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. 2003 Sep;11(9):1111-21.
doi: 10.1016/s0969-2126(03)00147-3.

Dextranase from Penicillium minioluteum: reaction course, crystal structure, and product complex

Anna M Larsson  1 , Rolf Andersson, Jerry Ståhlberg, Lennart Kenne, T Alwyn Jones
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Free article

Dextranase from Penicillium minioluteum: reaction course, crystal structure, and product complex

Anna M Larsson et al. Structure. 2003 Sep.
Free article

Abstract

Dextranase catalyzes the hydrolysis of the alpha-1,6-glycosidic linkage in dextran polymers. The structure of dextranase, Dex49A, from Penicillium minioluteum was solved in the apo-enzyme and product-bound forms. The main domain of the enzyme is a right-handed parallel beta helix, which is connected to a beta sandwich domain at the N terminus. In the structure of the product complex, isomaltose was found to bind in a crevice on the surface of the enzyme. The glycosidic oxygen of the glucose unit in subsite +1 forms a hydrogen bond to the suggested catalytic acid, Asp395. By NMR spectroscopy the reaction course was shown to occur with net inversion at the anomeric carbon, implying a single displacement mechanism. Both Asp376 and Asp396 are suitably positioned to activate the water molecule that performs the nucleophilic attack. A new clan that links glycoside hydrolase families 28 and 49 is suggested.

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