| IED ID | IndEnz0001000112 |
| Enzyme Type ID | amylase000112 |
| Protein Name |
Cyclomaltodextrinase EC 3.2.1.54 Maltodextrin glucosidase |
| Gene Name | aglB malA |
| Organism | Thermotoga neapolitana |
| Taxonomic Lineage | cellular organisms Bacteria Thermotogae Thermotogae Thermotogales Thermotogaceae Thermotoga Thermotoga neapolitana |
| Enzyme Sequence | MYPIPSWVYDSVVYQIFPDRFFIGKGKTVEDKKDLYLKRGGTIEKWGVPPRKLPGAQHVKVFYGGDLWGIAEKIDYLEELGVNAVYLTPIFLSDTNHKYDTIDYFKIDPQFGGKRAFVHLLKVLHSRNIKLILDGVFNHVGSQHPWFKKARKKDPEYVNRFFLYRDRHRSWFDVGSLPELNVEVEEVREYILKVVQHYLEVGVDGWRLDCGHDLGPLVNLWINMKVKEFSSEKYLVSEIWTYPAGWEMVDGLMNYNFRSLVLSYVNGETDSIGTELERAYRETKNIFGCWNMLDSHDTPRLATTVPVKDLRKLAIVLQFTYPGVPLVYYGTEIGLTGGEDPECRATMEWNREKWDMELFEFYKKMIRFRRTDPGLRFGEFILLKEKPLAFMRKAPHPLQDTIVVVNPEEEKNVVLSLPDGKIMNATPLFDIFTGEKFHVDGGVVKVPVGRRSFRILKPIDLRVGRYRLYKRV |
| Enzyme Length | 472 |
| Uniprot Accession Number | O86959 |
| Absorption | |
| Active Site | ACT_SITE 209; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 238; /note=Proton donor; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Addition of 1 mM MnCl(2), NiCl(2), CoCl(2), ZnCl(2), CuCl(2), or 0.1 mM HgCl(2) inhibits the enzyme activity to 0-6%. Activity is increased in vitro upon addition of CaCl(2), DTT (relative activity 147%), KCl (180%), or EDTA (180%), as well as after heating of the enzyme. Is not inhibited by acarbose, a potent alpha-amylase and alpha-glucosidase inhibitor; on the contrary, acarbose is degraded quantitatively by AglB, yielding glucose. {ECO:0000269|PubMed:14593917}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=cyclomaltodextrin + H2O = linear maltodextrin; Xref=Rhea:RHEA:23980, Rhea:RHEA-COMP:14584, Rhea:RHEA-COMP:14707, ChEBI:CHEBI:15377, ChEBI:CHEBI:17623, ChEBI:CHEBI:18398; EC=3.2.1.54; Evidence={ECO:0000269|PubMed:14593917}; |
| DNA Binding | |
| EC Number | 3.2.1.54 |
| Enzyme Function | FUNCTION: Is able to efficiently hydrolyze alpha-, beta-, and gamma-cyclomaltodextrins and linear maltooligosaccharides, to glucose and maltose, by decycling cyclodextrins and liberating glucose from the reducing end of the molecules. Shows a very weak activity on starch and pullulan. Cannot hydrolyze maltose or disaccharides with various types of alpha-links. Is not active against beta-glycosidic bonds of poly-, oligo-, and disaccharides. {ECO:0000269|PubMed:14593917}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 85 degrees Celsius with pNP-alpha-D-maltoside as substrate. Remains stable after preincubation for various periods up to 48 hours at temperatures between 50 and 90 degrees Celsius, pH 6.5. The half-life of the enzyme at 95 degrees Celsius is 2 hours. {ECO:0000269|PubMed:14593917}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 with pNP-alpha-D-maltoside as substrate. {ECO:0000269|PubMed:14593917}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Site (1) |
| Keywords | Carbohydrate metabolism;Glycosidase;Hydrolase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 55,112 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.9 mM for beta-cyclodextrin (at 80 degrees Celsius) {ECO:0000269|PubMed:14593917}; Vmax=66 umol/min/mg enzyme with beta-cyclodextrin as substrate (at 80 degrees Celsius) {ECO:0000269|PubMed:14593917}; |
| Metal Binding | |
| Rhea ID | RHEA:23980 |
| Cross Reference Brenda |