EzCatDB: S00723
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DB codeS00723
RLCP classification1.12.30000.10 : Hydrolysis
CATH domainDomain 13.40.50.1820 : Rossmann foldCatalytic domain
E.C.3.1.1.73

CATH domainRelated DB codes (homologues)
3.40.50.1820 : Rossmann foldS00544,S00344,S00517,S00525,S00526,S00720,S00724,S00725,S00919,S00057,S00374,S00345,S00347,S00348,S00346,S00350,S00352,S00353,S00355,S00356,S00358,D00189,D00210,D00539,T00253

Enzyme Name
UniProtKBKEGG

O42807
Protein nameFeruloyl esterase AFeruloyl esterase
Ferulic acid esterase, hydroxycinnamoyl esterase, hemicellulase accessory enzymes
FAE-III, cinnamoyl ester hydrolase, FAEA, cinnAE, FAE-I, FAE-II
SynonymsEC 3.1.1.73
Ferulic acid esterase A
FAE-III
Cinnamoyl esterase
PfamPF01764 (Lipase_3)
[Graphical view]


UniProtKB:Accession NumberO42807
Entry nameFAEA_ASPNG
ActivityFeruloyl-polysaccharide + H(2)O = ferulate + polysaccharide.
Subunit
Subcellular locationSecreted.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idL00064C00001C01889C01494C10446I00081I00082I00083
CompoundFeruloylated arabinoxylanH2OArabinoxylanFerulate5,5'-Diferulic acidFeruloyl-polysaccharide-tetrahedral intermediateAcyl-enzyme (Peptidyl-SER-ferulate)Feruloyl-tetrahedral intermediate
Typearomatic ring (only carbon atom),carbohydrate,polysaccharideH2Opolysaccharidearomatic ring (only carbon atom),carbohydrate,carboxyl grouparomatic ring (only carbon atom),carbohydrate,carboxyl group


ChEBI
15377

17620




PubChem
962
22247451

445858
5281770



                
1uswA00Unbound UnboundUnboundUnbound   
1uwcA00Unbound UnboundBound:FER 1262Unbound   
1uwcB00Unbound UnboundBound:FER 1262Unbound   
1uzaA00Unbound UnboundUnboundUnbound   
1uzaB00Unbound UnboundUnboundUnbound   
2bjhA00Unbound UnboundBound:FERUnbound   
2bjhB00Unbound UnboundBound:FERUnbound   
2bjhC00Unbound UnboundBound:FERUnbound   
2hl6A00Unbound UnboundUnboundUnbound   
2hl6B00Unbound UnboundUnboundUnbound   
2ix9A00Unbound UnboundUnboundUnbound   
2ix9B00Unbound UnboundUnboundUnbound   

Active-site residues
resource
Literature [2], [3], [6]
pdbCatalytic residuesMain-chain involved in catalysiscomment
           
1uswA00SER 133;ASP 194;HIS 247
THR 68;LEU 134
 
1uwcA00SER 133;ASP 194;HIS 247
THR 68;LEU 134
 
1uwcB00SER 133;ASP 194;HIS 247
THR 68;LEU 134
 
1uzaA00SER 133;ASP 194;HIS 247
THR 68;LEU 134
 
1uzaB00SER 133;ASP 194;HIS 247
THR 68;LEU 134
 
2bjhA00       ;ASP 194;HIS 247
THR 68;LEU 134
mutant S133A
2bjhB00       ;ASP 194;HIS 247
THR 68;LEU 134
mutant S133A
2bjhC00       ;ASP 194;HIS 247
THR 68;LEU 134
mutant S133A
2hl6A00SER 133;ASP 194;HIS 247
THR 68;LEU 134
 
2hl6B00SER 133;ASP 194;HIS 247
THR 68;LEU 134
 
2ix9A00SER 133;ASP 194;HIS 247
THR 68;LEU 134
 
2ix9B00SER 133;ASP 194;HIS 247
THR 68;LEU 134
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]Figure 5
[3]p. 881
[6]Fig. 9

references
[1]
PubMed ID7805053
JournalCarbohydr Res
Year1994
Volume263
Pages257-69
AuthorsRalet MC, Faulds CB, Williamson G, Thibault JF
TitleDegradation of feruloylated oligosaccharides from sugar-beet pulp and wheat bran by ferulic acid esterases from Aspergillus niger.
[2]
PubMed ID12475199
JournalChem Rev
Year2002
Volume102
Pages4501-24
AuthorsHedstrom L
TitleSerine protease mechanism and specificity.
[3]
CommentsX-RAY CRYSTALLOGRAPHY (1.08 ANGSTROMS) OF 22-281 IN COMPLEX WITH FERULIC ACID.
PubMed ID15103133
JournalActa Crystallogr D Biol Crystallogr
Year2004
Volume60
Pages878-87
AuthorsMcAuley KE, Svendsen A, Patkar SA, Wilson KS
TitleStructure of a feruloyl esterase from Aspergillus niger.
Related PDB1uwc,1uza
Related UniProtKBO42807
[4]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-281, DISULFID BONDS, FUNCTION, MUTAGENESIS OF SER-154.
PubMed ID15081808
JournalJ Mol Biol
Year2004
Volume338
Pages495-506
AuthorsHermoso JA, Sanz-Aparicio J, Molina R, Juge N, Gonzalez R, Faulds CB
TitleThe crystal structure of feruloyl esterase A from Aspergillus niger suggests evolutive functional convergence in feruloyl esterase family.
Related PDB1usw
Related UniProtKBO42807
[5]
CommentsX-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 22-281 OF MUTANT SER-154 IN COMPLEX WITH SUBSTRATE, MUTAGENESIS OF TYR-101 AND TRP-281.
PubMed ID16128806
JournalFEBS J
Year2005
Volume272
Pages4362-71
AuthorsFaulds CB, Molina R, Gonzalez R, Husband F, Juge N, Sanz-Aparicio J, Hermoso JA
TitleProbing the determinants of substrate specificity of a feruloyl esterase, AnFaeA, from Aspergillus niger.
Related PDB2bjh
Related UniProtKBO42807
[6]
PubMed ID16702605
JournalAppl Biochem Biotechnol
Year2006
Volume133
Pages87-112
AuthorsWong DW
TitleFeruloyl esterase: a key enzyme in biomass degradation.
[7]
CommentsX-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 22-281, GLYCOSYLATION, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
PubMed ID17027758
JournalFEBS Lett
Year2006
Volume580
Pages5815-21
AuthorsBenoit I, Asther M, Sulzenbacher G, Record E, Marmuse L, Parsiegla G, Gimbert I, Asther M, Bignon C
TitleRespective importance of protein folding and glycosylation in the thermal stability of recombinant feruloyl esterase A.
Related PDB2hl6,2ix9
Related UniProtKBO42807

comments
This enzyme is homologous to carboxylesterase 2 (EC 3.1.1.1; S00345 in EzCatDB), bile salt-activated lipase (EC 3.1.1.3, 3.1.1.13; S00347 in EzCatDB) and carboxypeptidase Y (EC 3.4.16.5; D00189 in EzCatDB), which belong to alpha/beta-hydrolase superfamily.
According to the literature [4] and [5], feruloyl esterases (EC 3.1.1.73) are subdivided into four sub-classes, type A to D, based on the sequence and substrate specificity. This enzyme belongs to the type-A sublclass (see [4]).
This enzyme has got a catalytic triad, composed of Ser133, Asp194 and His247, as well as an oxyanion hole, composed of mainchain amide groups of Thr68 and Leu134, which may facilitate the same catalytic reaction as other homologous enzymes in the alpha/beta-hydrolase superfamily (see [3], [4], [5] and [6]).

createdupdated
2011-01-212011-12-06


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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