| IED ID | IndEnz0001000411 |
| Enzyme Type ID | amylase000411 |
| Protein Name |
Cyclomaltodextrinase EC 3.2.1.54 Maltodextrin glucosidase TMG |
| Gene Name | aglB TM_1835 |
| Organism | Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) |
| Taxonomic Lineage | cellular organisms Bacteria Thermotogae Thermotogae Thermotogales Thermotogaceae Thermotoga Thermotoga maritima Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) |
| Enzyme Sequence | MMYPMPSWVYDSVVYQIFPDRFFIGKGKTVEDKKDLYLKRGGVIEKWGVPPRKLPGAQHVKIFYGGDLWGIAEKVDYFEELGINVLYLTPIFLSDTNHKYDTIDYFRVDPQFGGKRAFLHLLRVLHERSMKLILDGVFNHVGSQHPWFKKAKKNDPEYVNRFFLYKDRHRSWFDVGSLPELNVEVEEVKEYILKVVEHYLKLGIDGWRLDCGHDLGPTVNLWINMKVKEFSAEKYLVSEIWTYPAGWDMVDGLMNYNFRNLVLSYVNGETDSIGFHLERAYRETKNIFGCWNMLDSHDTPRLATMVPDRDLRKLAVVLQFTYPGVPLVYYGTEIGLTGGEDPECRATMEWNREKWDVDLFEFYKKMIRLRRTDPGLRFGEFVLLNDSPLAFLRKAPHPLQNTIVVVNPGEEKVLVLSIPDGKIMNTTPLVDVFSGERFHVDGGVVKLPLLARSFRILKPEDLRVGKYRLYKRV |
| Enzyme Length | 473 |
| Uniprot Accession Number | Q9X2F4 |
| Absorption | |
| Active Site | ACT_SITE 210; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 239; /note=Proton donor; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Mn(2+), Co(2+), Zn(2+), Fe(2+), Mg(2+), and Ca(2+) inhibit the hydrolysis activity of the enzyme whereas EGTA and EDTA do not affect the activity. {ECO:0000269|PubMed:12127967}. |
| 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:12127967}; |
| DNA Binding | |
| EC Number | 3.2.1.54 |
| Enzyme Function | FUNCTION: Is able to hydrolyze various linear maltooligosaccharides (maltotriose to maltoheptaose) and cyclomaltodextrins (CDs), to mainly glucose and maltose, by liberating glucose from the reducing end of the molecules. Shows a very weak activity on starch. Can neither hydrolyze maltose nor degrade pullulan, but rapidly hydrolyzes acarbose, a strong amylase and glucosidase inhibitor, to acarviosine and glucose. {ECO:0000269|PubMed:12127967}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 85 degrees Celsius with beta-cyclodextrin as substrate. Retains 80% of its activity at 90 degrees Celsius. The half-lives of the enzyme examined at 80, 85, and 90 degrees Celsius are 147, 108, and 23 minutes, respectively. {ECO:0000269|PubMed:12127967}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 with beta-cyclodextrin as substrate. {ECO:0000269|PubMed:12127967}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Site (1) |
| Keywords | Carbohydrate metabolism;Glycosidase;Hydrolase;Reference proteome |
| 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 | 55,181 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20.64 mM for maltotriose (at pH 6.5 and 85 degrees Celsius) {ECO:0000269|PubMed:12127967}; KM=11.84 mM for maltotetraose (at pH 6.5 and 85 degrees Celsius) {ECO:0000269|PubMed:12127967}; KM=9.95 mM for maltopentaose (at pH 6.5 and 85 degrees Celsius) {ECO:0000269|PubMed:12127967}; KM=7.77 mM for maltohexaose (at pH 6.5 and 85 degrees Celsius) {ECO:0000269|PubMed:12127967}; KM=7.41 mM for maltoheptaose (at pH 6.5 and 85 degrees Celsius) {ECO:0000269|PubMed:12127967}; KM=2.26 mM for pNP-maltopentaose (at pH 6.5 and 85 degrees Celsius) {ECO:0000269|PubMed:12127967}; KM=14.53 mM for beta-cyclodextrin (at pH 6.5 and 85 degrees Celsius) {ECO:0000269|PubMed:12127967}; |
| Metal Binding | |
| Rhea ID | RHEA:23980 |
| Cross Reference Brenda | 3.2.1.B8; |