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Information on EC 3.1.1.73 - feruloyl esterase and Organism(s) Aspergillus oryzae and UniProt Accession Q75P26
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3.1.1.73 feruloyl esteraseIUBMB 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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Word Map
- 3.1.1.73
- aspergillus
- esterases
- wheat
- niger
- bran
- xylans
- arabinoxylans
-
hydroxycinnamic
-
p-coumaric
- thermocellum
- hemicellulose
-
destarched
- caffeate
- fermentum
- degradation
- synthesis
-
talaromyces
-
xylanolytic
- xylanases
-
diferulic
-
psycinfo
- sinapinate
- nutrition
- spelt
- arabinofuranosidase
-
ester-linked
-
ensile
-
lignocellulolytic
- awamori
- acetylxylan
- neocallimastix
-
fibrolytic
- food industry
- agriculture
- paper production
- biotechnology
- pharmacology
- biofuel production
- industry
- medicine
The taxonomic range for the selected organisms is: Aspergillus oryzae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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, xylanase z, fae-ii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cinnAE
-
-
-
-
cinnamoyl ester hydrolase
-
-
-
-
Cinnamoyl esterase
-
-
-
-
EstA
-
-
-
-
FAE-I
-
-
-
-
FAE-II
-
-
-
-
FAE-III
-
-
-
-
FAEA
-
-
-
-
ferulic acid esterase
-
-
-
-
feruloyl/p-coumaroyl esterase
-
-
-
-
Feruloylesterase
-
-
-
-
hemicellulase acessory enzymes
-
-
-
-
hydroxycinnamoyl esterase
-
-
-
-
phenolic acid esterase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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
134712-49-5
-
224306-54-1
-
224306-55-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl 2-O-acetyl-alpha-L-arabinofuranoside + H2O
4-nitrophenyl-alpha-L-arabinofuranoside + acetate
-
-
-
-
?
4-nitrophenyl 2-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl-beta-D-xylopyranoside + acetate
-
-
-
-
?
4-nitrophenyl 2-O-trans-feruloyl-alpha-L-arabinofuranoside + H2O
ferulic acid + 4-nitrophenyl alpha-L-arabinofuranoside
4-nitrophenyl 3-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl-beta-D-xylopyranoside + acetate
-
-
-
-
?
4-nitrophenyl 4-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl-beta-D-xylopyranoside + acetate
-
-
-
-
?
4-nitrophenyl 5-O-acetyl-alpha-L-arabinofuranoside + H2O
4-nitrophenyl-alpha-L-arabinofuranoside + acetate
-
-
-
-
?
4-nitrophenyl 5-O-trans-feruloyl-alpha-L-arabinofuranoside + H2O
ferulic acid + 4-nitrophenyl alpha-L-arabinofuranoside
alpha-naphthyl propionate + H2O
alpha-naphthol + propionate
-
-
-
?
ethyl ferulate + H2O
ethanol + ferulate
no substrate of wild-type, but substrate of mutants W144Y and W142F
-
-
?
feruloyl polysaccharide + H2O
ferulic acid + ?
-
involved in the degradation of plant cell wall material, breaks ferulic acid cross-links between cell wall components
-
-
?
feruloyl-polysaccharide + H2O
ferulate + polysaccharide
-
-
-
-
?
hemicellulose + H2O
ferulic acid + arabinoxylan + pectin + ?
-
involved in the degradation of plant cell wall material, breaks ferulic acid cross-links between cell wall components
-
-
?
methyl caffeate + H2O
methanol + caffeate
no substrate of wild-type, but substrate of mutants W144Y and W142F
-
-
?
methyl ferulate + H2O
methanol + ferulate
no substrate of wild-type, but substrate of mutants W144Y and W142F
-
-
?
methyl p-coumarate + H2O
methanol + p-coumarate
no substrate of wild-type, but substrate of mutants W144Y and W142F
-
-
?
methyl sinapinate + H2O
methanol + sinapinate
no substrate of wild-type, but substrate of mutants W144Y and W142F
-
-
?
xylan polysaccharide + H2O
ferulic acid + p-coumaric acid
-
-
-
-
?
additional information
?
-
wild-type rAoFaeD fails to cleave the methyl esters of ferulic acid, p-coumaric acid, caffeic acid, and sinapic acid and ethyl ester of ferulic acid
-
-
?
4-nitrophenyl 2-O-trans-feruloyl-alpha-L-arabinofuranoside + H2O
ferulic acid + 4-nitrophenyl alpha-L-arabinofuranoside
-
O-5 linkage is hydrolyzed much faster than the O-2 linkage
-
-
?
4-nitrophenyl 2-O-trans-feruloyl-alpha-L-arabinofuranoside + H2O
ferulic acid + 4-nitrophenyl alpha-L-arabinofuranoside
-
suitable substrate for the determination of enzyme activity in a coupled assay together with alpha-L-arabinofuranosidase
-
-
?
4-nitrophenyl 5-O-trans-feruloyl-alpha-L-arabinofuranoside + H2O
ferulic acid + 4-nitrophenyl alpha-L-arabinofuranoside
-
O-5 linkage is hydrolyzed much faster than the O-2 linkage
-
-
?
4-nitrophenyl 5-O-trans-feruloyl-alpha-L-arabinofuranoside + H2O
ferulic acid + 4-nitrophenyl alpha-L-arabinofuranoside
-
suitable substrate for the determination of enzyme activity in a coupled assay together with alpha-L-arabinofuranosidase
-
-
?
feruloyl xylooligosaccharide + H2O
ferulic acid + xylooligosaccharide
-
-
-
-
?
feruloyl xylooligosaccharide + H2O
ferulic acid + xylooligosaccharide
-
esterified xylooligomers generated by xylanase action
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
feruloyl polysaccharide + H2O
ferulic acid + ?
-
involved in the degradation of plant cell wall material, breaks ferulic acid cross-links between cell wall components
-
-
?
feruloyl-polysaccharide + H2O
ferulate + polysaccharide
-
-
-
-
?
hemicellulose + H2O
ferulic acid + arabinoxylan + pectin + ?
-
involved in the degradation of plant cell wall material, breaks ferulic acid cross-links between cell wall components
-
-
?
feruloyl xylooligosaccharide + H2O
ferulic acid + xylooligosaccharide
-
-
-
-
?
feruloyl xylooligosaccharide + H2O
ferulic acid + xylooligosaccharide
-
esterified xylooligomers generated by xylanase action
-
-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
ferulic acid release by recombinant FaeB or FaeC is increased considerably by 17.6fold and 16fold, respectively in the presence of Thermomyces lanuginosus xylanase
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.28
4-nitrophenyl 2-O-trans-feruloyl-alpha-L-arabinofuranoside
-
pH 5.5, 30°C
0.23
4-nitrophenyl 5-O-trans-feruloyl-alpha-L-arabinofuranoside
-
pH 5.5, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 6
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7
-
purified recombinant FaeB and FaeC show more than 90% of their maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the isozyme A.O.5 belongs to the subfamily FEF 6B of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
evolution
additional information
evolution
the isozyme A.O.1 belongs to the subfamily FEF 4A of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
evolution
the isozyme A.O.11 belongs to the subfamily FEF 4B of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
evolution
the isozyme A.O.12 belongs to the subfamily FEF 11A of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
evolution
the isozyme A.O.13 belongs to the subfamily FEF 12B of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
evolution
the isozyme A.O.2 belongs to the subfamily FEF 4A of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
evolution
the isozyme A.O.3 belongs to the subfamily FEF 4B of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
evolution
the isozyme A.O.4 belongs to the subfamily FEF 6B of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
evolution
the isozyme A.O.6 belongs to the subfamily FEF 7A of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
evolution
the isozyme A.O.7 belongs to the subfamily FEF 7A of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
evolution
the isozyme A.O.8 belongs to the subfamily FEF 7A of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
evolution
the isozyme A.O.9 belongs to the subfamily FEF 7A of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
additional information
active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
additional information
active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
additional information
active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
additional information
active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
additional information
active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
additional information
active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
additional information
active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
additional information
active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
additional information
active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
additional information
active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
additional information
active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
additional information
active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
additional information
-
active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
additional information
active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
additional information
active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
additional information
active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
additional information
active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
additional information
active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
additional information
active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
additional information
active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
additional information
active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
additional information
active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
additional information
active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
additional information
active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
additional information
active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
additional information
-
active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
additional information
-
the enzyme structure consists of a catalytic alpha/beta-hydrolase fold domain and a large lid domain with a unique fold, binding models of substrates and docking analysis, overview. The catalytic triad of the enzyme comprises residues Ser203, Asp417, and His457, and the serine and histidine residues are directly connected by a disulfide bond of the neighboring cysteine residues, Cys202 and Cys458. The CS-D-HC structural motif plays an essential role in the function of the active site
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30000
55000
61000
67000
-
2 * 55000, recombinant deglycosylated enzyme, SDS-PAGE, 2 * 67000, recombinant glycosylated enzyme, SDS-PAGE
75000
55000
-
x * 61000, purified recombinant FaeB, SDS-PAGE. x * 75000, purified recombinant FaeC, SDS-PAGE. x * 55000, purified recombinant FaeB and FaeC after N-deglycosylation with endo-H, SDS-PAGE
55000
-
2 * 55000, recombinant deglycosylated enzyme, SDS-PAGE, 2 * 67000, recombinant glycosylated enzyme, SDS-PAGE
61000
-
x * 61000, purified recombinant FaeB, SDS-PAGE. x * 75000, purified recombinant FaeC, SDS-PAGE. x * 55000, purified recombinant FaeB and FaeC after N-deglycosylation with endo-H, SDS-PAGE
75000
-
x * 61000, purified recombinant FaeB, SDS-PAGE. x * 75000, purified recombinant FaeC, SDS-PAGE. x * 55000, purified recombinant FaeB and FaeC after N-deglycosylation with endo-H, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
2 * 55000, recombinant deglycosylated enzyme, SDS-PAGE, 2 * 67000, recombinant glycosylated enzyme, SDS-PAGE
?
-
x * 61000, purified recombinant FaeB, SDS-PAGE. x * 75000, purified recombinant FaeC, SDS-PAGE. x * 55000, purified recombinant FaeB and FaeC after N-deglycosylation with endo-H, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
the recombinant extracellular enzyme is deglycosylated by endoglycosidase H
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 7
3 - 9
7 - 10
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
-
purified recombinant FaeB and FaeC retain more than 90% of their activity after incubation at 55°C for 30 min. FaeC retains 40% of its activity after treatment at 65°C, whereas FaeB almost loses its activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Pichia pastoris strain SMD1168H by nickel affinity chromatography and ultrafiltration
FaeB and FaeC, in a two-step procedure using anion-exchange chromatography and gel filtration
-
recombinant extracellular enzyme from Pichia pastoris strain KM71H culture supernatant by ammonium sulfate fractionation, anion exchange chromatography, and deglycosylation with endoglycosidase H, followed by hydrophobic interaction chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
subcloning in Escherichia coli strain TOP10, recombinant expression of the His-tagged enzyme in Pichia pastoris strain SMD1168H
PCR product cloned into the pGEM-T Easy vector. FaeB and FaeC fragments subcloned into EcoRI-XbaI-digested pPICZalphaA expression vector. FaeB and FaeC expressed in Pichia pastoris GS115 by fusing to the Saccharomyces cerevisiae alpha-factor secretion signal peptide
-
recombinant expression in Pichia pastoris strain KM71H, the enzyme is secreted
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
isolation of phenolic acids from lignocellulosic wastes as precursors for the synthesis of chemicals
synthesis
-
potential application in the bioconversion of lignocellulosic wastes yielding ferulic acid as precursor for chemical synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Castanares, A.; McCrae, S.I.; Wood, T.M.
Purification and properties of a feruloyl/p-coumaroyl esterase from the fungus Penicillium pinophilum
Enzyme Microb. Technol.
14
875-884
1992
Aspergillus awamori, Aspergillus oryzae, Neocallimastix sp., Talaromyces pinophilus, Schizophyllum commune, Streptomyces olivochromogenes
-
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
-
Garcia, B.L.; Ball, A.S.; Rodriguez, J.; Perez-Leblic, M.I.; Arias, M.E.; Copa-Patino, J.L.
Production and characterization of ferulic acid esterase activity in crude extracts by Streptomyces avermitilis CECT 3339
Appl. Microbiol. Biotechnol.
50
213-218
1998
Aspergillus oryzae, Streptomyces sp., Neocallimastix sp., Streptomyces olivochromogenes, Streptomyces avermitilis, Streptomyces sp. C-248, Streptomyces avermitilis CECT 3339
-
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
Biely, P.; Mastihubova, M.; van Zyl, W.H.; Prior, B.A.
Differentiation of feruloyl esterases on synthetic substrates in alpha-arabinofuranosidase-coupled and ultraviolet-spectrophotometric assays
Anal. Biochem.
311
68-75
2002
Aspergillus oryzae
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)
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
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)
-
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)
Koseki, T.; Hori, A.; Seki, S.; Murayama, T.; Shiono, Y.
Characterization of two distinct feruloyl esterases, AoFaeB and AoFaeC, from Aspergillus oryzae
Appl. Microbiol. Biotechnol.
83
689-696
2009
Aspergillus oryzae, Aspergillus oryzae RIB 40
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)
Udatha, D.B.; Mapelli, V.; Panagiotou, G.; Olsson, L.
Common and distant structural characteristics of feruloyl esterase families from Aspergillus oryzae
PLoS ONE
7
e39473
2012
Aspergillus oryzae (Q2TWG0), Aspergillus oryzae (Q2TX21), Aspergillus oryzae (Q2TYH6), Aspergillus oryzae (Q2U9N5), Aspergillus oryzae (Q2UBD6), Aspergillus oryzae (Q2UF27), Aspergillus oryzae (Q2UH24), Aspergillus oryzae (Q2UII1), Aspergillus oryzae (Q2UMX6), Aspergillus oryzae (Q2UNW5), Aspergillus oryzae (Q2UP89), Aspergillus oryzae (Q75P26), Aspergillus oryzae, Aspergillus oryzae ATCC 42149 (Q2TWG0), Aspergillus oryzae ATCC 42149 (Q2TX21), Aspergillus oryzae ATCC 42149 (Q2TYH6), Aspergillus oryzae ATCC 42149 (Q2U9N5), Aspergillus oryzae ATCC 42149 (Q2UBD6), Aspergillus oryzae ATCC 42149 (Q2UF27), Aspergillus oryzae ATCC 42149 (Q2UH24), Aspergillus oryzae ATCC 42149 (Q2UII1), Aspergillus oryzae ATCC 42149 (Q2UMX6), Aspergillus oryzae ATCC 42149 (Q2UNW5), Aspergillus oryzae ATCC 42149 (Q2UP89), Aspergillus oryzae ATCC 42149 (Q75P26)
Suzuki, K.; Hori, A.; Kawamoto, K.; Thangudu, R.R.; Ishida, T.; Igarashi, K.; Samejima, M.; Yamada, C.; Arakawa, T.; Wakagi, T.; Koseki, T.; Fushinobu, S.
Crystal structure of a feruloyl esterase belonging to the tannase family: A disulfide bond near a catalytic triad
Proteins
82
2857-2867
2014
Aspergillus oryzae
Koseki, T.; Handa, H.; Watanabe, Y.; Ohtsuka, M.; Shiono, Y.
An unusual feruloyl esterase from Aspergillus oryzae two tryptophan residues play a crucial role for the activity
J. Mol. Catal. B
133
S560-S568
2016
Aspergillus oryzae (Q2U7D3), Aspergillus oryzae ATCC 42149 (Q2U7D3)
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