| IED ID | IndEnz0001000014 |
| Enzyme Type ID | amylase000014 |
| Protein Name |
Trehalose synthase/amylase TreS EC 3.2.1.1 EC 5.4.99.16 Maltose alpha-D-glucosyltransferase MTase |
| Gene Name | treS MSMEG_6515 MSMEI_6343 |
| Organism | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycolicibacterium Mycolicibacterium smegmatis (Mycobacterium smegmatis) Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
| Enzyme Sequence | MEEHTQGSHVEAGIVEHPNAEDFGHARTLPTDTNWFKHAVFYEVLVRAFYDSNADGIGDLRGLTEKLDYIKWLGVDCLWLPPFYDSPLRDGGYDIRDFYKVLPEFGTVDDFVTLLDAAHRRGIRIITDLVMNHTSDQHEWFQESRHNPDGPYGDFYVWSDTSDRYPDARIIFVDTEESNWTFDPVRRQFYWHRFFSHQPDLNYDNPAVQEAMLDVLRFWLDLGIDGFRLDAVPYLFEREGTNCENLPETHAFLKRCRKAIDDEYPGRVLLAEANQWPADVVAYFGDPDTGGDECHMAFHFPLMPRIFMAVRRESRFPISEILAQTPPIPDTAQWGIFLRNHDELTLEMVTDEERDYMYAEYAKDPRMKANVGIRRRLAPLLENDRNQIELFTALLLSLPGSPVLYYGDEIGMGDIIWLGDRDSVRTPMQWTPDRNAGFSKATPGRLYLPPNQDAVYGYHSVNVEAQLDSSSSLLNWTRNMLAVRSRHDAFAVGTFRELGGSNPSVLAYIREVTRQQGDGGAKTDAVLCVNNLSRFPQPIELNLQQWAGYIPVEMTGYVEFPSIGQLPYLLTLPGHGFYWFQLREPDPEPGAQQ |
| Enzyme Length | 593 |
| Uniprot Accession Number | A0R6E0 |
| Absorption | |
| Active Site | ACT_SITE 230; /note=Nucleophile; /evidence=ECO:0000269|PubMed:21840994; ACT_SITE 272; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:Q9ZEU2 |
| Activity Regulation | ACTIVITY REGULATION: The amylase activity is stimulated by addition of Ca(2+), but this cation and other divalent cations inhibit the trehalose synthase activity. In addition, trehalose synthase activity, but not amylase activity, is strongly inhibited, and in a competitive manner, by validoxylamine. On the other hand, amylase, but not trehalose synthase activity, is inhibited by the known transition-state amylase inhibitor, acarbose, suggesting the possibility of two different active sites. Other metal ions such as Mg(2+), Mn(2+), and Co(2+) are also somewhat effective in the stimulation of amylase activity, but Hg(2+), Cu(2+), Ni(2+) and Zn(2+) are inhibitory. {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:3294776}. |
| Binding Site | BINDING 90; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ZEU2; BINDING 133; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ZEU2; BINDING 198; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ZEU2; BINDING 228; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ZEU2; BINDING 341; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ZEU2; BINDING 342; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ZEU2 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=D-maltose = alpha,alpha-trehalose; Xref=Rhea:RHEA:15145, ChEBI:CHEBI:16551, ChEBI:CHEBI:17306; EC=5.4.99.16; Evidence={ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; Evidence={ECO:0000269|PubMed:18505459}; |
| DNA Binding | |
| EC Number | 3.2.1.1; 5.4.99.16 |
| Enzyme Function | FUNCTION: Catalyzes the reversible interconversion of maltose and trehalose by transglucosylation (PubMed:15511231, PubMed:18505459, PubMed:20118231, PubMed:21840994). Maltose is the preferred substrate (PubMed:15511231, PubMed:18505459). To a lesser extent, also displays amylase activity, catalyzing the endohydrolysis of (1->4)-alpha-D-glucosidic linkages in glycogen and maltooligosaccharides such as maltoheptaose, to produce maltose which then can be converted to trehalose (PubMed:18505459). TreS plays a key role in the utilization of trehalose for the production of glycogen and alpha-glucan via the TreS-Pep2 branch involved in the biosynthesis of maltose-1-phosphate (M1P) (PubMed:20118231, PubMed:27513637). Might also function as a sensor and/or regulator of trehalose levels within the cell. Thus, when trehalose levels in the cell become dangerously low, TreS can expedite the conversion of glycogen to maltose via its amylase activity and then convert the maltose to trehalose; but this enzyme also can expedite or promote the conversion of trehalose to glycogen when cytoplasmic trehalose levels become too high. Is also able to catalyze the hydrolytic cleavage of alpha-aryl glucosides, as well as alpha-glucosyl fluoride in vitro. {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:20118231, ECO:0000269|PubMed:21840994, ECO:0000269|PubMed:27513637}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 6.0-6.2 for the amylase activity and 7.0 for the trehalose synthase activity. {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459}; |
| Pathway | PATHWAY: Glycan biosynthesis; glycogen biosynthesis. {ECO:0000269|PubMed:20118231, ECO:0000269|PubMed:27513637}. |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (23); Binding site (6); Chain (1); Helix (28); Metal binding (5); Turn (13) |
| Keywords | 3D-structure;Calcium;Carbohydrate metabolism;Glycogen biosynthesis;Glycogen metabolism;Glycosidase;Hydrolase;Isomerase;Metal-binding;Polysaccharide degradation;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 3ZO9; 3ZOA; 5JY7; |
| Mapped Pubmed ID | 30877199; |
| Motif | |
| Gene Encoded By | |
| Mass | 68,201 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8.0 mM for maltose (at pH 6.8 and 37 degrees Celsius) {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994}; KM=87 mM for trehalose (at pH 6.8 and at 37 degrees Celsius) {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994}; KM=2.9 mM for 2,4-dinitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius) {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994}; KM=2.5 mM for 3,4-dinitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius) {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994}; KM=2.2 mM for 4-chloro-2-nitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius) {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994}; KM=5.8 mM for 4-nitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius) {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994}; KM=0.7 mM for 2-nitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius) {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994}; KM=0.15 mM for alpha-glucosyl fluoride (at pH 6.8 and 37 degrees Celsius) {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994}; |
| Metal Binding | METAL 132; /note="Calcium"; /evidence="ECO:0000269|PubMed:23735230, ECO:0007744|PDB:3ZO9, ECO:0007744|PDB:3ZOA"; METAL 200; /note="Calcium"; /evidence="ECO:0000269|PubMed:23735230, ECO:0007744|PDB:3ZO9, ECO:0007744|PDB:3ZOA"; METAL 234; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:23735230, ECO:0007744|PDB:3ZO9, ECO:0007744|PDB:3ZOA"; METAL 235; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:23735230, ECO:0007744|PDB:3ZO9, ECO:0007744|PDB:3ZOA"; METAL 237; /note="Calcium"; /evidence="ECO:0000269|PubMed:23735230, ECO:0007744|PDB:3ZO9, ECO:0007744|PDB:3ZOA" |
| Rhea ID | RHEA:15145 |
| Cross Reference Brenda | 5.4.99.16; |