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Literature summary extracted from
- Evolution of a new enzyme for carbon disulphide conversion by an acidothermophilic archaeon (2011), Nature, 478, 412-416.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.13.1.5 | - |
Acidianus sp. |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.13.1.5 | hanging-drop vapour diffusion method, crystal structures are determined from heterologously expressed selenomethionine-labelled protein at 2.6 A resolution and native purified protein at 2.4 A resolution | Acidianus sp. |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.13.1.5 | F77A | Km-value for carbon disulfide is 1.5fold fold lower than wild-type value, Vmax is 1.4fold higher than wild-type value | Acidianus sp. |
| 3.13.1.5 | F96S | Km-value for carbon disulfide is similar to wild-type value, Vmax is 2.4fold higher than wild-type value | Acidianus sp. |
| 3.13.1.5 | G199stop | Km-value for carbon disulfide is 1.5fold fold lower than wild-type value, Vmax is 1.2fold higher than wild-type value | Acidianus sp. |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.13.1.5 | 0.081 | - |
carbon disulfide | pH and temperature not specified in the publication, mutant enzyme G199stop | Acidianus sp. |  |
| 3.13.1.5 | 0.085 | - |
carbon disulfide | pH and temperature not specified in the publication, mutant enzyme F77A | Acidianus sp. | |
| 3.13.1.5 | 0.13 | - |
carbon disulfide | pH and temperature not specified in the publication, wild-type enzyme | Acidianus sp. | |
| 3.13.1.5 | 0.136 | - |
carbon disulfide | pH and temperature not specified in the publication, mutant enzyme F96S | Acidianus sp. | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.13.1.5 | Zn2+ | the active site of native CS2 lyase contains a zinc ion coordinated by Cys35, His88, Cys91 and a solvent molecule | Acidianus sp. | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.13.1.5 | 24000 | - |
x * 24000, in the CS2 hydrolase two octameric rings form a hexadecamer by interlocking at right angles to each other, forming a catenane structure, MALDI-TOF MS | Acidianus sp. |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.13.1.5 | carbon disulfide + 2 H2O | Acidianus sp. | under anaerobic or aerobic conditions, cell extracts of Acidianus A1-3 convert CS2 to H2S, with COS as the intermediate | CO2 + 2 hydrogen sulfide | - |
? | |
| 3.13.1.5 | carbon disulfide + 2 H2O | Acidianus sp. A1-3 | under anaerobic or aerobic conditions, cell extracts of Acidianus A1-3 convert CS2 to H2S, with COS as the intermediate | CO2 + 2 hydrogen sulfide | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.13.1.5 | Acidianus sp. | - |
a hyperthermophilic strain, which is isolated from the fumarolic, ancient sauna building at the Solfatara volcano Naples, Italy | - |
| 3.13.1.5 | Acidianus sp. A1-3 | - |
a hyperthermophilic strain, which is isolated from the fumarolic, ancient sauna building at the Solfatara volcano Naples, Italy | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.13.1.5 | - |
Acidianus sp. |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 3.13.1.5 | carbon disulfide + 2 H2O = CO2 + 2 hydrogen sulfide | overall reaction | Acidianus sp. |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.13.1.5 | carbon disulfide + 2 H2O | under anaerobic or aerobic conditions, cell extracts of Acidianus A1-3 convert CS2 to H2S, with COS as the intermediate | Acidianus sp. | CO2 + 2 hydrogen sulfide | - |
? | |
| 3.13.1.5 | carbon disulfide + 2 H2O | carbon disulfide is converted to hydrogen sulfide, with carbonyl sulfide as the intermediate. The carbon disulfide hydrolase converts the intermediate COS with a higher affinity and kcat than for carbon disulfide. The mechanism of the reaction is closely related to that of beta-carbonic anhydrases. However CO2 is not a substrate for carbon disulfide hydrolase. A specificity filter is built into the active site entrance | Acidianus sp. | CO2 + 2 hydrogen sulfide | - |
? | |
| 3.13.1.5 | carbon disulfide + 2 H2O | under anaerobic or aerobic conditions, cell extracts of Acidianus A1-3 convert CS2 to H2S, with COS as the intermediate | Acidianus sp. A1-3 | CO2 + 2 hydrogen sulfide | - |
? | |
| 3.13.1.5 | carbon disulfide + 2 H2O | carbon disulfide is converted to hydrogen sulfide, with carbonyl sulfide as the intermediate. The carbon disulfide hydrolase converts the intermediate COS with a higher affinity and kcat than for carbon disulfide. The mechanism of the reaction is closely related to that of beta-carbonic anhydrases. However CO2 is not a substrate for carbon disulfide hydrolase. A specificity filter is built into the active site entrance | Acidianus sp. A1-3 | CO2 + 2 hydrogen sulfide | - |
? | |
| 3.13.1.5 | carbonyl sulfide + H2O | carbon disulfide is converted to hydrogen sulfide, with COS as the intermediate. The carbon disulfide hydrolase converts the intermediate carbonyl sulfide with a higher affinity and kcat than for carbon disulfide | Acidianus sp. | CO2 + hydrogen sulfide | - |
? | |
| 3.13.1.5 | carbonyl sulfide + H2O | carbon disulfide is converted to hydrogen sulfide, with COS as the intermediate. The carbon disulfide hydrolase converts the intermediate carbonyl sulfide with a higher affinity and kcat than for carbon disulfide | Acidianus sp. A1-3 | CO2 + hydrogen sulfide | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.13.1.5 | ? | x * 24000, in the CS2 hydrolase two octameric rings form a hexadecamer by interlocking at right angles to each other, forming a catenane structure, MALDI-TOF MS | Acidianus sp. |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.13.1.5 | carbon disulfide hydrolase | misleading | Acidianus sp. |
| 3.13.1.5 | CS2 hydrolase | misleading | Acidianus sp. |
| 3.13.1.5 | CS2-converting enzyme | - |
Acidianus sp. |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.13.1.5 | 952 | - |
carbon disulfide | pH and temperature not specified in the publication | Acidianus sp. | |
| 3.13.1.5 | 1800 | - |
carbonyl sulfide | pH and temperature not specified in the publication | Acidianus sp. | |
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