EC number:3.2.1.54
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.2 Glycosylases |
| 3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds |
| ID: | 3.2.1.54 |
|---|---|
| Description: | Cyclomaltodextrinase. |
| Cath: | 3.20.20.80; 3.90.400.10; 2.60.40.10; 2.60.40.1180; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.2.1.54 |
| BRENDA Enzyme Link: | BRENDA 3.2.1.54 |
| KEGG Enzyme Link: | KEGG3.2.1.54 |
| BioCyc Enzyme Link: | BioCyc 3.2.1.54 |
| ExPASy Enzyme Link: | ExPASy3.2.1.54 |
| EC2PDB Enzyme Link: | EC2PDB 3.2.1.54 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.2.1.54 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.2.1.54 |
| IntEnz Enzyme Link: | IntEnz 3.2.1.54 |
| MEDLINE Enzyme Link: | MEDLINE 3.2.1.54 |
| RHEA:23980 | cyclomaltodextrin + H2O = linear maltodextrin |
| RULE(radius=1) | |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Purification and properties of the cyclodextrinase of Bacillus macerans. | DePinto JA, Campbell LL | 1968 Jan | 4922856 |
| [Thermotoga neopolitina gene cluster, participating in degradation of starch and maltodextrins: expression of aglB and aglA gene in Escherichia coli, properties of recombinant enzymes]. | Lunina NA, Berezina OV, Veith B, Zverlov VV, Vorob'eva IP, Chekanovskaia LA, Khromov IS, Raash G, Libel' V, Velikodvorskaia GA | 2003 Sep-Oct | 14593917 |
| A novel amylolytic enzyme from Thermotoga maritima, resembling cyclodextrinase and alpha-glucosidase, that liberates glucose from the reducing end of the substrates. | Lee MH, Kim YW, Kim TJ, Park CS, Kim JW, Moon TW, Park KH | 2002 Jul 26 | 12127967 |