Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
tetrahymanol synthase (Ths) is found in a variety of bacterial genomes, including aerobic methanotrophs, nitrite-oxidizers, and sulfate-reducers, and in a subset of aquatic and terrestrial metagenomes. The potential to produce tetrahymanol is more widespread in the bacterial domain than previously thought. Ths is not encoded in any eukaryotic genomes, nor is it homologous to eukaryotic squalene-tetrahymanol cyclase (EC 4.2.1.123), which catalyzes the cyclization of squalene directly to tetrahymanol
evolution
tetrahymanol synthase (Ths) is found in a variety of bacterial genomes, including aerobic methanotrophs, nitrite-oxidizers, and sulfate-reducers, and in a subset of aquatic and terrestrial metagenomes. The potential to produce tetrahymanol is more widespread in the bacterial domain than previously thought. Ths is not encoded in any eukaryotic genomes, nor is it homologous to eukaryotic squalene-tetrahymanol cyclase (EC 4.2.1.123), which catalyzes the cyclization of squalene directly to tetrahymanol
evolution
-
tetrahymanol synthase (Ths) is found in a variety of bacterial genomes, including aerobic methanotrophs, nitrite-oxidizers, and sulfate-reducers, and in a subset of aquatic and terrestrial metagenomes. The potential to produce tetrahymanol is more widespread in the bacterial domain than previously thought. Ths is not encoded in any eukaryotic genomes, nor is it homologous to eukaryotic squalene-tetrahymanol cyclase (EC 4.2.1.123), which catalyzes the cyclization of squalene directly to tetrahymanol
-
evolution
-
tetrahymanol synthase (Ths) is found in a variety of bacterial genomes, including aerobic methanotrophs, nitrite-oxidizers, and sulfate-reducers, and in a subset of aquatic and terrestrial metagenomes. The potential to produce tetrahymanol is more widespread in the bacterial domain than previously thought. Ths is not encoded in any eukaryotic genomes, nor is it homologous to eukaryotic squalene-tetrahymanol cyclase (EC 4.2.1.123), which catalyzes the cyclization of squalene directly to tetrahymanol
-
physiological function
tetrahymanol, whose catalysis is synthesized by tetrahymanol synthase, is a polycyclic triterpenoid lipid. Enzyme tetrahymanol synthase (Ths) functions on hopenes rather than squalene, it first demethylates squalene to form C23-norsqualene, which is then converted to a demethyl derivative of tetrahymanol by squalene-hopene cyclase (Shc, EC 5.4.99.17). This pathway requires the addition of a methyl group at C-23 to form tetrahymanol. Enzyme Shc cyclizes squalene to diploptene, and Ths then expands the E ring to form tetrahymanol, overview
physiological function
tetrahymanol, whose catalysis is synthesized by tetrahymanol synthase, is a polycyclic triterpenoid lipid. Enzyme tetrahymanol synthase (Ths) functions on hopenes rather than squalene, it first demethylates squalene to form C23-norsqualene, which is then converted to a demethyl derivative of tetrahymanol by squalene-hopene cyclase (Shc, EC 5.4.99.17). This pathway requires the addition of a methyl group at C-23 to form tetrahymanol. Enzyme Shc cyclizes squalene to diploptene, and Ths then expands the E ring to form tetrahymanol, overview
physiological function
-
tetrahymanol, whose catalysis is synthesized by tetrahymanol synthase, is a polycyclic triterpenoid lipid. Enzyme tetrahymanol synthase (Ths) functions on hopenes rather than squalene, it first demethylates squalene to form C23-norsqualene, which is then converted to a demethyl derivative of tetrahymanol by squalene-hopene cyclase (Shc, EC 5.4.99.17). This pathway requires the addition of a methyl group at C-23 to form tetrahymanol. Enzyme Shc cyclizes squalene to diploptene, and Ths then expands the E ring to form tetrahymanol, overview
-
physiological function
-
tetrahymanol, whose catalysis is synthesized by tetrahymanol synthase, is a polycyclic triterpenoid lipid. Enzyme tetrahymanol synthase (Ths) functions on hopenes rather than squalene, it first demethylates squalene to form C23-norsqualene, which is then converted to a demethyl derivative of tetrahymanol by squalene-hopene cyclase (Shc, EC 5.4.99.17). This pathway requires the addition of a methyl group at C-23 to form tetrahymanol. Enzyme Shc cyclizes squalene to diploptene, and Ths then expands the E ring to form tetrahymanol, overview
-
additional information
hopanoids, tetrahymanol, and sterol structures observed in Methylomicrobium alcaliphilum strain 20Z, overview
additional information
-
hopanoids, tetrahymanol, and sterol structures observed in Methylomicrobium alcaliphilum strain 20Z, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Banta, A.B.; Wei, J.H.; Welander, P.V.
A distinct pathway for tetrahymanol synthesis in bacteria
Proc. Natl. Acad. Sci. USA
112
13478-13483
2015
Rhodopseudomonas palustris (B3QED8), Methylotuvimicrobium alcaliphilum (G4SZH3), Rhodopseudomonas palustris TIE-1 (B3QED8), Methylotuvimicrobium alcaliphilum DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z (G4SZH3)
brenda
Enzyme Nomenclature
4.2.1.B28 tetrahymanol synthase (hopene)
top
