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3.1.1.73: feruloyl esterase

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

Word Map on EC 3.1.1.73

Reaction

feruloyl-polysaccharide
+
H2O
=
ferulate
 +
Polysaccharide

Synonyms

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

ECTree

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

Expression

Expression on EC 3.1.1.73 - feruloyl esterase

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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of EstA is controlled by the XlnR transcriptional activator
expression of genes faeT and faeD is not significantly affected by the addition of acetosyringone, benzoic acid, cinnamic acid, p-coumaric acid, vanillic acid, arabinogalactan, arabinose, galactose, galacturonate, mannose, pectin, polygalacturonate, rhamnose, salicine, xylose, or xylan
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
-
feruoyl esterases FaeD and FaeT are induced by ferulic acid. The product of the adjacent gene faeR is involved in the positive control of faeD in response to ferulic acid. Moreover, ferulic acid acts in synergy with polygalacturonate to induce pectate lyases, the main virulence determinant of soft rot disease
induction of the FAE synthesis is not related to the ferulic acid content in the substrate used
-
maximal level of activity in the presence of destarched wheat bran as the sole carbon source. 1% (m/v) of destarched wheat bran is the optimal concentration to induce its production. With this inducer, no ferulic acid dimers are released from the cell wall by the produced FAE. Destarched maize bran is capable of inducing the synthesis of a small amount of FAE. Maximal level of activity in the presence of oat spelt xylan as the sole carbon source. Rape cattle cake (Brassica napus), which does not contain esterified ferulic acid, is capable of inducing the synthesis of a small amount of FAE. With beet pectins or with white dextrins, FAE activity is detected when a drop of culture supernatant is deposited on the agar medium containing ethyl ferulate, but this activity is too weak to be quantified
-
no FAE activity in the presence of 0.1% ethyl ferulate in the culture medium. Low FAE activity in the absence of lignocellulosic substrate, maybe due to a constitutive synthesis of the FAE
-
sodium nitrate is the best nitrogen source. Inorganic nitrogen source yields better feruloyl esterases activity than an organic nitrogen source, such as urea. Moderate to good levels of feruloyl estrerases with ammonium chloride, ammonium citrate, ammonium tartrate and potassium nitrate as nitrogen sources. Optimal conditions for high level of feruloyl esterase production are: culturing temperature 30°C, shaker speed 250 rpm, initial pH 6, with wheat straw, corncobs or wheat germ as carbon source and sodium nitrate or urea as nitrogen source
the enzyme is induced by 3 mM methyl ferulate