CATH Classification

Domain Context

CATH Clusters

Superfamily Glycosidases
Functional Family Beta-amylase

Enzyme Information

3.2.1.2
Beta-amylase.
based on mapping to UniProt P16098
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.
-!- Acts on starch, glycogen and related polysaccharides and oligosaccharides producing beta-maltose by an inversion.

UniProtKB Entries (1)

P16098
AMYB_HORVU
Hordeum vulgare
Beta-amylase

PDB Structure

PDB 2XGI
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Chemical genetics and cereal starch metabolism: structural basis of the non-covalent and covalent inhibition of barley beta-amylase.
Rejzek, M., Stevenson, C.E., Southard, A.M., Stanley, D., Denyer, K., Smith, A.M., Naldrett, M.J., Lawson, D.M., Field, R.A.
Mol Biosyst