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Literature summary extracted from
- Biotechnical production of trehalose through the trehalose synthase pathway current status and future prospects (2018), Appl. Microbiol. Biotechnol., 102, 2965-2976 .
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 5.4.99.16 | additional information | physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease | Thermus thermophilus |
| 5.4.99.16 | additional information | physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease | Paenarthrobacter aurescens |
| 5.4.99.16 | additional information | physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease | Meiothermus ruber |
| 5.4.99.16 | additional information | physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease | Deinococcus geothermalis |
| 5.4.99.16 | additional information | physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease | Deinococcus radiodurans |
| 5.4.99.16 | additional information | physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease | Corynebacterium glutamicum |
| 5.4.99.16 | additional information | physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease | Picrophilus torridus |
| 5.4.99.16 | additional information | physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease | Thermobaculum terrenum |
| 5.4.99.16 | additional information | physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease | Thermobifida fusca |
| 5.4.99.16 | additional information | physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease | Thermomonospora curvata |
| 5.4.99.16 | additional information | physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease | Enterobacter hormaechei |
| 5.4.99.16 | additional information | physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease | Pseudomonas sp. P8005 |
| 5.4.99.16 | additional information | physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease | Pseudomonas stutzeri |
| 5.4.99.16 | additional information | physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease | Rhodococcus opacus |
| 5.4.99.16 | additional information | physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease | Mycobacterium tuberculosis |
| 5.4.99.16 | additional information | physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose was found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease | Mycolicibacterium smegmatis |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 5.4.99.16 | enzyme complexed with alpha-acarbose, Ca2+, Cl-, and Mg2+ or with Cl-, Ca2+, and Mg2+, PDB IDs 3ZOA and 3ZO9, X-ray diffraction structure determination and analysis at 1.85 and 1.84 A resolution, respectively | Mycolicibacterium smegmatis |
| 5.4.99.16 | enzyme complexed with Ca2+, glycerin, and sulfate ion, PDB ID 4LXF, X-ray diffraction structure determination and analysis at 2.6 A resolution | Mycobacterium tuberculosis |
| 5.4.99.16 | enzyme complexed with Ca2+, Mg2+, and tromethamine, PDB ID 4TVU, X-ray diffraction structure determination and analysis at 2.7 A resolution | Deinococcus radiodurans |
| 5.4.99.16 | enzyme, PDB ID 5X7U, X-ray diffraction structure determination and analysis at 2.5 A resolution | Thermobaculum terrenum |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 5.4.99.16 | E330A | site-directed mutagenesis, residue E330 is vital for product formation, the mutant shows only hydrolase activity but no transglucosidic activity | Thermomonospora curvata |
| 5.4.99.16 | H534Y | site-directed mutagenesis, mutation of the metal ion-binding site, the mutant shows 50% of the wild-type activity | Thermobaculum terrenum |
| 5.4.99.16 | I150F | site-directed mutagenesis, a residue in subdomain B, constitute part of the active-site pocket, the mutant shows 55% of the isomerase activity and 170% of the hydrolase activity compared to wild-type | Deinococcus radiodurans |
| 5.4.99.16 | L116E | site-directed mutagenesis, residue L116 forms bond with H120 and D217, supposedly important for substrate specificity, the mutant shows 101% activity with maltose and 74% with sucrose compared to wild-type | Thermomonospora curvata |
| 5.4.99.16 | L116G | site-directed mutagenesis, residue L116 forms bond with H120 and D217, supposedly important for substrate specificity, the mutant shows 17% activity with maltose and 144% with sucrose compared to wild-type | Thermomonospora curvata |
| 5.4.99.16 | L116M | site-directed mutagenesis, residue L116 forms bond with H120 and D217, supposedly important for substrate specificity, the mutant shows 118% activity with maltose and 78% with sucrose compared to wild-type | Thermomonospora curvata |
| 5.4.99.16 | N253A | site-directed mutagenesis, residue Asn253 forms a hydrogen bond with Glu324, N253A causes movement of the Glu324 side chain, leading to the creation of a small pore for water entry, the mutant shows 11% of the isomerase activity and 180% of the hydrolase activity compared to wild-type | Deinococcus radiodurans |
| 5.4.99.16 | R148A | site-directed mutagenesis, Arg148 forms salt bridges with Glu223 and Glu324, the mutant shows 12% of the isomerase activity and 150% of the hydrolase activity compared to wild-type | Deinococcus radiodurans |
| 5.4.99.16 | R283G/Y287R/R291G | site-directed mutagenesis, mutation of the metal ion-binding site, the mutant shows 36% of the wild-type activity | Thermobaculum terrenum |
| 5.4.99.16 | R283G/Y287R/R291G/H534Y | site-directed mutagenesis, mutation of the metal ion-binding site, the mutant shows 35% of the wild-type activity | Thermobaculum terrenum |
| 5.4.99.16 | Y213A/E320A/E324A | site-directed mutagenesis, the catalytic triad residues, no isomerase or hydrolase activity detected | Deinococcus radiodurans |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.16 | 60000 | - |
- |
Thermomonospora curvata |
| 5.4.99.16 | 61000 | - |
- |
Deinococcus radiodurans |
| 5.4.99.16 | 64000 | - |
- |
Deinococcus radiodurans |
| 5.4.99.16 | 65000 | - |
- |
Deinococcus geothermalis |
| 5.4.99.16 | 65000 | - |
- |
Picrophilus torridus |
| 5.4.99.16 | 65000 | - |
- |
Thermobaculum terrenum |
| 5.4.99.16 | 65000 | - |
- |
Enterobacter hormaechei |
| 5.4.99.16 | 66000 | - |
- |
Thermobifida fusca |
| 5.4.99.16 | 68000 | - |
- |
Paenarthrobacter aurescens |
| 5.4.99.16 | 76000 | - |
- |
Pseudomonas stutzeri |
| 5.4.99.16 | 79000 | - |
- |
Rhodococcus opacus |
| 5.4.99.16 | 106000 | - |
- |
Thermus thermophilus |
| 5.4.99.16 | 110000 | - |
- |
Meiothermus ruber |
| 5.4.99.16 | 126000 | - |
- |
Pseudomonas sp. P8005 |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.4.99.16 | maltose | Thermus thermophilus | - |
alpha,alpha-trehalose | - |
r |  |
| 5.4.99.16 | maltose | Paenarthrobacter aurescens | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Meiothermus ruber | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Deinococcus geothermalis | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Deinococcus radiodurans | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Mycolicibacterium smegmatis | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Corynebacterium glutamicum | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Picrophilus torridus | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Thermobaculum terrenum | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Thermobifida fusca | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Thermomonospora curvata | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Enterobacter hormaechei | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Pseudomonas sp. P8005 | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Pseudomonas stutzeri | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Rhodococcus opacus | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Mycobacterium tuberculosis | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Thermus thermophilus ATCC 33923 | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Pseudomonas stutzeri CJ38 | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Enterobacter hormaechei ATCC 49162 | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Corynebacterium glutamicum ATCC 13032 | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Rhodococcus opacus ATCC 41021 | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Mycobacterium tuberculosis ATCC 25618 / H37Rv | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Mycolicibacterium smegmatis ATCC 700084 / mc2_155 | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Thermobifida fusca DSM 43792 | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Picrophilus torridus DSM 9790 | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422 | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Deinococcus geothermalis DSMZ 11300 | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Thermomonospora curvata DSM 43183 | - |
alpha,alpha-trehalose | - |
r | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.4.99.16 | Corynebacterium glutamicum | A0A1R4FYB1 | - |
- |
| 5.4.99.16 | Corynebacterium glutamicum ATCC 13032 | A0A1R4FYB1 | - |
- |
| 5.4.99.16 | Deinococcus geothermalis | Q1J0Z5 | - |
- |
| 5.4.99.16 | Deinococcus geothermalis DSMZ 11300 | Q1J0Z5 | - |
- |
| 5.4.99.16 | Deinococcus radiodurans | I3NX86 | - |
- |
| 5.4.99.16 | Deinococcus radiodurans | Q9RST7 | - |
- |
| 5.4.99.16 | Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422 | I3NX86 | - |
- |
| 5.4.99.16 | Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422 | Q9RST7 | - |
- |
| 5.4.99.16 | Enterobacter hormaechei | F5S1H2 | - |
- |
| 5.4.99.16 | Enterobacter hormaechei ATCC 49162 | F5S1H2 | - |
- |
| 5.4.99.16 | Meiothermus ruber | B1PK99 | - |
- |
| 5.4.99.16 | Mycobacterium tuberculosis | P9WQ19 | - |
- |
| 5.4.99.16 | Mycobacterium tuberculosis ATCC 25618 / H37Rv | P9WQ19 | - |
- |
| 5.4.99.16 | Mycolicibacterium smegmatis | A0R6E0 | - |
- |
| 5.4.99.16 | Mycolicibacterium smegmatis ATCC 700084 / mc2_155 | A0R6E0 | - |
- |
| 5.4.99.16 | Paenarthrobacter aurescens | B8YM30 | - |
- |
| 5.4.99.16 | Picrophilus torridus | Q6L2Z7 | - |
- |
| 5.4.99.16 | Picrophilus torridus DSM 9790 | Q6L2Z7 | - |
- |
| 5.4.99.16 | Pseudomonas sp. P8005 | I3WCP4 | - |
- |
| 5.4.99.16 | Pseudomonas stutzeri | A0A4S2BJW1 | - |
- |
| 5.4.99.16 | Pseudomonas stutzeri CJ38 | A0A4S2BJW1 | - |
- |
| 5.4.99.16 | Rhodococcus opacus | M1PA89 | - |
- |
| 5.4.99.16 | Rhodococcus opacus ATCC 41021 | M1PA89 | - |
- |
| 5.4.99.16 | Thermobaculum terrenum | D1CE96 | - |
- |
| 5.4.99.16 | Thermobifida fusca | Q47SE5 | - |
- |
| 5.4.99.16 | Thermobifida fusca DSM 43792 | Q47SE5 | - |
- |
| 5.4.99.16 | Thermomonospora curvata | D1ABU6 | - |
- |
| 5.4.99.16 | Thermomonospora curvata DSM 43183 | D1ABU6 | - |
- |
| 5.4.99.16 | Thermus thermophilus | - |
- |
- |
| 5.4.99.16 | Thermus thermophilus | O06458 | - |
- |
| 5.4.99.16 | Thermus thermophilus ATCC 33923 | O06458 | - |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 5.4.99.16 | maltose = alpha,alpha-trehalose | two-step, double displacement mechanism of the enzyme, overview | Thermus thermophilus | |
| 5.4.99.16 | maltose = alpha,alpha-trehalose | two-step, double displacement mechanism of the enzyme, overview | Paenarthrobacter aurescens | |
| 5.4.99.16 | maltose = alpha,alpha-trehalose | two-step, double displacement mechanism of the enzyme, overview | Meiothermus ruber | |
| 5.4.99.16 | maltose = alpha,alpha-trehalose | two-step, double displacement mechanism of the enzyme, overview | Deinococcus geothermalis | |
| 5.4.99.16 | maltose = alpha,alpha-trehalose | two-step, double displacement mechanism of the enzyme, overview | Deinococcus radiodurans | |
| 5.4.99.16 | maltose = alpha,alpha-trehalose | two-step, double displacement mechanism of the enzyme, overview | Mycolicibacterium smegmatis | |
| 5.4.99.16 | maltose = alpha,alpha-trehalose | two-step, double displacement mechanism of the enzyme, overview | Corynebacterium glutamicum | |
| 5.4.99.16 | maltose = alpha,alpha-trehalose | two-step, double displacement mechanism of the enzyme, overview | Picrophilus torridus | |
| 5.4.99.16 | maltose = alpha,alpha-trehalose | two-step, double displacement mechanism of the enzyme, overview | Thermobaculum terrenum | |
| 5.4.99.16 | maltose = alpha,alpha-trehalose | two-step, double displacement mechanism of the enzyme, overview | Thermobifida fusca | |
| 5.4.99.16 | maltose = alpha,alpha-trehalose | two-step, double displacement mechanism of the enzyme, overview | Thermomonospora curvata | |
| 5.4.99.16 | maltose = alpha,alpha-trehalose | two-step, double displacement mechanism of the enzyme, overview | Enterobacter hormaechei | |
| 5.4.99.16 | maltose = alpha,alpha-trehalose | two-step, double displacement mechanism of the enzyme, overview | Pseudomonas sp. P8005 | |
| 5.4.99.16 | maltose = alpha,alpha-trehalose | two-step, double displacement mechanism of the enzyme, overview | Pseudomonas stutzeri | |
| 5.4.99.16 | maltose = alpha,alpha-trehalose | two-step, double displacement mechanism of the enzyme, overview | Rhodococcus opacus | |
| 5.4.99.16 | maltose = alpha,alpha-trehalose | two-step, double displacement mechanism of the enzyme, overview | Mycobacterium tuberculosis |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.16 | 2 | - |
pH 9.0, 50°C | Thermus thermophilus |
| 5.4.99.16 | 11.4 | - |
pH 7.6, 30°C | Deinococcus radiodurans |
| 5.4.99.16 | 18.5 | - |
pH 6.0, 37°C | Enterobacter hormaechei |
| 5.4.99.16 | 79.2 | - |
pH 8.5, 35°C | Pseudomonas stutzeri |
| 5.4.99.16 | 80 | - |
pH 6.0, 45°C | Picrophilus torridus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.4.99.16 | maltose | - |
Thermus thermophilus | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Paenarthrobacter aurescens | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Meiothermus ruber | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Deinococcus geothermalis | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Deinococcus radiodurans | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Mycolicibacterium smegmatis | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Corynebacterium glutamicum | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Picrophilus torridus | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Thermobaculum terrenum | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Thermobifida fusca | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Thermomonospora curvata | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Enterobacter hormaechei | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Pseudomonas sp. P8005 | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Pseudomonas stutzeri | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Rhodococcus opacus | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Mycobacterium tuberculosis | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Thermus thermophilus ATCC 33923 | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Pseudomonas stutzeri CJ38 | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Enterobacter hormaechei ATCC 49162 | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Corynebacterium glutamicum ATCC 13032 | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Rhodococcus opacus ATCC 41021 | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Mycobacterium tuberculosis ATCC 25618 / H37Rv | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Mycolicibacterium smegmatis ATCC 700084 / mc2_155 | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Thermobifida fusca DSM 43792 | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Picrophilus torridus DSM 9790 | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422 | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Deinococcus geothermalis DSMZ 11300 | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Thermomonospora curvata DSM 43183 | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | additional information | the enzyme yields 48% trehalose from 100 mM maltose at 37°C | Enterobacter hormaechei | ? | - |
? | |
| 5.4.99.16 | additional information | the enzyme yields 50-71% trehalose from 150 mM maltose at 20-60°C in 72 h with 3.6-19.2% D-glucose by-product | Picrophilus torridus | ? | - |
? | |
| 5.4.99.16 | additional information | the enzyme yields 55-65% trehalose from 440 mM maltose at 25°C in 24 h with 10-15% D-glucose by-product | Thermobifida fusca | ? | - |
? | |
| 5.4.99.16 | additional information | the enzyme yields 56.8-60.4% trehalose from 300 mM maltose at 40°C in 16-24 h with 7.3-8.6% D-glucose by-product | Deinococcus geothermalis | ? | - |
? | |
| 5.4.99.16 | additional information | the enzyme yields 58.2% trehalose from 300 mM maltose at 30°C in 24 h with 7.1% D-glucose by-product | Deinococcus radiodurans | ? | - |
? | |
| 5.4.99.16 | additional information | the enzyme yields 59-69% trehalose from 15 mM maltose at 25-35°C in 4-9 h with 14.4-21.7% D-glucose by-product | Corynebacterium glutamicum | ? | - |
? | |
| 5.4.99.16 | additional information | the enzyme yields 59.5% trehalose from 90 mM maltose at 30°C in 8 h with 13.2% D-glucose by-product | Paenarthrobacter aurescens | ? | - |
? | |
| 5.4.99.16 | additional information | the enzyme yields 61-64% trehalose from 60 mM maltose at 20-30°C in 24 h with 2.3-4.5% D-glucose by-product | Meiothermus ruber | ? | - |
? | |
| 5.4.99.16 | additional information | the enzyme yields 67% trehalose from 90 mM maltose at 25°C with 12% D-glucose by-product | Rhodococcus opacus | ? | - |
? | |
| 5.4.99.16 | additional information | the enzyme yields 70% trehalose at 35°C with 8% D-glucose by-product | Thermomonospora curvata | ? | - |
? | |
| 5.4.99.16 | additional information | the enzyme yields 70% trehalose from 100 mM maltose at 37°C in 12 h with 8.0% D-glucose by-product | Pseudomonas sp. P8005 | ? | - |
? | |
| 5.4.99.16 | additional information | the enzyme yields 70% trehalose from 150 mM maltose at 45°C in 10 h | Thermobaculum terrenum | ? | - |
? | |
| 5.4.99.16 | additional information | the enzyme yields 74% trehalose from 292 mM maltose at 50°C in 10 h | Thermus thermophilus | ? | - |
? | |
| 5.4.99.16 | additional information | the enzyme yields 75% trehalose from 580 mM maltose at 15°C in 19 h without D-glucose by-product | Pseudomonas stutzeri | ? | - |
? | |
| 5.4.99.16 | additional information | the enzyme yields 80% trehalose from 800 mM maltose at 30°C in 48 h | Thermus thermophilus | ? | - |
? | |
| 5.4.99.16 | additional information | the enzyme yields 92% trehalose from 800 mM maltose at 5°C in 48 h | Deinococcus radiodurans | ? | - |
? | |
| 5.4.99.16 | additional information | the enzyme yields 80% trehalose from 800 mM maltose at 30°C in 48 h | Thermus thermophilus ATCC 33923 | ? | - |
? | |
| 5.4.99.16 | additional information | the enzyme yields 75% trehalose from 580 mM maltose at 15°C in 19 h without D-glucose by-product | Pseudomonas stutzeri CJ38 | ? | - |
? | |
| 5.4.99.16 | additional information | the enzyme yields 48% trehalose from 100 mM maltose at 37°C | Enterobacter hormaechei ATCC 49162 | ? | - |
? | |
| 5.4.99.16 | additional information | the enzyme yields 59-69% trehalose from 15 mM maltose at 25-35°C in 4-9 h with 14.4-21.7% D-glucose by-product | Corynebacterium glutamicum ATCC 13032 | ? | - |
? | |
| 5.4.99.16 | additional information | the enzyme yields 67% trehalose from 90 mM maltose at 25°C with 12% D-glucose by-product | Rhodococcus opacus ATCC 41021 | ? | - |
? | |
| 5.4.99.16 | additional information | the enzyme yields 55-65% trehalose from 440 mM maltose at 25°C in 24 h with 10-15% D-glucose by-product | Thermobifida fusca DSM 43792 | ? | - |
? | |
| 5.4.99.16 | additional information | the enzyme yields 50-71% trehalose from 150 mM maltose at 20-60°C in 72 h with 3.6-19.2% D-glucose by-product | Picrophilus torridus DSM 9790 | ? | - |
? | |
| 5.4.99.16 | additional information | the enzyme yields 58.2% trehalose from 300 mM maltose at 30°C in 24 h with 7.1% D-glucose by-product | Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422 | ? | - |
? | |
| 5.4.99.16 | additional information | the enzyme yields 92% trehalose from 800 mM maltose at 5°C in 48 h | Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422 | ? | - |
? | |
| 5.4.99.16 | additional information | the enzyme yields 56.8-60.4% trehalose from 300 mM maltose at 40°C in 16-24 h with 7.3-8.6% D-glucose by-product | Deinococcus geothermalis DSMZ 11300 | ? | - |
? | |
| 5.4.99.16 | additional information | the enzyme yields 70% trehalose at 35°C with 8% D-glucose by-product | Thermomonospora curvata DSM 43183 | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.4.99.16 | dimer | - |
Deinococcus radiodurans |
| 5.4.99.16 | dimer | asymmetric | Mycolicibacterium smegmatis |
| 5.4.99.16 | tetramer | - |
Mycobacterium tuberculosis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.4.99.16 | Dgeo_0537 | - |
Deinococcus geothermalis |
| 5.4.99.16 | DOT40_01605 | locus name | Pseudomonas stutzeri |
| 5.4.99.16 | DR_2036 | - |
Deinococcus radiodurans |
| 5.4.99.16 | FM102_08285 | - |
Corynebacterium glutamicum |
| 5.4.99.16 | HMPREF9086_3732 | locus name | Enterobacter hormaechei |
| 5.4.99.16 | PTO0069 | - |
Picrophilus torridus |
| 5.4.99.16 | Tfu_0584 | - |
Thermobifida fusca |
| 5.4.99.16 | Trehalose synthase | - |
Thermus thermophilus |
| 5.4.99.16 | Trehalose synthase | - |
Paenarthrobacter aurescens |
| 5.4.99.16 | Trehalose synthase | - |
Meiothermus ruber |
| 5.4.99.16 | Trehalose synthase | - |
Deinococcus geothermalis |
| 5.4.99.16 | Trehalose synthase | - |
Deinococcus radiodurans |
| 5.4.99.16 | Trehalose synthase | - |
Mycolicibacterium smegmatis |
| 5.4.99.16 | Trehalose synthase | - |
Corynebacterium glutamicum |
| 5.4.99.16 | Trehalose synthase | - |
Picrophilus torridus |
| 5.4.99.16 | Trehalose synthase | - |
Thermobaculum terrenum |
| 5.4.99.16 | Trehalose synthase | - |
Thermobifida fusca |
| 5.4.99.16 | Trehalose synthase | - |
Thermomonospora curvata |
| 5.4.99.16 | Trehalose synthase | - |
Enterobacter hormaechei |
| 5.4.99.16 | Trehalose synthase | - |
Pseudomonas sp. P8005 |
| 5.4.99.16 | Trehalose synthase | - |
Pseudomonas stutzeri |
| 5.4.99.16 | Trehalose synthase | - |
Rhodococcus opacus |
| 5.4.99.16 | Trehalose synthase | - |
Mycobacterium tuberculosis |
| 5.4.99.16 | TreS | - |
Thermus thermophilus |
| 5.4.99.16 | TreS | - |
Paenarthrobacter aurescens |
| 5.4.99.16 | TreS | - |
Meiothermus ruber |
| 5.4.99.16 | TreS | - |
Enterobacter hormaechei |
| 5.4.99.16 | TreS | - |
Pseudomonas sp. P8005 |
| 5.4.99.16 | TreS | - |
Pseudomonas stutzeri |
| 5.4.99.16 | TreS | - |
Rhodococcus opacus |
| 5.4.99.16 | Tter_0330 | - |
Thermobaculum terrenum |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.16 | 15 | - |
- |
Deinococcus radiodurans |
| 5.4.99.16 | 25 | - |
- |
Thermobifida fusca |
| 5.4.99.16 | 25 | - |
- |
Rhodococcus opacus |
| 5.4.99.16 | 30 | - |
- |
Deinococcus radiodurans |
| 5.4.99.16 | 35 | - |
- |
Paenarthrobacter aurescens |
| 5.4.99.16 | 35 | - |
- |
Thermomonospora curvata |
| 5.4.99.16 | 35 | - |
- |
Pseudomonas stutzeri |
| 5.4.99.16 | 37 | - |
- |
Enterobacter hormaechei |
| 5.4.99.16 | 37 | - |
- |
Pseudomonas sp. P8005 |
| 5.4.99.16 | 40 | - |
- |
Deinococcus geothermalis |
| 5.4.99.16 | 45 | - |
- |
Picrophilus torridus |
| 5.4.99.16 | 45 | - |
- |
Thermobaculum terrenum |
| 5.4.99.16 | 50 | - |
- |
Thermus thermophilus |
| 5.4.99.16 | 50 | - |
- |
Meiothermus ruber |
| 5.4.99.16 | 65 | - |
- |
Thermus thermophilus |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.16 | 10 | 40 | over 80% activity remains after 30 min | Pseudomonas sp. P8005 |
| 5.4.99.16 | 15 | 45 | 100% activity remains after 1 h | Rhodococcus opacus |
| 5.4.99.16 | 20 | 35 | 100% activity remains after 20 min | Paenarthrobacter aurescens |
| 5.4.99.16 | 40 | - |
50% activity remains after 28.5 h | Deinococcus radiodurans |
| 5.4.99.16 | 40 | - |
90% activity remains after 30 min | Deinococcus radiodurans |
| 5.4.99.16 | 50 | - |
10% activity remains after 30 min | Pseudomonas sp. P8005 |
| 5.4.99.16 | 50 | - |
50% activity remains after 9.5 h | Deinococcus radiodurans |
| 5.4.99.16 | 55 | - |
50% activity remains after 30 min | Deinococcus radiodurans |
| 5.4.99.16 | 55 | - |
40% activity remains after 1 h | Pseudomonas stutzeri |
| 5.4.99.16 | 55 | - |
57% activity remains after 8 h | Deinococcus geothermalis |
| 5.4.99.16 | 60 | - |
90% activity remains after 20 min | Picrophilus torridus |
| 5.4.99.16 | 60 | - |
90% activity remains after 5 h | Meiothermus ruber |
| 5.4.99.16 | 60 | - |
no activity remains after 2 h | Deinococcus radiodurans |
| 5.4.99.16 | 60 | - |
no activity remains after 3 h | Rhodococcus opacus |
| 5.4.99.16 | 65 | - |
88% activity remains after 30 min | Thermus thermophilus |
| 5.4.99.16 | 70 | - |
80% activity remains after 30 min | Thermobaculum terrenum |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.16 | 6 | - |
- |
Picrophilus torridus |
| 5.4.99.16 | 6 | - |
- |
Enterobacter hormaechei |
| 5.4.99.16 | 6.5 | - |
- |
Paenarthrobacter aurescens |
| 5.4.99.16 | 6.5 | - |
- |
Meiothermus ruber |
| 5.4.99.16 | 6.5 | - |
- |
Deinococcus radiodurans |
| 5.4.99.16 | 6.5 | - |
- |
Thermobifida fusca |
| 5.4.99.16 | 6.5 | - |
- |
Thermomonospora curvata |
| 5.4.99.16 | 6.5 | - |
- |
Thermus thermophilus |
| 5.4.99.16 | 7 | - |
- |
Rhodococcus opacus |
| 5.4.99.16 | 7.2 | - |
- |
Pseudomonas sp. P8005 |
| 5.4.99.16 | 7.5 | - |
- |
Thermobaculum terrenum |
| 5.4.99.16 | 7.6 | - |
- |
Deinococcus geothermalis |
| 5.4.99.16 | 7.6 | - |
- |
Deinococcus radiodurans |
| 5.4.99.16 | 8.5 | - |
- |
Pseudomonas stutzeri |
| 5.4.99.16 | 9 | - |
- |
Thermus thermophilus |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 5.4.99.16 | evolution | phylogenetic tree | Thermus thermophilus |
| 5.4.99.16 | evolution | phylogenetic tree | Paenarthrobacter aurescens |
| 5.4.99.16 | evolution | phylogenetic tree | Meiothermus ruber |
| 5.4.99.16 | evolution | phylogenetic tree | Deinococcus geothermalis |
| 5.4.99.16 | evolution | phylogenetic tree | Deinococcus radiodurans |
| 5.4.99.16 | evolution | phylogenetic tree | Mycolicibacterium smegmatis |
| 5.4.99.16 | evolution | phylogenetic tree | Corynebacterium glutamicum |
| 5.4.99.16 | evolution | phylogenetic tree | Picrophilus torridus |
| 5.4.99.16 | evolution | phylogenetic tree | Thermobaculum terrenum |
| 5.4.99.16 | evolution | phylogenetic tree | Thermobifida fusca |
| 5.4.99.16 | evolution | phylogenetic tree | Thermomonospora curvata |
| 5.4.99.16 | evolution | phylogenetic tree | Enterobacter hormaechei |
| 5.4.99.16 | evolution | phylogenetic tree | Pseudomonas sp. P8005 |
| 5.4.99.16 | evolution | phylogenetic tree | Pseudomonas stutzeri |
| 5.4.99.16 | evolution | phylogenetic tree | Rhodococcus opacus |
| 5.4.99.16 | additional information | the C-terminal domain from TtTS plays a key role in maintaining the thermostability, reducing the byproduct glucose formation, and increasing enzyme activity | Thermus thermophilus |
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Release 2023.1 (January 2023)
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