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Information on EC 4.2.1.B28 - tetrahymanol synthase (hopene)
for references in articles please use BRENDA:EC4.2.1.B28
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Please check here for current data: EC unknown
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preliminary BRENDA-supplied EC number
EC Tree 4 Lyases
4.2 Carbon-oxygen lyases
4.2.1 Hydro-lyases
4.2.1.B28 tetrahymanol synthase (hopene)
The enzyme appears in viruses and cellular organisms
- 4.2.1.B28
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isobaric
-
orbitrap
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10-plex
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odour
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8-plexing
-
tmt-induced
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2,5-dihydro-2,4,5-trimethylthiazoline
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tmt-based
showSynonyms
MEALZ_1626, Rpal_0860, Ths, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
MEALZ_1626
Rpal_0860
Ths
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
tetrahymanol = hopene + H2O
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-
-
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SYSTEMATIC NAME
IUBMB Comments
hopene hydro-lyase (tetrahymanol forming)
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
hopene + H2O
tetrahymanol
B3QED8
Substrates: -
Products: -
Products: -
?
additional information
?
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Substrates: the enzyme catalyzes steps in the synthesis of tetrahymanol from hopene
Products: -
Products: -
?
additional information
?
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Methylotuvimicrobium alcaliphilum DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z
Substrates: the enzyme catalyzes steps in the synthesis of tetrahymanol from hopene
Products: -
Products: -
?
additional information
?
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B3QED8
Substrates: the enzyme catalyzes steps in the synthesis of tetrahymanol from hopene
Products: -
Products: -
?
additional information
?
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B3QED8
Substrates: the enzyme catalyzes steps in the synthesis of tetrahymanol from hopene
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
Substrates: the enzyme catalyzes steps in the synthesis of tetrahymanol from hopene
Products: -
Products: -
?
additional information
?
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Methylotuvimicrobium alcaliphilum DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z
Substrates: the enzyme catalyzes steps in the synthesis of tetrahymanol from hopene
Products: -
Products: -
?
additional information
?
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B3QED8
Substrates: the enzyme catalyzes steps in the synthesis of tetrahymanol from hopene
Products: -
Products: -
?
additional information
?
-
B3QED8
Substrates: the enzyme catalyzes steps in the synthesis of tetrahymanol from hopene
Products: -
Products: -
?
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
evolution
B3QED8
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
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evolution
Methylotuvimicrobium alcaliphilum DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z
-
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
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physiological function
B3QED8
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
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physiological function
Methylotuvimicrobium alcaliphilum DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z
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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
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additional information
hopanoids, tetrahymanol, and sterol structures observed in Methylomicrobium alcaliphilum strain 20Z, overview
additional information
Methylotuvimicrobium alcaliphilum DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z
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hopanoids, tetrahymanol, and sterol structures observed in Methylomicrobium alcaliphilum strain 20Z, overview
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). G4SZH3_META2
Methylotuvimicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z)
614
0
71091
TrEMBL
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of a DELTAths deletion mutant, functional complementation by expression of gene Rpal_0860, encoding wild-type Ths, and gene shc from Methylomicrobium alcaliphilum strain 20Z
additional information
Methylotuvimicrobium alcaliphilum DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z
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construction of a DELTAths deletion mutant, functional complementation by expression of gene Rpal_0860, encoding wild-type Ths, and gene shc from Methylomicrobium alcaliphilum strain 20Z
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene MEALZ_1626 or rhs, sequence comparisons and phylogenetic analysis, phylogenetics and metagenomics, recombinant expression in Methylococcus capsulatus Bath strains
gene Rpal_0860 or ths, sequence comparisons and phylogenetic analysis, phylogenetics and metagenomics, recombinant expression in and functional complementation of DELTAths deletion mutant strain of Methylomicrobium alcaliphilum
B3QED8
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Methylotuvimicrobium alcaliphilum (G4SZH3), Methylotuvimicrobium alcaliphilum DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z (G4SZH3), Rhodopseudomonas palustris (B3QED8), Rhodopseudomonas palustris TIE-1 (B3QED8)
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EXTERNAL LINKS (specific for EC-Number 4.2.1.B28)
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Release 2026.1 (March 2026)
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