3.1.1.73: feruloyl esterase

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For detailed information about feruloyl esterase, go to the full flat file.

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 Hydrolases

         3.1 Acting on ester bonds

             3.1.1 Carboxylic-ester hydrolases

                3.1.1.73 feruloyl esterase

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Results	in table
13	Activating Compound
2085	AA Sequence
110	Application
3	CAS Registry Number
91	Cloned(Commentary)
21	Crystallization (Commentary)
13	Expression
62	General Information
2	General Stability
179	Inhibitors
138	kcat/KM [mM/s]
5	Ki Value [mM]
406	KM Value [mM]
88	Localization
43	Metals/Ions
199	Molecular Weight [Da]
266	Natural Substrates/ Products (Substrates)
14	Organic Solvent Stability
553	Organism
1	Pathway
23	PDB ID
178	pH Optimum
53	pH Range
61	pH Stability
57	pI Value
19	Posttranslational Modification
118	Protein Variants
86	Purification (Commentary)
1	Reaction
1	Reaction Type
460	Reference
2	Renatured (Commentary)
25	Source Tissue
230	Specific Activity [micromol/min/mg]
13	Storage Stability
1454	Substrates and Products (Substrate)
126	Subunits
527	Synonyms
1	Systematic Name
161	Temperature Optimum [°C]
48	Temperature Range [°C]
154	Temperature Stability [°C]
320	Turnover Number [1/s]

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RENATURED/Commentary

ORGANISM

UNIPROT

LITERATURE

after treatment above the thermal denaturation temperature followed by cooling to room temperature, FaeI demonstrates spontaneous refolding into an active state

Actinomyces sp. oral taxon 448

F9ECN6

737514

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

Aspergillus niger

O42807

737333