| IED ID | IndEnz0001000391 |
| Enzyme Type ID | amylase000391 |
| Protein Name |
Malto-oligosyltrehalose trehalohydrolase MTHase EC 3.2.1.141 4-alpha-D- 1- 4 -alpha-D-glucano trehalose trehalohydrolase Maltooligosyl trehalose trehalohydrolase |
| Gene Name | treZ |
| Organism | Brevibacterium helvolum |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Micrococcales Brevibacteriaceae Brevibacterium Brevibacterium helvolum |
| Enzyme Sequence | MTLVNVGPERFDVWAPDVSSVVLVADGRQYPMQKKETAPGSEGWWTASDAPPNGDVDYGYLLDGNTTPVPEPRSRRLPAGVHNHSRTYNPPPYRWQDSRWRGKELQGTLIYQLHVGTSTPDGTLDAAGEKLSYLVDLGIDFIELLPVNGFNGTHNWGYDGVQWYTVHEGYGGPAAYQRFVDAAHAAGLGVIQDVVYNHLGLRGNYFPKLGPNLKQGDANTLGDSVNLDGAGSDVFREYILDNAALWVGDYHVDGVGFDAVHAVRDERAVHILEDLGALGDAISGETGLPKTLIAESDFNNPRLIYPRDVNGYGLAGQWSDDFHTAVHVSVSGETTGYYSDFESLAVLAKVLKDGFLHDGSYSSFRGRHHGRPINPSLANPAALVVCNQNHDQIGNRATGDRLSQSLSYGQLAVAAVLTLTSPFTPMLFMGEEYGASTPWQFFTSHPEPELGKATAEGRIKEFERMGWDPAVVPDPQDPETFNRSKLDWSEASTGDHARLLELYKSLTALRREHPDLADLGFGQTEVSFDDDAGWLRFRPVSVEVLVNLSDAKVRLDDAAGDLLLATDEGNPLDGGSLALVPWSAAVLKS |
| Enzyme Length | 589 |
| Uniprot Accession Number | O52520 |
| Absorption | |
| Active Site | ACT_SITE 258; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q55088; ACT_SITE 295; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:Q55088 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-((1->4)-alpha-D-glucanosyl)(n) trehalose to yield trehalose and (1->4)-alpha-D-glucan.; EC=3.2.1.141; Evidence={ECO:0000250|UniProtKB:Q55088}; |
| DNA Binding | |
| EC Number | 3.2.1.141 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Glycan biosynthesis; trehalose biosynthesis. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Region (3); Site (1) |
| Keywords | Carbohydrate metabolism;Cytoplasm;Glycosidase;Hydrolase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 64,217 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.141; |