EzCatDB: D00803

DB codeD00803
CATH domainDomain 12.60.350.10
Domain 22.160.20.10Catalytic domain
E.C.3.2.1.11

CATH domainRelated DB codes (homologues)
2.160.20.10S00168,S00171,S00546,S00837,S00170,S00169

Enzyme Name
Swiss-protKEGG

P48845
Protein nameDextranasedextranase
dextran hydrolase
endodextranase
dextranase DL 2
DL 2
endo-dextranase
alpha-D-1,6-glucan-6-glucanohydrolase
SynonymsEC 3.2.1.11
Alpha-1,6-glucan-6-glucanohydrolase


Swiss-prot:Accession NumberP48845
Entry nameDEXT_PENMI
ActivityEndohydrolysis of 1,6-alpha-D-glucosidic linkages in dextran.
Subunit
Subcellular locationSecreted.
Cofactor


SubstratesProducts
KEGG-idC00372C02695C00001C00031C00252C02160C02695
CompoundDextranIsomaltosaccharideH2OD-glucoseIsomaltoseIsomaltotrioseIsomaltosaccharide
TypepolysaccharidepolysaccharideH2Ocarbohydratepolysaccharidepolysaccharidepolysaccharide
1ogmX01UnboundUnbound
UnboundUnboundUnboundUnbound
1ogoX01UnboundUnbound
UnboundUnboundUnboundUnbound
1ogmX02UnboundUnbound
UnboundUnboundUnboundUnbound
1ogoX02UnboundUnbound
UnboundBound:BGC-GLCUnboundUnbound

Active-site residues
pdbCatalytic residues
1ogmX01
1ogoX01
1ogmX02ASP 376;ASP 395;ASP 396
1ogoX02ASP 376;ASP 395;ASP 396

References for Catalytic Mechanism
ReferencesSectionsNo. 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]
PubMed ID4731965
JournalBiochim Biophys Acta
Year1973
Volume309
Pages357-62
AuthorsSugiura M, Ito A, Ogiso T, Kato K, Asano H
TitleStudies on dextranase. Purification of dextranase from Penicillium funiculosum and its enzymatic properties.
[2]
PubMed ID4755424
JournalInt J Pept Protein Res
Year1973
Volume5
Pages161-9
AuthorsHiraoka N, Tsuji H, Fukumoto J, Yamamoto T, Tsuru D
TitleStudies on mold dextranases. Some physicochemical properties and substrate specificity of dextranases obtained from Aspergillus carneus and Penicillium luteum.
[3]
PubMed ID1139551
JournalCarbohydr Res
Year1975
Volume39
Pages303-15
AuthorsWalker GJ, Dewar MD
TitleThe action pattern of Penicillium lilacinum dextranase.
[4]
PubMed ID7712292
JournalCurr Opin Struct Biol
Year1994
Volume4
Pages885-92
AuthorsMcCarter JD, Withers SG
TitleMechanisms of enzymatic glycoside hydrolysis.
[5]
PubMed ID16232518
JournalJ Biosci Bioeng
Year1999
Volume87
Pages557-65
AuthorsKuriki T, Imanaka T
TitleThe concept of the alpha-amylase family: structural similarity and common catalytic mechanism.
[6]
PubMed ID11807273
JournalActa Crystallogr D Biol Crystallogr
Year2002
Volume58
Pages346-8
AuthorsLarsson AM, St?hlberg J, Jones TA
TitlePreparation and crystallization of selenomethionyl dextranase from Penicillium minioluteum expressed in Pichia pastoris.
[7]
CommentsX-RAY CRYSTALLOGRAPHY
PubMed ID12962629
JournalStructure
Year2003
Volume11
Pages1111-21
AuthorsLarsson AM, Andersson R, St?hlberg J, Kenne L, Jones TA
TitleDextranase from Penicillium minioluteum: reaction course, crystal structure, and product complex.
Related PDB1ogm,1ogo
Related Swiss-protP48845
[8]
PubMed ID15560783
JournalEur J Biochem
Year2004
Volume271
Pages4420-7
AuthorsAkeboshi H, Tonozuka T, Furukawa T, Ichikawa K, Aoki H, Shimonishi A, Nishikawa A, Sakano Y
TitleInsights into the reaction mechanism of glycosyl hydrolase family 49. Site-directed mutagenesis and substrate preference of isopullulanase.
[9]
PubMed ID16226731
JournalCarbohydr Res
Year2005
Volume340
Pages2728-34
AuthorsStam MR, Blanc E, Coutinho PM, Henrissat B
TitleEvolutionary and mechanistic relationships between glycosidases acting on alpha- and beta-bonds.
[10]
PubMed ID15944458
JournalMicrobiol Mol Biol Rev
Year2005
Volume69
Pages306-25
AuthorsKhalikova E, Susi P, Korpela T
TitleMicrobial dextran-hydrolyzing enzymes: fundamentals and applications.

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.

createdupdated
2008-07-172011-12-05
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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