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
 15377
 		4167
 4167
 		28189
 28189
PubChem 22247451
 962
 22247451
 962
 		5793
 5793
 		439193
 439193
 		439668
 439668
1ogmX01 Unbound Unbound Unbound Unbound Unbound Unbound
1ogoX01 Unbound Unbound Unbound Unbound Unbound Unbound
1ogmX02 Unbound Unbound Unbound Unbound Unbound Unbound
1ogoX02 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
1ogoX01
1ogmX02 ASP 376;ASP 395;ASP 396
1ogoX02 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