| EC |
3.2.1.98 |
| Accepted name: |
glucan 1,4-α-maltohexaosidase |
| Reaction: |
Hydrolysis of (1→4)-α-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltohexaose residues from the non-reducing chain ends |
| Other name(s): |
exo-maltohexaohydrolase; 1,4-α-D-glucan maltohexaohydrolase |
| Systematic name: |
4-α-D-glucan maltohexaohydrolase |
| Comments: |
cf. EC 3.2.1.3 glucan 1,4-α-glucosidase, which removes successive glucose residues; EC 3.2.1.2 β-amylase, which removes successive maltose residues; EC 3.2.1.116 glucan 1,4-α-maltotriohydrolase, which removes successive maltotriose units and EC 3.2.1.60 glucan 1,4-α-maltotetraohydrolase, which removes successive maltotetraose residues. The products have the α-configuration. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 72561-12-7 |
| References: |
| 1. |
Kainuma, K., Wako, K., Kobayashi, A., Nogami, A. and Suzuki, S. Purification and some properties of a novel maltohexaose-producing exo-amylase from Aerobacter aerogenes. Biochim. Biophys. Acta 410 (1975) 333–346. [DOI] [PMID: 1094] |
| 2. |
Nakakuki, T., Azuma, K. and Kainuma, K. Action patterns of various exo-amylases and the anomeric configurations of their products. Carbohydr. Res. 128 (1984) 297–310. |
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| [EC 3.2.1.98 created 1978] |
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