EzCatDB: S00346
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DB codeS00346
RLCP classification1.12.30000.26 : Hydrolysis
CATH domainDomain 13.40.50.1820 : Rossmann foldCatalytic domain
E.C.3.1.1.72
CSA1bs9

CATH domainRelated DB codes (homologues)
3.40.50.1820 : Rossmann foldS00544,S00344,S00517,S00525,S00526,S00720,S00723,S00724,S00725,S00919,S00057,S00374,S00345,S00347,S00348,S00350,S00352,S00353,S00355,S00356,S00358,D00189,D00210,D00539,T00253

Enzyme Name
UniProtKBKEGG

O59893Q99034
Protein nameAcetylxylan esterase 2Acetylxylan esteraseacetylxylan esterase
SynonymsEC 3.1.1.72
AXE II
EC 3.1.1.72
PfamPF01083 (Cutinase)
[Graphical view]
PF00734 (CBM_1)
PF01083 (Cutinase)
[Graphical view]


UniProtKB:Accession NumberO59893Q99034
Entry nameAXE2_PENPUAXE1_TRIRE
ActivityDeacetylation of xylans and xylo- oligosaccharides.Deacetylation of xylans and xylo- oligosaccharides.
SubunitMonomer.Monomer.
Subcellular locationSecreted.Secreted.
Cofactor


Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idL00032C00001C00707C00033
CompoundAcetyl xylanH2OXylanAcetate
Typecarbohydrate,polysaccharideH2Opolysaccharidecarboxyl group
ChEBI
15377

15366
PubChem
962
22247451

21980959
176
            
1bs9AUnbound UnboundUnbound
1g66AUnbound UnboundUnbound
2axeAUnbound UnboundUnbound
1qozAUnbound UnboundUnbound
1qozBUnbound UnboundUnbound

Active-site residues
resource
Swiss-prot & literature [2],[3]
pdbCatalytic residuesMain-chain involved in catalysis
          
1bs9ATHR 13;SER 90;ASP 175;HIS 187
THR 13
1g66ATHR 13;SER 90;ASP 175;HIS 187
THR 13
2axeATHR 13;SER 90;ASP 175;HIS 187
THR 13
1qozATHR 13;SER 90;ASP 175;HIS 187
THR 13
1qozBTHR 13;SER 90;ASP 175;HIS 187
THR 13

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]Fig.5, p.186-1893

references
[1]
CommentsX-ray crystallography (1.1 Angstroms)
PubMed ID10089308
JournalActa Crystallogr D
Year1999
Volume55
Pages779-84
AuthorsGhosh D, Erman M, Sawicki M, Lala P, Weeks DR, Li N, Pangborn W, Thiel DJ, Jornvall H, Gutierrez R, Eyzaguirre J
TitleDetermination of a protein structure by iodination: the structure of iodinated acetylxylan esterase.
Related PDB1bs9
[2]
CommentsX-ray crystallography (1.9 Angstroms), catalysis
PubMed ID11243887
JournalJ Struct Biol
Year2000
Volume132
Pages180-90
AuthorsHakulinen N, Tenkanen M, Rouvinen J
TitleThree-dimensional structure of the catalytic core of acetylxylan esterase from Trichoderma reesei: insights into the deacetylation mechanism.
[3]
CommentsX-ray crystallography (0.9 Angstroms)
PubMed ID11134051
JournalJ Biol Chem
Year2001
Volume276
Pages11159-66
AuthorsGhosh D, Sawicki M, Lala P, Erman M, Pangborn W, Eyzaguirre J, Gutierrez R, Jornvall H, Thiel DJ
TitleMultiple conformations of catalytic serine and histidine in acetylxylan esterase at 0.90 A.
Related PDB1g66,1qoz

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].

createdupdated
2002-07-042010-11-30


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