aspergillus niger, Acetivibrio thermocellus, Talaromyces pinophilus, Pseudomonas fluorescens, Streptomyces olivochromogenes
-
Manually annotated by BRENDA team
McCrae, S.I.; Leith, K.M.; Gordon, A.H.; Wood, T.M.
Xylan-degrading enzyme system produced by the fungus Aspergillus awamori: isolation and characterization of a feruloyl esterase and a p-coumaroyl esterase
Enzyme Microb. Technol.
16
826-834
1994
Aspergillus awamori, Aspergillus niger, Aspergillus oryzae, Aspergillus phoenicis, Fibrobacter succinogenes, Neocallimastix sp., Talaromyces pinophilus, Schizophyllum commune, Streptomyces olivochromogenes, Streptomyces viridosporus, Aspergillus awamori IMI 142717
-
Manually annotated by BRENDA team
Kroon, P.A.; Faulds, C.B.; Williamson, G.
Purification and characterization of a novel esterase induced by growth of Aspergillus niger on sugar-beet pulp
Biotechnol. Appl. Biochem.
23
255-262
1996
Aspergillus niger, Neocallimastix sp., Talaromyces pinophilus, Schizophyllum commune, Streptomyces olivochromogenes, Streptomyces viridosporus, Aspergillus niger CS 180
Manually annotated by BRENDA team
Donaghy, J.; McKay, A.M.
Purification and characterization of a feruloyl esterase from the fungus Penicillium expansum
J. Appl. Microbiol.
83
718-726
1997
Aspergillus niger, Fibrobacter succinogenes, Neocallimastix sp., Penicillium expansum, Talaromyces pinophilus, Schizophyllum commune, Streptomyces olivochromogenes
Manually annotated by BRENDA team
De Vries, R.P.; Michelsen, B.; Poulsen, C.H.; Kroon, P.A.; van den Heuvel, R.H.; Faulds, C.B.; Williamson, G.; van den Hombergh, J.P.; Visser, J.
The faeA genes from Aspergillus niger and Aspergillus tubingensis encode ferulic acid esterases involved in degradation of complex cell wall polysaccharides
Appl. Environ. Microbiol.
63
4638-4644
1997
Aspergillus niger, Aspergillus niger N402, Aspergillus tubingensis, Butyrivibrio fibrisolvens
Manually annotated by BRENDA team
Koseki, T.; Furuse, S.; Iwano, K.; Matsuzawa, H.
Purification and characterization of a feruloylesterase from Aspergillus awamori
Biosci. Biotechnol. Biochem.
62
2032-2034
1998
Aspergillus awamori, Aspergillus niger, Aspergillus oryzae, Streptomyces olivochromogenes
Manually annotated by BRENDA team
Ferreira, P.; Diez, N.; Gutierrez, C.; Soliveri, J.; Copa-Patino, J.L.
Streptomyces avermitilis CECT 3339 produces a ferulic acid esterase able to release ferulic acid from sugar beet pulp soluble feruloylated oligosaccharides
J. Sci. Food Agric.
79
440-442
1999
Aspergillus niger, Streptomyces sp., Pseudomonas fluorescens, Streptomyces olivochromogenes, Streptomyces avermitilis, Streptomyces sp. C-248, Streptomyces avermitilis CECT 3339
Manually annotated by BRENDA team
Dzedzyulya, E.I.; Becker, E.G.; Okunev, O.N.; Sinitsyn, A.P.
Feruloyl esterase from Aspergillus sp.: Purification, properties, and action on natural substrates
Biochemistry (Moscow)
64
405-410
1999
Aspergillus awamori, Aspergillus niger, Aspergillus sp.
Manually annotated by BRENDA team
Garcia-Conesa, M.T.; Kroon, P.A.; Ralph, J.; Mellon, F.A.; Colquhoun, I.J.; Saulnier, L.; Thibault, J.F.; Williamson, G.
A cinnamoyl esterase from Aspergillus niger can break plant cell wall cross-links without release of free diferulic acids
Eur. J. Biochem.
266
644-652
1999
Aspergillus niger, Pseudomonas fluorescens
Manually annotated by BRENDA team
Blum, D.L.; Kataeva, I.A.; Li, X.L.; Ljungdahl, L.G.
Feruloyl esterase activity of the Clostridium thermocellum cellulosome can be attributed to previously unknown domains of XynY and XynZ
J. Bacteriol.
182
1346-1351
2000
Aspergillus niger, Aspergillus tubingensis, Butyrivibrio fibrisolvens, Acetivibrio thermocellus, Neocallimastix sp., no activity in Escherichia coli, Orpinomyces sp., Pseudomonas fluorescens, Ruminococcus sp., Acetivibrio thermocellus JW20
Manually annotated by BRENDA team
Blum, D.L.; Schubot, F.D.; Ljungdahl, L.G.; Rose, J.P.; Wang, B.C.
Crystallization and preliminary x-ray analysis of the Clostridium thermocellum cellulosome xylanase Z feruloyl esterase domain
Acta Crystallogr. Sect. D
56
1027-1029
2000
Aspergillus niger, Aspergillus tubingensis, Butyrivibrio fibrisolvens, Acetivibrio thermocellus, Orpinomyces sp., Piromyces sp. 'equi', Pseudomonas fluorescens
-
Manually annotated by BRENDA team
Kroon, P.A.; Williamson, G.; Fish, N.M.; Archer, D.B.; Belshaw, N.J.
A modular esterase from Penicillium funiculosum which releases ferulic acid from plant cell walls and binds crystalline cellulose contains a carbohydrate binding module
Eur. J. Biochem.
267
6740-6752
2000
Aspergillus awamori, Aspergillus niger, Aspergillus sp., Butyrivibrio fibrisolvens, Acetivibrio thermocellus, Orpinomyces sp., Talaromyces funiculosus, Piromyces sp. 'equi', Talaromyces funiculosus IMI-134756
Manually annotated by BRENDA team
McAuley, K.E.; Svendsen, A.; Patkar, S.A.; Wilson, K.S.
Structure of a feruloyl esterase from Aspergillus niger
Acta Crystallogr. Sect. D
60
878-887
2004
Aspergillus niger (O42807), Aspergillus niger
Manually annotated by BRENDA team
Faulds, C.B.; Sancho, A.I.; Bartolome, B.
Mono- and dimeric ferulic acid release from brewer's spent grain by fungal feruloyl esterases
Appl. Microbiol. Biotechnol.
60
489-494
2002
Aspergillus niger, Humicola insolens
Manually annotated by BRENDA team
Record, E.; Asther, M.; Sigoillot, C.; Pages, S.; Punt, P.J.; Delattre, M.; Haon, M.; van den Hondel, C.A.; Sigoillot, J.C.; Lesage-Meessen, L.
Overproduction of the Aspergillus niger feruloyl esterase for pulp bleaching application
Appl. Microbiol. Biotechnol.
62
349-355
2003
Aspergillus niger
Manually annotated by BRENDA team
de Vries, R.P.; vanKuyk, P.A.; Kester, H.C.; Visser, J.
The Aspergillus niger faeB gene encodes a second feruloyl esterase involved in pectin and xylan degradation and is specifically induced in the presence of aromatic compounds
Biochem. J.
363
377-386
2002
Aspergillus niger (O42807), Aspergillus niger (Q8WZI8), Aspergillus niger
Manually annotated by BRENDA team
Giuliani, S.; Piana, C.; Setti, L.; Hochkoeppler, A.; Pifferi, P.G.; Williamson, G.; Faulds, C.B.
Synthesis of pentylferulate by a feruloyl esterase from Aspergillus niger using water-in-oil microemulsions
Biotechnol. Lett.
23
325-330
2001
Aspergillus niger
-
Manually annotated by BRENDA team
Faulds, C.B.; Molina, R.; Gonzalez, R.; Husband, F.; Juge, N.; Sanz-Aparicio, J.; Hermoso, J.A.
Probing the determinants of substrate specificity of a feruloyl esterase, AnFaeA, from Aspergillus niger
FEBS J.
272
4362-4371
2005
Aspergillus niger
Manually annotated by BRENDA team
Hermoso, J.A.; Sanz-Aparicio, J.; Molina, R.; Juge, N.; Gonzalez, R.; Faulds, C.B.
The crystal structure of feruloyl esterase A from Aspergillus niger suggests evolutive functional convergence in feruloyl esterase family
J. Mol. Biol.
338
495-506
2004
Aspergillus niger
Manually annotated by BRENDA team
Asther, M.; Haon, M.; Roussos, S.; Record, E.; Delattre, M.; Lesage-Meessen, L.; Labat, M.; Asther, M.
Feruloyl esterase from Aspergillus niger: a comparison of the production in solid state and submerged fermentation
Process Biochem.
38
685-691
2002
Aspergillus niger, Aspergillus niger I-1472
-
Manually annotated by BRENDA team
Levasseur, A.; Benoit, I.; Asther, M.; Asther, M.; Record, E.
Homologous expression of the feruloyl esterase B gene from Aspergillus niger and characterization of the recombinant enzyme
Protein Expr. Purif.
37
126-133
2004
Aspergillus niger (Q8WZI8), Aspergillus niger, Aspergillus niger BRFM131 (Q8WZI8)
Manually annotated by BRENDA team
Fazary, A.E.; Ju, Y.H.
Feruloyl esterases as biotechnological tools: current and future perspectives
Acta Biochim. Biophys. Sin.
39
811-828
2007
Aspergillus nidulans, Aspergillus sp., Aureobasidium pullulans, Thermothelomyces heterothallicus, Thermoclostridium stercorarium, Acetivibrio thermocellus, Fusarium oxysporum, Penicillium expansum, Talaromyces pinophilus, Talaromyces stipitatus, Pseudomonas fluorescens, Streptomyces olivochromogenes, Fusarium proliferatum, Aspergillus niger (O42807), Talaromyces funiculosus (Q9HE18), Neurospora crassa (Q9HGR3), Aspergillus awamori (Q9P979)
Manually annotated by BRENDA team
Buanafina, M.M.; Langdon, T.; Hauck, B.; Dalton, S.J.; Morris, P.
Manipulating the phenolic acid content and digestibility of italian ryegrass (Lolium multiflorum) by vacuolar-targeted expression of a fungal ferulic acid esterase
Appl. Biochem. Biotechnol.
129-132
416-426
2006
Aspergillus niger
Manually annotated by BRENDA team
Wong, D.W.
Feruloyl esterase: a key enzyme in biomass degradation
Appl. Biochem. Biotechnol.
133
87-112
2006
Aspergillus awamori, Aspergillus oryzae, Acetivibrio thermocellus, Fusarium oxysporum, Neocallimastix sp., Penicillium expansum, Pseudomonas fluorescens, Streptomyces olivochromogenes, Aspergillus niger (O42807), Talaromyces funiculosus (Q9HE18), Neurospora crassa (Q9HGR3), Piromyces sp. 'equi' (Q9Y871)
Manually annotated by BRENDA team
Levasseur, A.; Saloheimo, M.; Navarro, D.; Andberg, M.; Monot, F.; Nakari-Setaelae, T.; Asther, M.; Record, E.
Production of a chimeric enzyme tool associating the Trichoderma reesei swollenin with the Aspergillus niger feruloyl esterase A for release of ferulic acid
Appl. Microbiol. Biotechnol.
73
872-880
2006
Aspergillus niger (O42807), Aspergillus niger
Manually annotated by BRENDA team
Tsuchiyama, M.; Sakamoto, T.; Fujita, T.; Murata, S.; Kawasaki, H.
Esterification of ferulic acid with polyols using a ferulic acid esterase from Aspergillus niger
Biochim. Biophys. Acta
1760
1071-1079
2006
Aspergillus niger
Manually annotated by BRENDA team
Benoit, I.; Navarro, D.; Marnet, N.; Rakotomanomana, N.; Lesage-Meessen, L.; Sigoillot, J.C.; Asther, M.; Asther, M.
Feruloyl esterases as a tool for the release of phenolic compounds from agro-industrial by-products
Carbohydr. Res.
341
1820-1827
2006
Aspergillus niger (O42807), Aspergillus niger (Q8WZI8)
Manually annotated by BRENDA team
Marmuse, L.; Asther, M.; Navarro, D.; Lesage-Meessen, L.; Asther, M.; Fort, S.; Driguez, H.
Chromogenic substrates for feruloyl esterases
Carbohydr. Res.
342
2316-2321
2007
Aspergillus niger (O42807), Aspergillus niger (Q8WZI8)
Manually annotated by BRENDA team
Benoit, I.; Asther, M.; Sulzenbacher, G.; Record, E.; Marmuse, L.; Parsiegla, G.; Gimbert, I.; Asther, M.; Bignon, C.
Respective importance of protein folding and glycosylation in the thermal stability of recombinant feruloyl esterase A
FEBS Lett.
580
5815-5821
2006
Aspergillus niger (O42807)
Manually annotated by BRENDA team
Tapin, S.; Sigoillot, J.; Asther, M.; Petit-Conil, M.
Feruloyl esterase utilization for simultaneous processing of nonwood plants into phenolic compounds and pulp fibers
J. Agric. Food Chem.
54
3697-3703
2006
Aspergillus niger
Manually annotated by BRENDA team
Puchart, V.; Vrsanska, M.; Mastihubova, M.; Topakas, E.; Vafiadi, C.; Faulds, C.B.; Tenkanen, M.; Christakopoulos, P.; Biely, P.
Substrate and positional specificity of feruloyl esterases for monoferuloylated and monoacetylated 4-nitrophenyl glycosides
J. Biotechnol.
127
235-243
2007
Aspergillus niger (O42807), Aspergillus niger, Aspergillus oryzae, Fusarium oxysporum, Talaromyces stipitatus
Manually annotated by BRENDA team
Buanafina, M.M.; Langdon, T.; Hauck, B.; Dalton, S.; Morris, P.
Expression of a fungal ferulic acid esterase increases cell wall digestibility of tall fescue (Festuca arundinacea)
Plant Biotechnol. J.
6
264-280
2007
Aspergillus niger
Manually annotated by BRENDA team
Topakas, E.; Vafiadi, C.; Christakopoulos, P.
Microbial production, characterization and applications of feruloyl esterases
Process Biochem.
42
497-509
2007
Aspergillus oryzae, Aureobasidium pullulans, Aspergillus niger (O42807), Aspergillus niger (Q8WZI8), Aspergillus tubingensis (O42815), Acetivibrio thermocellus (P10478), Butyrivibrio fibrisolvens (P70884), Butyrivibrio fibrisolvens (P94315), Aspergillus nidulans (Q5BCF8), Aspergillus awamori (Q9P979)
-
Manually annotated by BRENDA team
Benoit, I.; Coutard, B.; Oubelaid, R.; Asther, M.; Bignon, C.
Expression in Escherichia coli, refolding and crystallization of Aspergillus niger feruloyl esterase A using a serial factorial approach
Protein Expr. Purif.
55
166-174
2007
Aspergillus niger
Manually annotated by BRENDA team
Matsuo, T.; Kobayashi, T.; Kimura, Y.; Tsuchiyama, M.; Oh, T.; Sakamoto, T.; Adachi, S.
Synthesis of glyceryl ferulate by immobilized ferulic acid esterase
Biotechnol. Lett.
30
2151-2156
2008
Aspergillus niger
Manually annotated by BRENDA team
Benoit, I.; Danchin, E.G.; Bleichrodt, R.; Vries, R.P.
Biotechnological applications and potential of fungal feruloyl esterases based on prevalence, classification and biochemical diversity
Biotechnol. Lett.
30
387-396
2008
Aspergillus niger, Aspergillus oryzae, Thermothelomyces heterothallicus, Penicillium brevicompactum, Talaromyces stipitatus, Talaromyces stipitatus (Q70Y21), Piromyces sp. E2 (Q870B0), Piromyces sp. 'equi' (Q9Y871)
Manually annotated by BRENDA team
Vafiadi, C.; Topakas, E.; Nahmias, V.R.; Faulds, C.B.; Christakopoulos, P.
Feruloyl esterase-catalysed synthesis of glycerol sinapate using ionic liquids mixtures
J. Biotechnol.
139
124-129
2009
Aspergillus niger (O42807)
Manually annotated by BRENDA team
Marmuse, L.; Asther, M.; Fabre, E.; Navarro, D.; Lesage-Meessen, L.; Asther, M.; ODonohue, M.; Fort, S.; Driguez, H.
New chromogenic substrates for feruloyl esterases
Org. Biomol. Chem.
6
1208-1214
2008
Aspergillus niger
Manually annotated by BRENDA team
Koseki, T.; Fushinobu, S.; Ardiansyah, S.; Shirakawa, H.; Komai, M.
Occurrence, properties, and applications of feruloyl esterases
Appl. Microbiol. Biotechnol.
84
803-810
2009
Aspergillus luchuensis, Aspergillus niger, Aspergillus niger (O42807), Aspergillus niger (Q8WZI8), Aspergillus oryzae, Aureobasidium pullulans, Thermothelomyces heterothallicus, Acetivibrio thermocellus, Fusarium oxysporum, Neocallimastix sp., Talaromyces stipitatus, Cellvibrio japonicus, Salmonella enterica subsp. enterica serovar Typhimurium (G2QND5), Aspergillus tubingensis (O42815), Penicillium chrysogenum (Q3V6C9), Aspergillus nidulans (Q5BCF8), Piromyces sp. E2 (Q870B0), Talaromyces funiculosus (Q9HE18), Neurospora crassa (Q9HGR3), Orpinomyces sp. PC-2 (Q9P8Y0), Aspergillus awamori (Q9P979), Piromyces sp. 'equi' (Q9Y871)
Manually annotated by BRENDA team
Buanafina, M.M.; Langdon, T.; Hauck, B.; Dalton, S.; Timms-Taravella, E.; Morris, P.
Targeting expression of a fungal ferulic acid esterase to the apoplast, endoplasmic reticulum or golgi can disrupt feruloylation of the growing cell wall and increase the biodegradability of tall fescue (Festuca arundinacea)
Plant Biotechnol. J.
8
316-331
2010
Aspergillus niger
Manually annotated by BRENDA team
Hegde, S.; Muralikrishna, G.
Isolation and partial characterization of alkaline feruloyl esterases from Aspergillus niger CFR 1105 grown on wheat bran
World J. Microbiol. Biotechnol.
25
1963-1969
2009
Aspergillus niger, Aspergillus niger CFR 1105
-
Manually annotated by BRENDA team
Zhang, S.B.; Wu, Z.L.
Identification of amino acid residues responsible for increased thermostability of feruloyl esterase A from Aspergillus niger using the PoPMuSiC algorithm
Biores. Technol.
102
2093-2096
2011
Aspergillus niger (O42807), Aspergillus niger, Aspergillus niger CIB 423.1 (O42807), Aspergillus niger CIB 423.1
Manually annotated by BRENDA team
Faulds, C.B.; Perez-Boada, M.; Martinez, A.T.
Influence of organic co-solvents on the activity and substrate specificity of feruloyl esterases
Biores. Technol.
102
4962-4967
2011
Aspergillus niger, Neurospora crassa, Talaromyces stipitatus
Manually annotated by BRENDA team
Harholt, J.; Bach, I.C.; Lind-Bouquin, S.; Nunan, K.J.; Madrid, S.M.; Brinch-Pedersen, H.; Holm, P.B.; Scheller, H.V.
Generation of transgenic wheat (Triticum aestivum L.) accumulating heterologous endo-xylanase or ferulic acid esterase in the endosperm
Plant Biotechnol. J.
8
351-362
2010
Aspergillus niger, no activity in Triticum aestivum
Manually annotated by BRENDA team
Zhang, S.B.; Pei, X.Q.; Wu, Z.L.
Multiple amino acid substitutions significantly improve the thermostability of feruloyl esterase A from Aspergillus niger
Biores. Technol.
117
140-147
2012
Aspergillus niger (O42807), Aspergillus niger, Aspergillus niger CIB 423.1 (O42807)
Manually annotated by BRENDA team
Badhan, A.; Jin, L.; Wang, Y.; Han, S.; Kowalczys, K.; Brown, D.C.; Ayala, C.J.; Latoszek-Green, M.; Miki, B.; Tsang, A.; McAllister, T.
Expression of a fungal ferulic acid esterase in alfalfa modifies cell wall digestibility
Biotechnol. Biofuels
7
39
2014
Aspergillus niger (Q8WZI8)
Manually annotated by BRENDA team
Li, J.; Zhang, S.; Yi, Z.; Pei, X.; Wu, Z.
Removal of the free cysteine residue reduces irreversible thermal inactivation of feruloyl esterase: evidence from circular dichroism and fluorescence spectra
Acta Biochim. Biophys. Sin. (Shanghai)
47
612-619
2015
Aspergillus niger (O42807), Aspergillus niger
Manually annotated by BRENDA team
Chen, X.; Zhou, M.; Huang, Z.; Jia, G.; Liu, G.; Zhao, H.
Codon optimization of Aspergillus niger feruloyl esterase and its expression in Pichia pastoris
Biologia
71
626-631
2016
Aspergillus niger (O42807)
-
Manually annotated by BRENDA team
Buanafina, M.M.; Dalton, S.; Langdon, T.; Timms-Taravella, E.; Shearer, E.A.; Morris, P.
Functional co-expression of a fungal ferulic acid esterase and a beta-1,4 endoxylanase in Festuca arundinacea (tall fescue) modifies post-harvest cell wall deconstruction
Planta
242
97-111
2015
Aspergillus niger
Manually annotated by BRENDA team
Li, J.; Pei, X.; Zhang, S.; Wu, Z.
Improving the thermostability of feruloyl esterase by DNA shuffling and site-directed mutagenesis
Process Biochem.
50
1783-1787
2015
Aspergillus niger (O42807), Aspergillus terreus (Q0CBM7), Aspergillus flavus (R9UUB4), Penicillium chrysogenum (S5Q8E1), Aspergillus terreus NIH 2624 (Q0CBM7)
-
Manually annotated by BRENDA team
Schaer, A.; Sprecher, I.; Topakas, E.; Faulds, C.B.; Nystroem, L.
Hydrolysis of nonpolar n-alkyl ferulates by feruloyl esterases
J. Agric. Food Chem.
64
8549-8554
2016
Acetivibrio thermocellus, rumen bacterium, Thermothelomyces thermophilus (G2QND5), Aspergillus niger (O42807), Thermothelomyces thermophilus DSM 1799 (G2QND5)
Manually annotated by BRENDA team
Morris, P.; Dalton, S.; Langdon, T.; Hauck, B.; de Buanafina, M.M.O.
Expression of a fungal ferulic acid esterase in suspension cultures of tall fescue (Festuca arundinacea) decreases cell wall feruloylation and increases rates of cell wall digestion
Plant Cell Tissue Organ Cult.
129
181-193
2017
Aspergillus niger (O42807), Aspergillus niger
Manually annotated by BRENDA team
Long, L.; Zhao, H.; Ding, D.; Xu, M.; Ding, S.
Heterologous expression of two Aspergillus niger feruloyl esterases in Trichoderma reesei for the production of ferulic acid from wheat bran
Bioprocess Biosyst. Eng.
41
593-601
2018
Aspergillus niger (A0A2I6U1R0), Aspergillus niger (A0A2I6U1R5), Aspergillus niger, Aspergillus niger 0913 (A0A2I6U1R0), Aspergillus niger 0913 (A0A2I6U1R5)
Manually annotated by BRENDA team
Dilokpimol, A.; Maekelae, M.R.; Varriale, S.; Zhou, M.; Cerullo, G.; Gidijala, L.; Hinkka, H.; Bras, J.L.A.; Juetten, P.; Piechot, A.; Verhaert, R.; Hilden, K.S.; Faraco, V.; de Vries, R.P.
Fungal feruloyl esterases Functional validation of genome mining based enzyme discovery including uncharacterized subfamilies
New Biotechnol.
41
9-14
2018
Thermothelomyces thermophilus (G2QND5), Aspergillus niger (Q8WZI8), Thermothelomyces thermophilus DSM 1799 (G2QND5)
Manually annotated by BRENDA team