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Literature summary for 4.2.1.112 extracted from
- Acetylene hydratase a non-redox enzyme with tungsten and iron-sulfur centers at the active site (2016), J. Biol. Inorg. Chem., 21, 29-38 .
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| high resolution crystal structure determination of the W-dependent enzyme crystallized under the exclusion of dioxygen (N2/H2 (94%/6% v/v)) at 1.26 A resolution, PDB ID 2E7Z | Syntrophotalea acetylenica |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C141S | site-directed mutagenesis | Syntrophotalea acetylenica |
| D13A | site-directed mutagenesis of catalytically important Asp13, a direct neighbor of the [4Fe-4S] coordinating Cys12, forms a close hydrogen bond of 2.41 A to the oxygen ligand of the W ion, the mutant shows significant loss of activity compared to wild-type | Syntrophotalea acetylenica |
| D13E | site-directed mutagenesis of catalytically important Asp13, a direct neighbor of the [4Fe-4S] coordinating Cys12, forms a close hydrogen bond of 2.41 A to the oxygen ligand of the W ion, the mutant shows unaltered activity compared to wild-type | Syntrophotalea acetylenica |
| I142A | site-directed mutagenesis, Ile142 is part of the hydrophobic ring that is proposed to form the substrate binding cavity at the end of the access tunnel towards the active site, its exchange against alanine results in a strong loss of activity | Syntrophotalea acetylenica |
| K48A | site-directed mutagenesis of the residue involved in electron transfer between the two cofactors, the exchange of Lys48 against alanine does not affect catalysis | Syntrophotalea acetylenica |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| cyanide | a cyanide sensitive enzyme | Syntrophotalea acetylenica |  |
| additional information | oxidation of AH with one equivalent [Fe(CN)6]3- | Syntrophotalea acetylenica |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| soluble | the enzyme activity is localized exclusively in the soluble fraction of the cell extract | Syntrophotalea acetylenica | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | in [4Fe-4S] cluster | Rhodobacter capsulatus | |
| Fe2+ | in [4Fe-4S] cluster | Rhodococcus ruber | |
| Fe2+ | in [4Fe-4S] cluster | Rhodococcus opacus | |
| Fe2+ | in [4Fe-4S] cluster | Gordonia alkanivorans | |
| Fe2+ | in [4Fe-4S] cluster | Norcadia rhodochorous | |
| Fe2+ | in [4Fe-4S] cluster | Rhodococcus sp. A1 | |
| Fe2+ | in [4Fe-4S] cluster, the enzyme contains 3.7-3.9 mol Fe/mol enzyme | Syntrophotalea acetylenica | |
| Molybdenum | a Mo-dependent active form of AH (Mo-AH) can also be obtained from Pelobacter acetylenicus | Syntrophotalea acetylenica | |
| Molybdenum | a Mo-dependent active form of AH (Mo-AH) can also be obtained from Rhodobacter capsulatus | Rhodobacter capsulatus | |
| additional information | Mo-dependent enzyme is approximately 10fold less active than the native W-dependent enzyme | Rhodobacter capsulatus | |
| additional information | the dependence of AH activity on the applied redox potential gives a midpoint potential of -340 mV. Mo-dependent enzyme is approximately 10fold less active than the native W-dependent enzyme. Attempts to insert vanadium into the enzyme's active site fail | Syntrophotalea acetylenica | |
| Ti(III) citrate | required for activity | Rhodococcus opacus | |
| Tungsten | bound with two pyranopterins | Rhodobacter capsulatus | |
| Tungsten | bound with two pyranopterins | Rhodococcus ruber | |
| Tungsten | bound with two pyranopterins | Rhodococcus opacus | |
| Tungsten | bound with two pyranopterins | Gordonia alkanivorans | |
| Tungsten | bound with two pyranopterins | Norcadia rhodochorous | |
| Tungsten | bound with two pyranopterins | Rhodococcus sp. A1 | |
| Tungsten | bound with two pyranopterins, the enzyme contains 0.4-0.5 mol W/mol enzyme | Syntrophotalea acetylenica | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetylene + H2O | Rhodobacter capsulatus | - |
acetaldehyde | - |
r | |
| acetylene + H2O | Rhodococcus ruber | - |
acetaldehyde | - |
r | |
| acetylene + H2O | Rhodococcus opacus | - |
acetaldehyde | - |
r | |
| acetylene + H2O | Gordonia alkanivorans | - |
acetaldehyde | - |
r | |
| acetylene + H2O | Syntrophotalea acetylenica | - |
acetaldehyde | - |
r | |
| acetylene + H2O | Norcadia rhodochorous | - |
acetaldehyde | - |
r | |
| acetylene + H2O | Rhodococcus sp. A1 | - |
acetaldehyde | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Gordonia alkanivorans | - |
- |
- |
| Norcadia rhodochorous | - |
- |
- |
| Rhodobacter capsulatus | - |
- |
- |
| Rhodococcus opacus | - |
- |
- |
| Rhodococcus ruber | - |
- |
- |
| Rhodococcus sp. A1 | - |
- |
- |
| Syntrophotalea acetylenica | Q71EW5 | - |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| acetaldehyde = acetylene + H2O | acetylene hydratase harbors two pyranopterins bound to tungsten, and a [4Fe-4S] cluster. Tungsten is coordinated by four dithiolene sulfur atoms, one cysteine sulfur, and one oxygen ligand. The enzyme activity requires a strong reductant suggesting (IV) as the active oxidation state. Two different types of reaction pathways have been proposed, the reaction does not involve a net electron transfer | Rhodobacter capsulatus | |
| acetaldehyde = acetylene + H2O | acetylene hydratase harbors two pyranopterins bound to tungsten, and a [4Fe-4S] cluster. Tungsten is coordinated by four dithiolene sulfur atoms, one cysteine sulfur, and one oxygen ligand. The enzyme activity requires a strong reductant suggesting (IV) as the active oxidation state. Two different types of reaction pathways have been proposed, the reaction does not involve a net electron transfer | Rhodococcus ruber | |
| acetaldehyde = acetylene + H2O | acetylene hydratase harbors two pyranopterins bound to tungsten, and a [4Fe-4S] cluster. Tungsten is coordinated by four dithiolene sulfur atoms, one cysteine sulfur, and one oxygen ligand. The enzyme activity requires a strong reductant suggesting (IV) as the active oxidation state. Two different types of reaction pathways have been proposed, the reaction does not involve a net electron transfer | Rhodococcus opacus | |
| acetaldehyde = acetylene + H2O | acetylene hydratase harbors two pyranopterins bound to tungsten, and a [4Fe-4S] cluster. Tungsten is coordinated by four dithiolene sulfur atoms, one cysteine sulfur, and one oxygen ligand. The enzyme activity requires a strong reductant suggesting (IV) as the active oxidation state. Two different types of reaction pathways have been proposed, the reaction does not involve a net electron transfer | Gordonia alkanivorans | |
| acetaldehyde = acetylene + H2O | acetylene hydratase harbors two pyranopterins bound to tungsten, and a [4Fe-4S] cluster. Tungsten is coordinated by four dithiolene sulfur atoms, one cysteine sulfur, and one oxygen ligand. The enzyme activity requires a strong reductant suggesting (IV) as the active oxidation state. Two different types of reaction pathways have been proposed, the reaction does not involve a net electron transfer | Norcadia rhodochorous | |
| acetaldehyde = acetylene + H2O | acetylene hydratase harbors two pyranopterins bound to tungsten, and a [4Fe-4S] cluster. Tungsten is coordinated by four dithiolene sulfur atoms, one cysteine sulfur, and one oxygen ligand. The enzyme activity requires a strong reductant suggesting (IV) as the active oxidation state. Two different types of reaction pathways have been proposed, the reaction does not involve a net electron transfer | Rhodococcus sp. A1 | |
| acetaldehyde = acetylene + H2O | acetylene hydratase harbors two pyranopterins bound to tungsten, and a [4Fe-4S] cluster. Tungsten is coordinated by four dithiolene sulfur atoms, one cysteine sulfur, and one oxygen ligand. The enzyme activity requires a strong reductant suggesting (IV) as the active oxidation state. Two different types of reaction pathways have been proposed, the reaction does not involve a net electron transfer. The nature of the oxygen ligand of the W center in the enzyme is crucial to formulate a reaction mechanism. Residue Asp13 is catalytically important because it activates the oxygen atom for the addition to the C-C triple bond. Representation of the five-step catalytic cycle, with Asp13 acting as a key player in the mechanism, and W binding and activating C2H2, and providing electrostatic stabilization to the transition states and intermediates | Syntrophotalea acetylenica |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| additional information | the organism grows on C2H2 as sole source of carbon and energy in the presence of dioxygen | Norcadia rhodochorous | - |
| additional information | the organism grows on C2H2 as sole source of carbon and energy in the presence of dioxygen | Rhodococcus sp. A1 | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetylene + H2O | - |
Rhodobacter capsulatus | acetaldehyde | - |
r | |
| acetylene + H2O | - |
Rhodococcus ruber | acetaldehyde | - |
r | |
| acetylene + H2O | - |
Rhodococcus opacus | acetaldehyde | - |
r | |
| acetylene + H2O | - |
Gordonia alkanivorans | acetaldehyde | - |
r | |
| acetylene + H2O | - |
Syntrophotalea acetylenica | acetaldehyde | - |
r | |
| acetylene + H2O | - |
Norcadia rhodochorous | acetaldehyde | - |
r | |
| acetylene + H2O | - |
Rhodococcus sp. A1 | acetaldehyde | - |
r | |
| additional information | the enzyme is highly specific for acetylene | Rhodobacter capsulatus | ? | - |
? | |
| additional information | the enzyme is highly specific for acetylene | Rhodococcus ruber | ? | - |
? | |
| additional information | the enzyme is highly specific for acetylene | Rhodococcus opacus | ? | - |
? | |
| additional information | the enzyme is highly specific for acetylene | Gordonia alkanivorans | ? | - |
? | |
| additional information | the enzyme is highly specific for acetylene | Syntrophotalea acetylenica | ? | - |
? | |
| additional information | the enzyme is highly specific for acetylene | Norcadia rhodochorous | ? | - |
? | |
| additional information | the enzyme is highly specific for acetylene | Rhodococcus sp. A1 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 83500, about, mass spectrometry | Syntrophotalea acetylenica |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| tungsto-bis(pyranopterin guanine dinucleotide) | harbors two pyranopterins bound to tungsten | Rhodobacter capsulatus | |
| tungsto-bis(pyranopterin guanine dinucleotide) | harbors two pyranopterins bound to tungsten | Rhodococcus ruber | |
| tungsto-bis(pyranopterin guanine dinucleotide) | harbors two pyranopterins bound to tungsten | Rhodococcus opacus | |
| tungsto-bis(pyranopterin guanine dinucleotide) | harbors two pyranopterins bound to tungsten | Gordonia alkanivorans | |
| tungsto-bis(pyranopterin guanine dinucleotide) | harbors two pyranopterins bound to tungsten | Norcadia rhodochorous | |
| tungsto-bis(pyranopterin guanine dinucleotide) | harbors two pyranopterins bound to tungsten | Rhodococcus sp. A1 | |
| tungsto-bis(pyranopterin guanine dinucleotide) | harbors two pyranopterins bound to tungsten, the enzyme contains 1.3-1.4 mol pyranopterin-guaninedinucleotide cofactor (MGD) | Syntrophotalea acetylenica | |
| [4Fe-4S] cluster | - |
Rhodobacter capsulatus | |
| [4Fe-4S] cluster | - |
Rhodococcus ruber | |
| [4Fe-4S] cluster | - |
Rhodococcus opacus | |
| [4Fe-4S] cluster | - |
Gordonia alkanivorans | |
| [4Fe-4S] cluster | - |
Norcadia rhodochorous | |
| [4Fe-4S] cluster | - |
Rhodococcus sp. A1 | |
| [4Fe-4S] cluster | low potential ferredoxin-type [4Fe-4S] cluster, the [4Fe-4S] has a midpoint potential around -410 mV | Syntrophotalea acetylenica | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the tungsten containing enzymes, it is a unique W, Fe-S enzyme and a member of the dimethyl sulfoxide reductase (DMSOR) family of enzymes. The W, Fe-S-dependent enzyme might have arosen recently as a means for microbes to take advantage of local anthropogenic sources of acetylene or it represents the relic of some ancestral biochemical process | Rhodobacter capsulatus |
| evolution | the enzyme belongs to the tungsten containing enzymes, it is a unique W, Fe-S enzyme and a member of the dimethyl sulfoxide reductase (DMSOR) family of enzymes. The W, Fe-S-dependent enzyme might have arosen recently as a means for microbes to take advantage of local anthropogenic sources of acetylene or it represents the relic of some ancestral biochemical process | Rhodococcus ruber |
| evolution | the enzyme belongs to the tungsten containing enzymes, it is a unique W, Fe-S enzyme and a member of the dimethyl sulfoxide reductase (DMSOR) family of enzymes. The W, Fe-S-dependent enzyme might have arosen recently as a means for microbes to take advantage of local anthropogenic sources of acetylene or it represents the relic of some ancestral biochemical process | Rhodococcus opacus |
| evolution | the enzyme belongs to the tungsten containing enzymes, it is a unique W, Fe-S enzyme and a member of the dimethyl sulfoxide reductase (DMSOR) family of enzymes. The W, Fe-S-dependent enzyme might have arosen recently as a means for microbes to take advantage of local anthropogenic sources of acetylene or it represents the relic of some ancestral biochemical process | Gordonia alkanivorans |
| evolution | the enzyme belongs to the tungsten containing enzymes, it is a unique W, Fe-S enzyme and a member of the dimethyl sulfoxide reductase (DMSOR) family of enzymes. The W, Fe-S-dependent enzyme might have arosen recently as a means for microbes to take advantage of local anthropogenic sources of acetylene or it represents the relic of some ancestral biochemical process | Syntrophotalea acetylenica |
| evolution | the enzyme belongs to the tungsten containing enzymes, it is a unique W, Fe-S enzyme and a member of the dimethyl sulfoxide reductase (DMSOR) family of enzymes. The W, Fe-S-dependent enzyme might have arosen recently as a means for microbes to take advantage of local anthropogenic sources of acetylene or it represents the relic of some ancestral biochemical process | Norcadia rhodochorous |
| evolution | the enzyme belongs to the tungsten containing enzymes, it is a unique W, Fe-S enzyme and a member of the dimethyl sulfoxide reductase (DMSOR) family of enzymes. The W, Fe-S-dependent enzyme might have arosen recently as a means for microbes to take advantage of local anthropogenic sources of acetylene or it represents the relic of some ancestral biochemical process | Rhodococcus sp. A1 |
| additional information | Mo-dependent enzyme is approximately 10fold less active than the native W-dependent enzyme | Rhodobacter capsulatus |
| additional information | Mo-dependent enzyme is approximately 10fold less active than the native W-dependent enzyme. Active site cavity structure of Pelobacter acetylenicus acetylene hydratase, overview. A C2H2 molecule docked computationally at the AH active site gives an excellent fit in the pocket of the hydrophobic ring with its carbon atoms positioned directly above the oxygen ligand and the carboxylic acid group of Asp13 | Syntrophotalea acetylenica |
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