First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.


From Proteopedia

Jump to: navigation, search

2dqx, resolution 2.20Å ()
Activity: Beta-amylase, with EC number
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml


mutant beta-amylase (W55R) from soy bean

Publication Abstract from PubMed

Beta-amylase (EC is starch-hydrolyzing exo-type enzyme that can catalyze the successive liberation of beta-maltose from the nonreducing ends of alpha-1,4-linked glucopyranosyl polymers. There is a well-known phenomenon called multiple or repetitive attack where the enzyme releases several maltose molecules in a single enzyme-substrate complex. In order to understand it further, we examined the beta-amylase-catalyzed reaction using maltooligosaccharides. The Monte Carlo method was applied for simulation of the beta-amylase-catalyzed reaction including the multiple attack mechanism. Through site-directed mutagenesis, we have successfully prepared a mutant enzyme which may be simulated as a multiple attack action reduced one with retaining significant hydrolytic activity. From the results of X-ray structure analysis of the mutant enzyme, it was clarified that one carboxyl residue plays a very important role in the multiple attack. The multiple attack action needs the force of enzyme sliding on the substrate. In addition, it is important for the multiple attack that the enzyme and substrate have the characteristics of a stable productive substrate-enzyme complex through a hydrogen bond between the nonreducing end of the substrate and the carboxyl residue of the enzyme.

Kinetic and structural analysis of enzyme sliding on a substrate: multiple attack in beta-amylase., Ishikawa K, Nakatani H, Katsuya Y, Fukazawa C, Biochemistry. 2007 Jan 23;46(3):792-8. PMID:17223700

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

2dqx is a 1 chain structure with sequence from Glycine max. Full crystallographic information is available from OCA.

See Also


  • Ishikawa K, Nakatani H, Katsuya Y, Fukazawa C. Kinetic and structural analysis of enzyme sliding on a substrate: multiple attack in beta-amylase. Biochemistry. 2007 Jan 23;46(3):792-8. PMID:17223700 doi:10.1021/bi061605w

Proteopedia Page Contributors and Editors (what is this?)


Personal tools