Literature summary for 5.4.99.16 extracted from

Cai, X.; Seitl, I.; Mu, W.; Zhang, T.; Stressler, T.; Fischer, L.; Jiang, B.
Biotechnical production of trehalose through the trehalose synthase pathway current status and future prospects (2018), Appl. Microbiol. Biotechnol., 102, 2965-2976 .

Search for more literature for 5.4.99.16

Application

Application	Comment	Organism
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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)

Crystallization (Comment)	Organism
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
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
enzyme complexed with Ca2+, Mg2+, and tromethamine, PDB ID 4TVU, X-ray diffraction structure determination and analysis at 2.7 A resolution	Deinococcus radiodurans
enzyme, PDB ID 5X7U, X-ray diffraction structure determination and analysis at 2.5 A resolution	Thermobaculum terrenum

Protein Variants

Protein Variants	Comment	Organism
E330A	site-directed mutagenesis, residue E330 is vital for product formation, the mutant shows only hydrolase activity but no transglucosidic activity	Thermomonospora curvata
H534Y	site-directed mutagenesis, mutation of the metal ion-binding site, the mutant shows 50% of the wild-type activity	Thermobaculum terrenum
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
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
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
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
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
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
R283G/Y287R/R291G	site-directed mutagenesis, mutation of the metal ion-binding site, the mutant shows 36% of the wild-type activity	Thermobaculum terrenum
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
Y213A/E320A/E324A	site-directed mutagenesis, the catalytic triad residues, no isomerase or hydrolase activity detected	Deinococcus radiodurans

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
60000	-	-	Thermomonospora curvata
61000	-	-	Deinococcus radiodurans
64000	-	-	Deinococcus radiodurans
65000	-	-	Deinococcus geothermalis
65000	-	-	Picrophilus torridus
65000	-	-	Thermobaculum terrenum
65000	-	-	Enterobacter hormaechei
66000	-	-	Thermobifida fusca
68000	-	-	Paenarthrobacter aurescens
76000	-	-	Pseudomonas stutzeri
79000	-	-	Rhodococcus opacus
106000	-	-	Thermus thermophilus
110000	-	-	Meiothermus ruber
126000	-	-	Pseudomonas sp. P8005

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
maltose	Thermus thermophilus	-	alpha,alpha-trehalose	-	r
maltose	Paenarthrobacter aurescens	-	alpha,alpha-trehalose	-	r
maltose	Meiothermus ruber	-	alpha,alpha-trehalose	-	r
maltose	Deinococcus geothermalis	-	alpha,alpha-trehalose	-	r
maltose	Deinococcus radiodurans	-	alpha,alpha-trehalose	-	r
maltose	Mycolicibacterium smegmatis	-	alpha,alpha-trehalose	-	r
maltose	Corynebacterium glutamicum	-	alpha,alpha-trehalose	-	r
maltose	Picrophilus torridus	-	alpha,alpha-trehalose	-	r
maltose	Thermobaculum terrenum	-	alpha,alpha-trehalose	-	r
maltose	Thermobifida fusca	-	alpha,alpha-trehalose	-	r
maltose	Thermomonospora curvata	-	alpha,alpha-trehalose	-	r
maltose	Enterobacter hormaechei	-	alpha,alpha-trehalose	-	r
maltose	Pseudomonas sp. P8005	-	alpha,alpha-trehalose	-	r
maltose	Pseudomonas stutzeri	-	alpha,alpha-trehalose	-	r
maltose	Rhodococcus opacus	-	alpha,alpha-trehalose	-	r
maltose	Mycobacterium tuberculosis	-	alpha,alpha-trehalose	-	r
maltose	Thermus thermophilus ATCC 33923	-	alpha,alpha-trehalose	-	r
maltose	Pseudomonas stutzeri CJ38	-	alpha,alpha-trehalose	-	r
maltose	Enterobacter hormaechei ATCC 49162	-	alpha,alpha-trehalose	-	r
maltose	Corynebacterium glutamicum ATCC 13032	-	alpha,alpha-trehalose	-	r
maltose	Rhodococcus opacus ATCC 41021	-	alpha,alpha-trehalose	-	r
maltose	Mycobacterium tuberculosis ATCC 25618 / H37Rv	-	alpha,alpha-trehalose	-	r
maltose	Mycolicibacterium smegmatis ATCC 700084 / mc2_155	-	alpha,alpha-trehalose	-	r
maltose	Thermobifida fusca DSM 43792	-	alpha,alpha-trehalose	-	r
maltose	Picrophilus torridus DSM 9790	-	alpha,alpha-trehalose	-	r
maltose	Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422	-	alpha,alpha-trehalose	-	r
maltose	Deinococcus geothermalis DSMZ 11300	-	alpha,alpha-trehalose	-	r
maltose	Thermomonospora curvata DSM 43183	-	alpha,alpha-trehalose	-	r

Organism

Organism	UniProt	Comment	Textmining
Corynebacterium glutamicum	A0A1R4FYB1	-	-
Corynebacterium glutamicum ATCC 13032	A0A1R4FYB1	-	-
Deinococcus geothermalis	Q1J0Z5	-	-
Deinococcus geothermalis DSMZ 11300	Q1J0Z5	-	-
Deinococcus radiodurans	I3NX86	-	-
Deinococcus radiodurans	Q9RST7	-	-
Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422	I3NX86	-	-
Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422	Q9RST7	-	-
Enterobacter hormaechei	F5S1H2	-	-
Enterobacter hormaechei ATCC 49162	F5S1H2	-	-
Meiothermus ruber	B1PK99	-	-
Mycobacterium tuberculosis	P9WQ19	-	-
Mycobacterium tuberculosis ATCC 25618 / H37Rv	P9WQ19	-	-
Mycolicibacterium smegmatis	A0R6E0	-	-
Mycolicibacterium smegmatis ATCC 700084 / mc2_155	A0R6E0	-	-
Paenarthrobacter aurescens	B8YM30	-	-
Picrophilus torridus	Q6L2Z7	-	-
Picrophilus torridus DSM 9790	Q6L2Z7	-	-
Pseudomonas sp. P8005	I3WCP4	-	-
Pseudomonas stutzeri	A0A4S2BJW1	-	-
Pseudomonas stutzeri CJ38	A0A4S2BJW1	-	-
Rhodococcus opacus	M1PA89	-	-
Rhodococcus opacus ATCC 41021	M1PA89	-	-
Thermobaculum terrenum	D1CE96	-	-
Thermobifida fusca	Q47SE5	-	-
Thermobifida fusca DSM 43792	Q47SE5	-	-
Thermomonospora curvata	D1ABU6	-	-
Thermomonospora curvata DSM 43183	D1ABU6	-	-
Thermus thermophilus	-	-	-
Thermus thermophilus	O06458	-	-
Thermus thermophilus ATCC 33923	O06458	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
maltose = alpha,alpha-trehalose	two-step, double displacement mechanism of the enzyme, overview	Thermus thermophilus	a
maltose = alpha,alpha-trehalose	two-step, double displacement mechanism of the enzyme, overview	Paenarthrobacter aurescens	a
maltose = alpha,alpha-trehalose	two-step, double displacement mechanism of the enzyme, overview	Meiothermus ruber	a
maltose = alpha,alpha-trehalose	two-step, double displacement mechanism of the enzyme, overview	Deinococcus geothermalis	a
maltose = alpha,alpha-trehalose	two-step, double displacement mechanism of the enzyme, overview	Deinococcus radiodurans	a
maltose = alpha,alpha-trehalose	two-step, double displacement mechanism of the enzyme, overview	Mycolicibacterium smegmatis	a
maltose = alpha,alpha-trehalose	two-step, double displacement mechanism of the enzyme, overview	Corynebacterium glutamicum	a
maltose = alpha,alpha-trehalose	two-step, double displacement mechanism of the enzyme, overview	Picrophilus torridus	a
maltose = alpha,alpha-trehalose	two-step, double displacement mechanism of the enzyme, overview	Thermobaculum terrenum	a
maltose = alpha,alpha-trehalose	two-step, double displacement mechanism of the enzyme, overview	Thermobifida fusca	a
maltose = alpha,alpha-trehalose	two-step, double displacement mechanism of the enzyme, overview	Thermomonospora curvata	a
maltose = alpha,alpha-trehalose	two-step, double displacement mechanism of the enzyme, overview	Enterobacter hormaechei	a
maltose = alpha,alpha-trehalose	two-step, double displacement mechanism of the enzyme, overview	Pseudomonas sp. P8005	a
maltose = alpha,alpha-trehalose	two-step, double displacement mechanism of the enzyme, overview	Pseudomonas stutzeri	a
maltose = alpha,alpha-trehalose	two-step, double displacement mechanism of the enzyme, overview	Rhodococcus opacus	a
maltose = alpha,alpha-trehalose	two-step, double displacement mechanism of the enzyme, overview	Mycobacterium tuberculosis	a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
2	-	pH 9.0, 50°C	Thermus thermophilus
11.4	-	pH 7.6, 30°C	Deinococcus radiodurans
18.5	-	pH 6.0, 37°C	Enterobacter hormaechei
79.2	-	pH 8.5, 35°C	Pseudomonas stutzeri
80	-	pH 6.0, 45°C	Picrophilus torridus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
maltose	-	Thermus thermophilus	alpha,alpha-trehalose	-	r
maltose	-	Paenarthrobacter aurescens	alpha,alpha-trehalose	-	r
maltose	-	Meiothermus ruber	alpha,alpha-trehalose	-	r
maltose	-	Deinococcus geothermalis	alpha,alpha-trehalose	-	r
maltose	-	Deinococcus radiodurans	alpha,alpha-trehalose	-	r
maltose	-	Mycolicibacterium smegmatis	alpha,alpha-trehalose	-	r
maltose	-	Corynebacterium glutamicum	alpha,alpha-trehalose	-	r
maltose	-	Picrophilus torridus	alpha,alpha-trehalose	-	r
maltose	-	Thermobaculum terrenum	alpha,alpha-trehalose	-	r
maltose	-	Thermobifida fusca	alpha,alpha-trehalose	-	r
maltose	-	Thermomonospora curvata	alpha,alpha-trehalose	-	r
maltose	-	Enterobacter hormaechei	alpha,alpha-trehalose	-	r
maltose	-	Pseudomonas sp. P8005	alpha,alpha-trehalose	-	r
maltose	-	Pseudomonas stutzeri	alpha,alpha-trehalose	-	r
maltose	-	Rhodococcus opacus	alpha,alpha-trehalose	-	r
maltose	-	Mycobacterium tuberculosis	alpha,alpha-trehalose	-	r
maltose	-	Thermus thermophilus ATCC 33923	alpha,alpha-trehalose	-	r
maltose	-	Pseudomonas stutzeri CJ38	alpha,alpha-trehalose	-	r
maltose	-	Enterobacter hormaechei ATCC 49162	alpha,alpha-trehalose	-	r
maltose	-	Corynebacterium glutamicum ATCC 13032	alpha,alpha-trehalose	-	r
maltose	-	Rhodococcus opacus ATCC 41021	alpha,alpha-trehalose	-	r
maltose	-	Mycobacterium tuberculosis ATCC 25618 / H37Rv	alpha,alpha-trehalose	-	r
maltose	-	Mycolicibacterium smegmatis ATCC 700084 / mc2_155	alpha,alpha-trehalose	-	r
maltose	-	Thermobifida fusca DSM 43792	alpha,alpha-trehalose	-	r
maltose	-	Picrophilus torridus DSM 9790	alpha,alpha-trehalose	-	r
maltose	-	Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422	alpha,alpha-trehalose	-	r
maltose	-	Deinococcus geothermalis DSMZ 11300	alpha,alpha-trehalose	-	r
maltose	-	Thermomonospora curvata DSM 43183	alpha,alpha-trehalose	-	r
additional information	the enzyme yields 48% trehalose from 100 mM maltose at 37°C	Enterobacter hormaechei	?	-	?
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	?	-	?
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	?	-	?
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	?	-	?
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	?	-	?
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	?	-	?
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	?	-	?
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	?	-	?
additional information	the enzyme yields 67% trehalose from 90 mM maltose at 25°C with 12% D-glucose by-product	Rhodococcus opacus	?	-	?
additional information	the enzyme yields 70% trehalose at 35°C with 8% D-glucose by-product	Thermomonospora curvata	?	-	?
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	?	-	?
additional information	the enzyme yields 70% trehalose from 150 mM maltose at 45°C in 10 h	Thermobaculum terrenum	?	-	?
additional information	the enzyme yields 74% trehalose from 292 mM maltose at 50°C in 10 h	Thermus thermophilus	?	-	?
additional information	the enzyme yields 75% trehalose from 580 mM maltose at 15°C in 19 h without D-glucose by-product	Pseudomonas stutzeri	?	-	?
additional information	the enzyme yields 80% trehalose from 800 mM maltose at 30°C in 48 h	Thermus thermophilus	?	-	?
additional information	the enzyme yields 92% trehalose from 800 mM maltose at 5°C in 48 h	Deinococcus radiodurans	?	-	?
additional information	the enzyme yields 80% trehalose from 800 mM maltose at 30°C in 48 h	Thermus thermophilus ATCC 33923	?	-	?
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	?	-	?
additional information	the enzyme yields 48% trehalose from 100 mM maltose at 37°C	Enterobacter hormaechei ATCC 49162	?	-	?
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	?	-	?
additional information	the enzyme yields 67% trehalose from 90 mM maltose at 25°C with 12% D-glucose by-product	Rhodococcus opacus ATCC 41021	?	-	?
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	?	-	?
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	?	-	?
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	?	-	?
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	?	-	?
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	?	-	?
additional information	the enzyme yields 70% trehalose at 35°C with 8% D-glucose by-product	Thermomonospora curvata DSM 43183	?	-	?

Subunits

Subunits	Comment	Organism
dimer	-	Deinococcus radiodurans
dimer	asymmetric	Mycolicibacterium smegmatis
tetramer	-	Mycobacterium tuberculosis

Synonyms

Synonyms	Comment	Organism
Dgeo_0537	-	Deinococcus geothermalis
DOT40_01605	locus name	Pseudomonas stutzeri
DR_2036	-	Deinococcus radiodurans
FM102_08285	-	Corynebacterium glutamicum
HMPREF9086_3732	locus name	Enterobacter hormaechei
PTO0069	-	Picrophilus torridus
Tfu_0584	-	Thermobifida fusca
Trehalose synthase	-	Thermus thermophilus
Trehalose synthase	-	Paenarthrobacter aurescens
Trehalose synthase	-	Meiothermus ruber
Trehalose synthase	-	Deinococcus geothermalis
Trehalose synthase	-	Deinococcus radiodurans
Trehalose synthase	-	Mycolicibacterium smegmatis
Trehalose synthase	-	Corynebacterium glutamicum
Trehalose synthase	-	Picrophilus torridus
Trehalose synthase	-	Thermobaculum terrenum
Trehalose synthase	-	Thermobifida fusca
Trehalose synthase	-	Thermomonospora curvata
Trehalose synthase	-	Enterobacter hormaechei
Trehalose synthase	-	Pseudomonas sp. P8005
Trehalose synthase	-	Pseudomonas stutzeri
Trehalose synthase	-	Rhodococcus opacus
Trehalose synthase	-	Mycobacterium tuberculosis
TreS	-	Thermus thermophilus
TreS	-	Paenarthrobacter aurescens
TreS	-	Meiothermus ruber
TreS	-	Enterobacter hormaechei
TreS	-	Pseudomonas sp. P8005
TreS	-	Pseudomonas stutzeri
TreS	-	Rhodococcus opacus
Tter_0330	-	Thermobaculum terrenum

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
15	-	-	Deinococcus radiodurans
25	-	-	Thermobifida fusca
25	-	-	Rhodococcus opacus
30	-	-	Deinococcus radiodurans
35	-	-	Paenarthrobacter aurescens
35	-	-	Thermomonospora curvata
35	-	-	Pseudomonas stutzeri
37	-	-	Enterobacter hormaechei
37	-	-	Pseudomonas sp. P8005
40	-	-	Deinococcus geothermalis
45	-	-	Picrophilus torridus
45	-	-	Thermobaculum terrenum
50	-	-	Thermus thermophilus
50	-	-	Meiothermus ruber
65	-	-	Thermus thermophilus

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
10	40	over 80% activity remains after 30 min	Pseudomonas sp. P8005
15	45	100% activity remains after 1 h	Rhodococcus opacus
20	35	100% activity remains after 20 min	Paenarthrobacter aurescens
40	-	50% activity remains after 28.5 h	Deinococcus radiodurans
40	-	90% activity remains after 30 min	Deinococcus radiodurans
50	-	10% activity remains after 30 min	Pseudomonas sp. P8005
50	-	50% activity remains after 9.5 h	Deinococcus radiodurans
55	-	50% activity remains after 30 min	Deinococcus radiodurans
55	-	40% activity remains after 1 h	Pseudomonas stutzeri
55	-	57% activity remains after 8 h	Deinococcus geothermalis
60	-	90% activity remains after 20 min	Picrophilus torridus
60	-	90% activity remains after 5 h	Meiothermus ruber
60	-	no activity remains after 2 h	Deinococcus radiodurans
60	-	no activity remains after 3 h	Rhodococcus opacus
65	-	88% activity remains after 30 min	Thermus thermophilus
70	-	80% activity remains after 30 min	Thermobaculum terrenum

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6	-	-	Picrophilus torridus
6	-	-	Enterobacter hormaechei
6.5	-	-	Paenarthrobacter aurescens
6.5	-	-	Meiothermus ruber
6.5	-	-	Deinococcus radiodurans
6.5	-	-	Thermobifida fusca
6.5	-	-	Thermomonospora curvata
6.5	-	-	Thermus thermophilus
7	-	-	Rhodococcus opacus
7.2	-	-	Pseudomonas sp. P8005
7.5	-	-	Thermobaculum terrenum
7.6	-	-	Deinococcus geothermalis
7.6	-	-	Deinococcus radiodurans
8.5	-	-	Pseudomonas stutzeri
9	-	-	Thermus thermophilus

General Information

General Information	Comment	Organism
evolution	phylogenetic tree	Thermus thermophilus
evolution	phylogenetic tree	Paenarthrobacter aurescens
evolution	phylogenetic tree	Meiothermus ruber
evolution	phylogenetic tree	Deinococcus geothermalis
evolution	phylogenetic tree	Deinococcus radiodurans
evolution	phylogenetic tree	Mycolicibacterium smegmatis
evolution	phylogenetic tree	Corynebacterium glutamicum
evolution	phylogenetic tree	Picrophilus torridus
evolution	phylogenetic tree	Thermobaculum terrenum
evolution	phylogenetic tree	Thermobifida fusca
evolution	phylogenetic tree	Thermomonospora curvata
evolution	phylogenetic tree	Enterobacter hormaechei
evolution	phylogenetic tree	Pseudomonas sp. P8005
evolution	phylogenetic tree	Pseudomonas stutzeri
evolution	phylogenetic tree	Rhodococcus opacus
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