DB code: S00723

RLCP classification 1.12.30000.10 : Hydrolysis
CATH domain 3.40.50.1820 : Rossmann fold Catalytic domain
E.C. 3.1.1.73
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.50.1820 : Rossmann fold S00544 S00344 S00517 S00525 S00526 S00720 S00724 S00725 S00919 S00057 S00374 S00345 S00347 S00348 S00346 S00350 S00352 S00353 S00355 S00356 S00358 D00189 D00210 D00539 T00253

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
O42807 Feruloyl esterase A
EC 3.1.1.73
Ferulic acid esterase A
FAE-III
Cinnamoyl esterase
PF01764 (Lipase_3)
[Graphical View]

KEGG enzyme name
Feruloyl esterase
Ferulic acid esterase, hydroxycinnamoyl esterase, hemicellulase accessory enzymes
FAE-III, cinnamoyl ester hydrolase, FAEA, cinnAE, FAE-I, FAE-II

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
O42807 FAEA_ASPNG Feruloyl-polysaccharide + H(2)O = ferulate + polysaccharide. Secreted.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id L00064 C00001 C01889 C01494 C10446 I00081 I00082 I00083
E.C.
Compound Feruloylated arabinoxylan H2O Arabinoxylan Ferulate 5,5'-Diferulic acid Feruloyl-polysaccharide-tetrahedral intermediate Acyl-enzyme (Peptidyl-SER-ferulate) Feruloyl-tetrahedral intermediate
Type aromatic ring (only carbon atom),carbohydrate,polysaccharide H2O polysaccharide aromatic ring (only carbon atom),carbohydrate,carboxyl group aromatic ring (only carbon atom),carbohydrate,carboxyl group
ChEBI 15377
 15377
 		17620
 17620
PubChem 22247451
 962
 22247451
 962
 		445858
 445858
 		5281770
 5281770
1uswA00 Unbound Unbound Unbound Unbound
1uwcA00 Unbound Unbound Bound:FER_1262 Unbound
1uwcB00 Unbound Unbound Bound:FER_1262 Unbound
1uzaA00 Unbound Unbound Unbound Unbound
1uzaB00 Unbound Unbound Unbound Unbound
2bjhA00 Unbound Unbound Bound:FER Unbound
2bjhB00 Unbound Unbound Bound:FER Unbound
2bjhC00 Unbound Unbound Bound:FER Unbound
2hl6A00 Unbound Unbound Unbound Unbound
2hl6B00 Unbound Unbound Unbound Unbound
2ix9A00 Unbound Unbound Unbound Unbound
2ix9B00 Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Literature [2], [3], [6]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1uswA00 SER 133;ASP 194;HIS 247 THR 68;LEU 134
1uwcA00 SER 133;ASP 194;HIS 247 THR 68;LEU 134
1uwcB00 SER 133;ASP 194;HIS 247 THR 68;LEU 134
1uzaA00 SER 133;ASP 194;HIS 247 THR 68;LEU 134
1uzaB00 SER 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
2hl6A00 SER 133;ASP 194;HIS 247 THR 68;LEU 134
2hl6B00 SER 133;ASP 194;HIS 247 THR 68;LEU 134
2ix9A00 SER 133;ASP 194;HIS 247 THR 68;LEU 134
2ix9B00 SER 133;ASP 194;HIS 247 THR 68;LEU 134

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
Figure 5
[3]
p. 881
[6]
Fig. 9

References
[1]
Resource
Comments
Medline ID
PubMed ID 7805053
Journal Carbohydr Res
Year 1994
Volume 263
Pages 257-69
Authors Ralet MC, Faulds CB, Williamson G, Thibault JF
Title Degradation of feruloylated oligosaccharides from sugar-beet pulp and wheat bran by ferulic acid esterases from Aspergillus niger.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 12475199
Journal Chem Rev
Year 2002
Volume 102
Pages 4501-24
Authors Hedstrom L
Title Serine protease mechanism and specificity.
Related PDB
Related UniProtKB
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.08 ANGSTROMS) OF 22-281 IN COMPLEX WITH FERULIC ACID.
Medline ID
PubMed ID 15103133
Journal Acta Crystallogr D Biol Crystallogr
Year 2004
Volume 60
Pages 878-87
Authors McAuley KE, Svendsen A, Patkar SA, Wilson KS
Title Structure of a feruloyl esterase from Aspergillus niger.
Related PDB 1uwc 1uza
Related UniProtKB O42807
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-281, DISULFID BONDS, FUNCTION, MUTAGENESIS OF SER-154.
Medline ID
PubMed ID 15081808
Journal J Mol Biol
Year 2004
Volume 338
Pages 495-506
Authors Hermoso JA, Sanz-Aparicio J, Molina R, Juge N, Gonzalez R, Faulds CB
Title The crystal structure of feruloyl esterase A from Aspergillus niger suggests evolutive functional convergence in feruloyl esterase family.
Related PDB 1usw
Related UniProtKB O42807
[5]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 22-281 OF MUTANT SER-154 IN COMPLEX WITH SUBSTRATE, MUTAGENESIS OF TYR-101 AND TRP-281.
Medline ID
PubMed ID 16128806
Journal FEBS J
Year 2005
Volume 272
Pages 4362-71
Authors Faulds CB, Molina R, Gonzalez R, Husband F, Juge N, Sanz-Aparicio J, Hermoso JA
Title Probing the determinants of substrate specificity of a feruloyl esterase, AnFaeA, from Aspergillus niger.
Related PDB 2bjh
Related UniProtKB O42807
[6]
Resource
Comments
Medline ID
PubMed ID 16702605
Journal Appl Biochem Biotechnol
Year 2006
Volume 133
Pages 87-112
Authors Wong DW
Title Feruloyl esterase: a key enzyme in biomass degradation.
Related PDB
Related UniProtKB
[7]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 22-281, GLYCOSYLATION, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
Medline ID
PubMed ID 17027758
Journal FEBS Lett
Year 2006
Volume 580
Pages 5815-21
Authors Benoit I, Asther M, Sulzenbacher G, Record E, Marmuse L, Parsiegla G, Gimbert I, Asther M, Bignon C
Title Respective importance of protein folding and glycosylation in the thermal stability of recombinant feruloyl esterase A.
Related PDB 2hl6 2ix9
Related UniProtKB O42807

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]).

Created Updated
2011-01-21 2011-12-06