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 | 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 | 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 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 | 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 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 | 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 | 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 (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 | 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 | 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 | 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 | 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 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 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 Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
5 | 8 | activity range | Rhodopseudomonas palustris |
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 |