DB code: D00803

CATH domain 2.60.350.10 : Dex49a from penicillium minioluteum complex, domain 1
2.160.20.10 : Pectate Lyase C-like Catalytic domain
E.C. 3.2.1.11
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
2.160.20.10 : Pectate Lyase C-like S00168 S00171 S00546 S00837 S00170 S00169

Uniprot Enzyme Name
UniprotKB Protein name Synonyms CAZy Pfam
P48845 Dextranase
EC 3.2.1.11
Alpha-1,6-glucan-6-glucanohydrolase
GH49 (Glycoside Hydrolase Family 49)
PF03718 (Glyco_hydro_49)
[Graphical View]

KEGG enzyme name
dextranase
dextran hydrolase
endodextranase
dextranase DL 2
DL 2
endo-dextranase
alpha-D-1,6-glucan-6-glucanohydrolase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P48845 DEXT_PENMI Endohydrolysis of 1,6-alpha-D-glucosidic linkages in dextran. Secreted.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C00372 C02695 C00001 C00031 C00252 C02160 C02695
E.C.
Compound Dextran Isomaltosaccharide H2O D-glucose Isomaltose Isomaltotriose Isomaltosaccharide
Type polysaccharide polysaccharide H2O carbohydrate polysaccharide polysaccharide polysaccharide
ChEBI 15377
4167
28189
PubChem 22247451
962
5793
439193
439668
1ogmX01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1ogoX01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1ogmX02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1ogoX02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Bound:BGC-GLC Unbound Unbound

Reference for Active-site residues
resource references E.C.

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1ogmX01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ogoX01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ogmX02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 376;ASP 395;ASP 396
1ogoX02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 376;ASP 395;ASP 396

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[5]
Fig.4, p.561
[7]
Fig.6, Fig.8, p.1115, p.1118
[8]
p.4425-4426
[10]
p.318

References
[1]
Resource
Comments
Medline ID
PubMed ID 4731965
Journal Biochim Biophys Acta
Year 1973
Volume 309
Pages 357-62
Authors Sugiura M, Ito A, Ogiso T, Kato K, Asano H
Title Studies on dextranase. Purification of dextranase from Penicillium funiculosum and its enzymatic properties.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 4755424
Journal Int J Pept Protein Res
Year 1973
Volume 5
Pages 161-9
Authors Hiraoka N, Tsuji H, Fukumoto J, Yamamoto T, Tsuru D
Title Studies on mold dextranases. Some physicochemical properties and substrate specificity of dextranases obtained from Aspergillus carneus and Penicillium luteum.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 1139551
Journal Carbohydr Res
Year 1975
Volume 39
Pages 303-15
Authors Walker GJ, Dewar MD
Title The action pattern of Penicillium lilacinum dextranase.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 7712292
Journal Curr Opin Struct Biol
Year 1994
Volume 4
Pages 885-92
Authors McCarter JD, Withers SG
Title Mechanisms of enzymatic glycoside hydrolysis.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 16232518
Journal J Biosci Bioeng
Year 1999
Volume 87
Pages 557-65
Authors Kuriki T, Imanaka T
Title The concept of the alpha-amylase family: structural similarity and common catalytic mechanism.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 11807273
Journal Acta Crystallogr D Biol Crystallogr
Year 2002
Volume 58
Pages 346-8
Authors Larsson AM, St?hlberg J, Jones TA
Title Preparation and crystallization of selenomethionyl dextranase from Penicillium minioluteum expressed in Pichia pastoris.
Related PDB
Related UniProtKB
[7]
Resource
Comments X-RAY CRYSTALLOGRAPHY
Medline ID
PubMed ID 12962629
Journal Structure
Year 2003
Volume 11
Pages 1111-21
Authors Larsson AM, Andersson R, St?hlberg J, Kenne L, Jones TA
Title Dextranase from Penicillium minioluteum: reaction course, crystal structure, and product complex.
Related PDB 1ogm 1ogo
Related UniProtKB P48845
[8]
Resource
Comments
Medline ID
PubMed ID 15560783
Journal Eur J Biochem
Year 2004
Volume 271
Pages 4420-7
Authors Akeboshi H, Tonozuka T, Furukawa T, Ichikawa K, Aoki H, Shimonishi A, Nishikawa A, Sakano Y
Title Insights into the reaction mechanism of glycosyl hydrolase family 49. Site-directed mutagenesis and substrate preference of isopullulanase.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 16226731
Journal Carbohydr Res
Year 2005
Volume 340
Pages 2728-34
Authors Stam MR, Blanc E, Coutinho PM, Henrissat B
Title Evolutionary and mechanistic relationships between glycosidases acting on alpha- and beta-bonds.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 15944458
Journal Microbiol Mol Biol Rev
Year 2005
Volume 69
Pages 306-25
Authors Khalikova E, Susi P, Korpela T
Title Microbial dextran-hydrolyzing enzymes: fundamentals and applications.
Related PDB
Related UniProtKB

Comments
This enzyme belongs to the glycosidase family-49, with an inverting mechanism.
According to the literature [7], [8] and [10], Asp395 acts as a general acid to protonate O6 atom of the O6-C1 bond, whereas either Asp376 or Asp396 acts as a general base to activate a nearby water molecule, which will make a nucleophilic attack on the C1 atom.

Created Updated
2008-07-17 2011-12-05