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Literature summary for 4.2.1.129 extracted from
- Squalene-hopene cyclases (2011), Appl. Environ. Microbiol., 77, 3905-3915.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene shc or hpnF, part of a gene cluster containing four open reading frames, hpnCDEF | Bradyrhizobium japonicum |
| gene shc or hpnF, part of a gene cluster containing six open reading frames, hpnABCDEF | Zymomonas mobilis |
| gene shc, DNA and amino acid sequence determination, expression in Escherichia coli | Alicyclobacillus acidocaldarius |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C435S/D374I/D374V/H451F | site-directed mutagenesis, inactive mutant | Alicyclobacillus acidocaldarius |
| D376E | site-directed mutagenesis, inactive mutant | Alicyclobacillus acidocaldarius |
| D377C/D377N/Y612A | site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview | Alicyclobacillus acidocaldarius |
| D377E/D376Q/D376R/D377R/E45K/W406V/W417A/D377C | site-directed mutagenesis, inactive mutant | Alicyclobacillus acidocaldarius |
| F365A | site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview | Alicyclobacillus acidocaldarius |
| F601A | site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview | Alicyclobacillus acidocaldarius |
| F605A | site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview | Alicyclobacillus acidocaldarius |
| I261A | site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview | Alicyclobacillus acidocaldarius |
| Q262G/Q262A/P263G/P263A | site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview | Alicyclobacillus acidocaldarius |
| V380E | site-directed mutagenesis, inactive mutant | Alicyclobacillus acidocaldarius |
| V381A/D376C | site-directed mutagenesis, inactive mutant | Alicyclobacillus acidocaldarius |
| W169F/W169H/W489A/F605K | site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview | Alicyclobacillus acidocaldarius |
| Y420A | site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview | Alicyclobacillus acidocaldarius |
| Y606A/W23V/W495V/W522V/W533A/W591L/W78S/E35Q/E197Q/D530N/T378A | site-directed mutagenesis, the mutant shows the same product pattern and activity as the wild-type | Alicyclobacillus acidocaldarius |
| Y609A/Y612A/L607K | site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview | Alicyclobacillus acidocaldarius |
| Y609F | site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview | Alicyclobacillus acidocaldarius |
| Y609F | site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview. The phenotype of Y609F mutein is contrarily described in two publications | Alicyclobacillus acidocaldarius |
| Y612F/D376E/D376G/D377E/D377G/D377Q/E45A/E45D/F365W/T41A/E93A/R127Q/W133A/Y267A/F434A/F437A/W258L/D350N/D421N/D442N/H451R/D447N/D377N/D313N/E535Q/D374E | site-directed mutagenesis, the mutant shows the same product pattern as the wild-type with less enzyme activity | Alicyclobacillus acidocaldarius |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate | i.e. CHAPS, almost complete inhibition | Methylococcus capsulatus |  |
| additional information | different glucopyranosides inhibit this enzyme more or less completely; no inhibition by Triton X-100 and Tween 80 | Methylococcus capsulatus | |
| additional information | the enzyme is inhibited by detergents | Rhodopseudomonas palustris | |
| sodium-taurodeoxycholate | almost complete inhibition | Methylococcus capsulatus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.003 | 0.016 | squalene | pH 6.0, 60°C | Alicyclobacillus acidocaldarius | |
| 0.018 | - |
squalene | pH 7.0, 30°C | Tetrahymena thermophila | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | - |
Rhodopseudomonas palustris | 16020 | - |
| membrane | - |
Methylococcus capsulatus | 16020 | - |
| plasma membrane | SHC in vivo is a membrane-associated protein and can be solubilized from cell extracts by nonionic detergents, such as Triton X-100 or octylthioglucopyranoside. The enzyme is attached to the inner side of the cytoplasmic membrane by interactions of hydrophobic residues with the phospholipids. The membrane-binding part of the enzyme is a nonpolar region that is encircled by positive-charged amino acids enforcing the anchoring of the enzyme to the negatively charged surface of the phospholipid membrane | Alicyclobacillus acidocaldarius | 5886 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 71600 | - |
2 * 71600, about, sequence calculation | Alicyclobacillus acidocaldarius |
| 71600 | - |
x * 71600, about, sequence calculation | Tetrahymena thermophila |
| 72300 | - |
x * 72300, about, sequence calculation | Rhodopseudomonas palustris |
| 74100 | - |
x * 74100, about, sequence calculation | Streptomyces peucetius |
| 74100 | - |
x * 74100, about, sequence calculation | Zymomonas mobilis |
| 74100 | - |
x * 74100, about, sequence calculation | Methylococcus capsulatus |
| 76300 | - |
x * 76300, about, sequence calculation | Bradyrhizobium japonicum |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Alicyclobacillus acidocaldarius | product pattern of alternative substrates, overview | ? | - |
? | |
| squalene + H2O | Bradyrhizobium japonicum | - |
hopan-22-ol | - |
? | |
| squalene + H2O | Rhodopseudomonas palustris | - |
hopan-22-ol | - |
? | |
| squalene + H2O | Streptomyces peucetius | - |
hopan-22-ol | - |
? | |
| squalene + H2O | Zymomonas mobilis | - |
hopan-22-ol | - |
? | |
| squalene + H2O | Methylococcus capsulatus | - |
hopan-22-ol | - |
? | |
| squalene + H2O | Tetrahymena thermophila | - |
hopan-22-ol | - |
? | |
| squalene + H2O | Alicyclobacillus acidocaldarius | - |
hopan-22-ol | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Alicyclobacillus acidocaldarius | P33247 | formerly Bacillus acidocaldarius, gene shc | - |
| Bradyrhizobium japonicum | - |
gene shc or hpnF | - |
| Methylococcus capsulatus | - |
- |
- |
| no activity in Escherichia coli | - |
- |
- |
| Rhodopseudomonas palustris | - |
- |
- |
| Streptomyces peucetius | - |
- |
- |
| Tetrahymena thermophila | - |
- |
- |
| Zymomonas mobilis | - |
gene shc or hpnF | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native and/or recombinant enzyme, SHC in vivo is a membrane-associated protein and can be solubilized from cell extracts by nonionic detergents, such as Triton X-100 or octylthioglucopyranoside | Alicyclobacillus acidocaldarius |
| the native enzyme can be solubilized from membranes by Triton X-100 and Tween 80 without loss of activity, but ionic detergents, such as 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS), sodium-taurodeoxycolate, and different glucopyranosides, inhibit this enzyme more or less completely | Methylococcus capsulatus |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| hopan-22-ol = squalene + H2O | overall mechanism of the polycyclization reaction of SHCs and structures of squalene cyclization products, overview | Bradyrhizobium japonicum | |
| hopan-22-ol = squalene + H2O | overall mechanism of the polycyclization reaction of SHCs and structures of squalene cyclization products, overview | Rhodopseudomonas palustris | |
| hopan-22-ol = squalene + H2O | overall mechanism of the polycyclization reaction of SHCs and structures of squalene cyclization products, overview | Streptomyces peucetius | |
| hopan-22-ol = squalene + H2O | overall mechanism of the polycyclization reaction of SHCs and structures of squalene cyclization products, overview | Zymomonas mobilis | |
| hopan-22-ol = squalene + H2O | overall mechanism of the polycyclization reaction of SHCs and structures of squalene cyclization products, overview | Methylococcus capsulatus | |
| hopan-22-ol = squalene + H2O | overall mechanism of the polycyclization reaction of SHCs and structures of squalene cyclization products, overview | Tetrahymena thermophila | |
| hopan-22-ol = squalene + H2O | overall mechanism of the polycyclization reaction of SHCs and structures of squalene cyclization products, overview | Alicyclobacillus acidocaldarius |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | substrate specificity, overview | Alicyclobacillus acidocaldarius | ? | - |
? | |
| additional information | product pattern of alternative substrates, overview | Alicyclobacillus acidocaldarius | ? | - |
? | |
| squalene + H2O | - |
Bradyrhizobium japonicum | hopan-22-ol | - |
? | |
| squalene + H2O | - |
Rhodopseudomonas palustris | hopan-22-ol | - |
? | |
| squalene + H2O | - |
Streptomyces peucetius | hopan-22-ol | - |
? | |
| squalene + H2O | - |
Zymomonas mobilis | hopan-22-ol | - |
? | |
| squalene + H2O | - |
Methylococcus capsulatus | hopan-22-ol | - |
? | |
| squalene + H2O | - |
Tetrahymena thermophila | hopan-22-ol | - |
? | |
| squalene + H2O | - |
Alicyclobacillus acidocaldarius | hopan-22-ol | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 71600, about, sequence calculation | Tetrahymena thermophila |
| ? | x * 72300, about, sequence calculation | Rhodopseudomonas palustris |
| ? | x * 74100, about, sequence calculation | Streptomyces peucetius |
| ? | x * 74100, about, sequence calculation | Zymomonas mobilis |
| ? | x * 74100, about, sequence calculation | Methylococcus capsulatus |
| ? | x * 76300, about, sequence calculation | Bradyrhizobium japonicum |
| homodimer | 2 * 71600, about, sequence calculation | Alicyclobacillus acidocaldarius |
| More | each subunit consists of alpha-helical domains that build up a dumbbell-shaped structure. The first domain consists of a regular (alpha/alpha)6 barrel structure, whereas the second domain shows an alpha-barrel structure in a less periodic manner | Alicyclobacillus acidocaldarius |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| SHC | - |
Bradyrhizobium japonicum |
| SHC | - |
Rhodopseudomonas palustris |
| SHC | - |
Streptomyces peucetius |
| SHC | - |
Zymomonas mobilis |
| SHC | - |
Methylococcus capsulatus |
| SHC | - |
Tetrahymena thermophila |
| SHC | - |
Alicyclobacillus acidocaldarius |
| squalene-hopene cyclase | - |
Bradyrhizobium japonicum |
| squalene-hopene cyclase | - |
Rhodopseudomonas palustris |
| squalene-hopene cyclase | - |
Streptomyces peucetius |
| squalene-hopene cyclase | - |
Zymomonas mobilis |
| squalene-hopene cyclase | - |
Methylococcus capsulatus |
| squalene-hopene cyclase | - |
Tetrahymena thermophila |
| squalene-hopene cyclase | - |
Alicyclobacillus acidocaldarius |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 28 | - |
- |
Bradyrhizobium japonicum |
| 30 | - |
- |
Rhodopseudomonas palustris |
| 30 | - |
- |
Zymomonas mobilis |
| 30 | - |
- |
Tetrahymena thermophila |
| 35 | - |
- |
Streptomyces peucetius |
| 40 | - |
- |
Methylococcus capsulatus |
| 60 | - |
- |
Alicyclobacillus acidocaldarius |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
- |
Zymomonas mobilis |
| 6 | - |
- |
Alicyclobacillus acidocaldarius |
| 6.5 | - |
- |
Bradyrhizobium japonicum |
| 6.5 | - |
- |
Rhodopseudomonas palustris |
| 6.8 | - |
- |
Streptomyces peucetius |
| 6.8 | - |
- |
Methylococcus capsulatus |
| 7 | - |
- |
Tetrahymena thermophila |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 8 | activity range | Rhodopseudomonas palustris |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | enzyme distribution in the different taxa, overview | Bradyrhizobium japonicum |
| evolution | enzyme distribution in the different taxa, overview | Rhodopseudomonas palustris |
| evolution | enzyme distribution in the different taxa, overview | Streptomyces peucetius |
| evolution | enzyme distribution in the different taxa, overview | Zymomonas mobilis |
| evolution | enzyme distribution in the different taxa, overview | Methylococcus capsulatus |
| evolution | enzyme distribution in the different taxa, overview | Tetrahymena thermophila |
| evolution | enzyme distribution in the different taxa, overview | Alicyclobacillus acidocaldarius |
| metabolism | the enzyme converts squalene to hopanol, EC 4.2.1.129 as well as to tetrahymanol, EC 4.2.1.123, but not to hopene, EC 5.4.99.17, pathway overview | Tetrahymena thermophila |
| metabolism | the enzyme converts squalene to hopanol, EC 4.2.1.129, and to hopene, EC 5.4.99.17, but not to tetrahymanol, EC 4.2.1.123, pathway overview | Alicyclobacillus acidocaldarius |
| metabolism | the enzyme converts squalene to hopanol, EC 4.2.1.129, but not to tetrahymanol, EC 4.2.1.123, and not to hopene, EC 5.4.99.17, pathway overview | Methylococcus capsulatus |
| metabolism | the enzyme converts squalene to hopanol, EC 4.2.1.129, but not to tetrahymanol, EC 4.2.1.123, pathway overview | Rhodopseudomonas palustris |
| metabolism | the enzyme converts squalene to hopanol, pathway overview | Streptomyces peucetius |
| metabolism | the enzyme converts squalene to hopanol, pathway overview | Zymomonas mobilis |
| metabolism | the enzyme converts squalene to tetrahymanol, EC 4.2.1.123, to hopene, EC 5.4.99.17, and to hopanol, EC 4.2.1.129, pathway overview | Bradyrhizobium japonicum |
| additional information | structure-function relationships of SHCs, active site structure, overview | Bradyrhizobium japonicum |
| additional information | structure-function relationships of SHCs, active site structure, overview | Rhodopseudomonas palustris |
| additional information | structure-function relationships of SHCs, active site structure, overview | Streptomyces peucetius |
| additional information | structure-function relationships of SHCs, active site structure, overview | Zymomonas mobilis |
| additional information | structure-function relationships of SHCs, active site structure, overview | Methylococcus capsulatus |
| additional information | structure-function relationships of SHCs, active site structure, overview | Tetrahymena thermophila |
| additional information | structure-function relationships of SHCs, active site structure, overview. A protruding part in the center of the nonpolar region contains a lipophilic channel and directs the substrate to the active-site cavity inside the protein. The channel and cavity are separated by a narrow constriction buildup of four amino acids, D376, F166, C435, and F434, that appear to block access to the active site. Residues C435 and F434 are part of a loop that seems to be flexible enough to permit passage of the substrate and the product | Alicyclobacillus acidocaldarius |
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