DB code: S00346

RLCP classification 1.12.30000.26 : Hydrolysis
CATH domain 3.40.50.1820 : Rossmann fold Catalytic domain
E.C. 3.1.1.72
CSA 1bs9
M-CSA 1bs9
MACiE

CATH domain Related DB codes (homologues)
3.40.50.1820 : Rossmann fold S00544 S00344 S00517 S00525 S00526 S00720 S00723 S00724 S00725 S00919 S00057 S00374 S00345 S00347 S00348 S00350 S00352 S00353 S00355 S00356 S00358 D00189 D00210 D00539 T00253

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam CAZy
O59893 Acetylxylan esterase 2
EC 3.1.1.72
AXE II
PF01083 (Cutinase)
[Graphical View]
Q99034 Acetylxylan esterase
EC 3.1.1.72
PF00734 (CBM_1)
PF01083 (Cutinase)
[Graphical View] 		CBM1 (Carbohydrate-Binding Module Family 1)

KEGG enzyme name
acetylxylan esterase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
O59893 AXE2_PENPU Deacetylation of xylans and xylo- oligosaccharides. Monomer. Secreted.
Q99034 AXE1_TRIRE Deacetylation of xylans and xylo- oligosaccharides. Monomer. Secreted.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id L00032 C00001 C00707 C00033
E.C.
Compound Acetyl xylan H2O Xylan Acetate
Type carbohydrate,polysaccharide H2O polysaccharide carboxyl group
ChEBI 15377
 15377
 		15366
 15366
PubChem 22247451
 962
 22247451
 962
 		176
 21980959
 176
 21980959
1bs9A Unbound Unbound Unbound
1g66A Unbound Unbound Unbound
2axeA Unbound Unbound Unbound
1qozA Unbound Unbound Unbound
1qozB Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot & literature [2],[3]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1bs9A THR 13;SER 90;ASP 175;HIS 187 THR 13
1g66A THR 13;SER 90;ASP 175;HIS 187 THR 13
2axeA THR 13;SER 90;ASP 175;HIS 187 THR 13
1qozA THR 13;SER 90;ASP 175;HIS 187 THR 13
1qozB THR 13;SER 90;ASP 175;HIS 187 THR 13

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
Fig.5, p.186-189 3

References
[1]
Resource
Comments X-ray crystallography (1.1 Angstroms)
Medline ID
PubMed ID 10089308
Journal Acta Crystallogr D
Year 1999
Volume 55
Pages 779-84
Authors Ghosh D, Erman M, Sawicki M, Lala P, Weeks DR, Li N, Pangborn W, Thiel DJ, Jornvall H, Gutierrez R, Eyzaguirre J
Title Determination of a protein structure by iodination: the structure of iodinated acetylxylan esterase.
Related PDB 1bs9
Related UniProtKB
[2]
Resource
Comments X-ray crystallography (1.9 Angstroms), catalysis
Medline ID
PubMed ID 11243887
Journal J Struct Biol
Year 2000
Volume 132
Pages 180-90
Authors Hakulinen N, Tenkanen M, Rouvinen J
Title Three-dimensional structure of the catalytic core of acetylxylan esterase from Trichoderma reesei: insights into the deacetylation mechanism.
Related PDB
Related UniProtKB
[3]
Resource
Comments X-ray crystallography (0.9 Angstroms)
Medline ID
PubMed ID 11134051
Journal J Biol Chem
Year 2001
Volume 276
Pages 11159-66
Authors Ghosh D, Sawicki M, Lala P, Erman M, Pangborn W, Eyzaguirre J, Gutierrez R, Jornvall H, Thiel DJ
Title Multiple conformations of catalytic serine and histidine in acetylxylan esterase at 0.90 A.
Related PDB 1g66 1qoz
Related UniProtKB

Comments
The literature [2] suggests that the acetyl groups of acetylxylan are removed from xylan by the mechanism involved in the catalytic triad (Asp175-His187-Ser90).
Moreover, the oxyanion hole is composed of the mainchain amide and sidechain of Thr13, according to the literature [2].

Created Updated
2002-07-04 2010-11-30