Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

3.2.1.11: dextranase

This is an abbreviated version!
For detailed information about dextranase, go to the full flat file.

Word Map on EC 3.2.1.11

Reaction

Dextran
+
H2O
=
dextran fragment 1
 +
dextran fragment 2

Synonyms

1,6-alpha-D-glucan-6-glucanohydrolase, 6-alpha-D-glucan 6-glucanohydrolase, alpha-1,6-D-glucan 6-glucanohydrolase, alpha-1,6-D-glucan-6-glucanohydrolase, Alpha-1,6-glucan-6-glucanohydrolase, alpha-D-1,6-glucan-6-glucanohydrolase, alpha-dextranase, alpha-glucanase, AODex, Dex, Dex2, Dex410, Dex49A, DexA, dextran hydrolase, dextranase, dextranase DL 2, dextranase I, dextranase II, Dextranase Plus L, dextransucrase, DL 2, DXSR, endo-dextranase, endodextranase, extracellular dextranase, Fjoh_4430, LSD1, More, rDex, SmDex, Teth39_0264, TLDex, TPDex

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.11 dextranase

Crystallization

Crystallization on EC 3.2.1.11 - dextranase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CD-I
Achaetomiella gracilis
-
molecular modeling of structure, based on PDB entry 1ogm.1
hanging drop vapor diffusion method, using 0.2 M MgCl2, 0.1 M HEPES (pH 7.5), and 30% (w/v) polyethylene glycol 400
crystal structure of the conserved fragment from residue Gln100 to Ile732, devoid of its N- and C-terminal variable regions, 1.6 A resolution. Structural domain N possesses an immunoglobulin-like beta-sandwich fold, domain A contains the enzyme's catalytic module, comprising a (beta/alpha)8-barrel, and domain C forms a beta-sandwich structure containing two Greek key motifs. In the enzyme-isomaltotriose complex structure, the bound isomaltooligosaccharide with four glucose moieties is observed in the catalytic glycone cleft and considered to be the transglycosylation product of the enzyme, indicating the presence of four subsites in the catalytic cleft. The complexed structure with suicide substrate 4',5'-epoxypentyl-alpha-D-glucopyranoside reveals that the epoxide ring reacts to form a covalent bond with the Asp385 side chain. Asp385 is the catalytic nucleophile and Glu453 is the acid/base of the double displacement mechanism
crystal structure of apo-Dex49A and Dex49A complexed with product at 1.8 A and 1.65 A, respectively
crystallization of selenomethionyl-rDEX
-
crystal structures of the wild type and catalytic mutant D312G in complex with isomaltohexaose. The enzyme consists of a catalytic domain comprising an (beta/alpha)8-barrel and two beta-domains located at both N- and C-terminal ends. The isomaltohexaose molecule is bound across the catalytic site, showing the existence of six subsites (-4 to +2) in the catalytic cleft. Marked movement of the W376 side-chain along with loop 6, which is the side wall component of the cleft at subsite +1, is observed to occupy subsite +1