Any feedback?
Literature summary for 4.1.99.5 extracted from
- Oxygen-independent alkane formation by non-heme iron-dependent cyanobacterial aldehyde decarbonylase: investigation of kinetics and requirement for an external electron donor (2011), Biochemistry, 50, 10743-10750.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of N-terminally His-tagged enzyme in Escherichia coli | Synechococcus sp. |
| expression of N-terminally His-tagged enzyme in Escherichia coli | Synechocystis sp. |
| expression of N-terminally His-tagged enzyme in Escherichia coli | Prochlorococcus marinus |
| expression of N-terminally His-tagged enzyme in Escherichia coli | Nostoc punctiforme |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| ethyl acetate | - |
Nostoc punctiforme |  |
| ethyl acetate | - |
Prochlorococcus marinus | |
| ethyl acetate | - |
Synechococcus sp. | |
| ethyl acetate | - |
Synechocystis sp. | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Nostoc punctiforme | - |
- |
- |
| Prochlorococcus marinus | - |
- |
- |
| Prochlorococcus marinus MIT9313 | - |
- |
- |
| Synechococcus sp. | - |
- |
- |
| Synechocystis sp. | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+ | mechanistic proposal for the oxygen-independent formation of alkanes by the enzyme. In this mechanism the external reducing system functions catalytically to generate a reactive ketyl radical anion and facilitate carbon-carbon bond cleavage | Synechococcus sp. | |
| octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+ | mechanistic proposal for the oxygen-independent formation of alkanes by the enzyme. In this mechanism the external reducing system functions catalytically to generate a reactive ketyl radical anion and facilitate carbon-carbon bond cleavage | Synechocystis sp. | |
| octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+ | mechanistic proposal for the oxygen-independent formation of alkanes by the enzyme. In this mechanism the external reducing system functions catalytically to generate a reactive ketyl radical anion and facilitate carbon-carbon bond cleavage | Prochlorococcus marinus | |
| octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+ | mechanistic proposal for the oxygen-independent formation of alkanes by the enzyme. In this mechanism the external reducing system functions catalytically to generate a reactive ketyl radical anion and facilitate carbon-carbon bond cleavage | Nostoc punctiforme |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| heptanal + O2 + 2 NADH + 2 H+ | with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase | Synechococcus sp. | hexane + formate + H2O + 2 NAD+ | GC-MS poduct analysis | ? | |
| heptanal + O2 + 2 NADH + 2 H+ | with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase | Synechocystis sp. | hexane + formate + H2O + 2 NAD+ | GC-MS poduct analysis | ? | |
| heptanal + O2 + 2 NADH + 2 H+ | with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase | Prochlorococcus marinus | hexane + formate + H2O + 2 NAD+ | GC-MS poduct analysis | ? | |
| heptanal + O2 + 2 NADH + 2 H+ | with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase | Nostoc punctiforme | hexane + formate + H2O + 2 NAD+ | GC-MS poduct analysis | ? | |
| heptanal + O2 + 2 NADH + 2 H+ | with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase | Prochlorococcus marinus MIT9313 | hexane + formate + H2O + 2 NAD+ | GC-MS poduct analysis | ? | |
| additional information | the enzyme catalyzes the unusual hydrolysis of aldehydes to produce alkanes and formate. The reaction requires an external reducing system but does not require oxygen. The enzyme catalyzes aldehyde decarbonylation at a much faster rate under anaerobic conditions, and the oxygen in formate derives from water. Eventhough an oxygen-dependent mechanism may operate in cAD, the oxygen-independent decarbonylation of aldehydes is a general feature of these enzymes | Synechococcus sp. | ? | - |
? | |
| additional information | the enzyme catalyzes the unusual hydrolysis of aldehydes to produce alkanes and formate. The reaction requires an external reducing system but does not require oxygen. The enzyme catalyzes aldehyde decarbonylation at a much faster rate under anaerobic conditions, and the oxygen in formate derives from water. Eventhough an oxygen-dependent mechanism may operate in cAD, the oxygen-independent decarbonylation of aldehydes is a general feature of these enzymes | Synechocystis sp. | ? | - |
? | |
| additional information | the enzyme catalyzes the unusual hydrolysis of aldehydes to produce alkanes and formate. The reaction requires an external reducing system but does not require oxygen. The enzyme catalyzes aldehyde decarbonylation at a much faster rate under anaerobic conditions, and the oxygen in formate derives from water. Eventhough an oxygen-dependent mechanism may operate in cAD, the oxygen-independent decarbonylation of aldehydes is a general feature of these enzymes | Prochlorococcus marinus | ? | - |
? | |
| additional information | the enzyme catalyzes the unusual hydrolysis of aldehydes to produce alkanes and formate. The reaction requires an external reducing system but does not require oxygen. The enzyme catalyzes aldehyde decarbonylation at a much faster rate under anaerobic conditions, and the oxygen in formate derives from water. Eventhough an oxygen-dependent mechanism may operate in cAD, the oxygen-independent decarbonylation of aldehydes is a general feature of these enzymes | Nostoc punctiforme | ? | - |
? | |
| additional information | the enzyme catalyzes the unusual hydrolysis of aldehydes to produce alkanes and formate. The reaction requires an external reducing system but does not require oxygen. The enzyme catalyzes aldehyde decarbonylation at a much faster rate under anaerobic conditions, and the oxygen in formate derives from water. Eventhough an oxygen-dependent mechanism may operate in cAD, the oxygen-independent decarbonylation of aldehydes is a general feature of these enzymes | Prochlorococcus marinus MIT9313 | ? | - |
? | |
| octadecanal + O2 + 2 NADH + 2 H+ | with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase | Synechococcus sp. | heptadecane + formate + H2O + 2 NAD+ | GC-MS poduct analysis | ? | |
| octadecanal + O2 + 2 NADH + 2 H+ | with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase | Synechocystis sp. | heptadecane + formate + H2O + 2 NAD+ | GC-MS poduct analysis | ? | |
| octadecanal + O2 + 2 NADH + 2 H+ | with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase | Prochlorococcus marinus | heptadecane + formate + H2O + 2 NAD+ | GC-MS poduct analysis | ? | |
| octadecanal + O2 + 2 NADH + 2 H+ | with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase | Nostoc punctiforme | heptadecane + formate + H2O + 2 NAD+ | GC-MS poduct analysis | ? | |
| octadecanal + O2 + 2 NADH + 2 H+ | with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase | Prochlorococcus marinus MIT9313 | heptadecane + formate + H2O + 2 NAD+ | GC-MS poduct analysis | ? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CAD | - |
Synechococcus sp. |
| CAD | - |
Synechocystis sp. |
| CAD | - |
Prochlorococcus marinus |
| CAD | - |
Nostoc punctiforme |
| cyanobacterial aldehyde decarbonylase | - |
Synechococcus sp. |
| cyanobacterial aldehyde decarbonylase | - |
Synechocystis sp. |
| cyanobacterial aldehyde decarbonylase | - |
Prochlorococcus marinus |
| cyanobacterial aldehyde decarbonylase | - |
Nostoc punctiforme |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Synechococcus sp. |
| 37 | - |
assay at | Synechocystis sp. |
| 37 | - |
assay at | Prochlorococcus marinus |
| 37 | - |
assay at | Nostoc punctiforme |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
assay at | Synechococcus sp. |
| 7.2 | - |
assay at | Synechocystis sp. |
| 7.2 | - |
assay at | Prochlorococcus marinus |
| 7.2 | - |
assay at | Nostoc punctiforme |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADH | - |
Synechococcus sp. | |
| NADH | - |
Synechocystis sp. | |
| NADH | - |
Prochlorococcus marinus | |
| NADH | - |
Nostoc punctiforme | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | the very low activity of the enzyme appears to result from inhibition by the ferredoxin reducing system used in the assay and the low solubility of the substrate | Synechococcus sp. |
| additional information | the very low activity of the enzyme appears to result from inhibition by the ferredoxin reducing system used in the assay and the low solubility of the substrate | Synechocystis sp. |
| additional information | the very low activity of the enzyme appears to result from inhibition by the ferredoxin reducing system used in the assay and the low solubility of the substrate | Prochlorococcus marinus |
| additional information | the very low activity of the enzyme appears to result from inhibition by the ferredoxin reducing system used in the assay and the low solubility of the substrate | Nostoc punctiforme |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
