Any feedback?
Literature summary for 1.2.1.57 extracted from
- Oxygen-tolerant coenzyme A-acylating aldehyde dehydrogenase facilitates efficient photosynthetic n-butanol biosynthesis in cyanobacteria (2013), Energy Environ. Sci., 6, 2672-2681 .
No PubMed abstract available
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene bldh, recombinant expression in Escherichia coli strain JCL166, strain JCL166 cannot grow anaerobically unless complemented by an exogenous fermentation pathway such as n-butanol biosynthesis | Synechococcus elongatus |
| gene bldh, recombinant expression in Escherichia coli strain JCL166, strain JCL166 cannot grow anaerobically unless complemented by an exogenous fermentation pathway such as n-butanol biosynthesis. Recombinant coexpression of PduP with the enzymes of the n-butanol synthesis pathway in Synechococcus elongatus strain PCC 7942 results in autotrophic n-butanol production | Clostridium saccharoperbutylacetonicum |
| gene pduP, recombinant expression in Escherichia coli strain JCL166, strain JCL166 cannot grow anaerobically unless complemented by an exogenous fermentation pathway such as n-butanol biosynthesis. Recombinant coexpression of PduP with the enzymes of the n-butanol synthesis pathway in Synechococcus elongatus strain PCC 7942 results in autotrophic n-butanol production. PduP from Lactobacillus brevis produces more n-butanol than ethanol | Levilactobacillus brevis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | design of a coenzyme A (CoA) dependent n-butanol biosynthesis pathway tailored to the metabolic physiology of the cyanobacterium Synechococcus elongatus PCC 7942 by incorporating an ATP driving force and a kinetically irreversible trap. Oxygen-sensitive CoA-acylating butyraldehyde dehydrogenase (Bldh) is exchanged for the oxygen-tolerant PduP from Salmonella enterica. Replacing Bldh with PduP in the n-butanol synthesis pathway results in n-butanol production to a cumulative titer of 404 mg/l with peak productivity of 51 mg/l per day, exceeding the base strain by 20fold. Anaerobic growth rescue of Escherichia coli strain JCL166 by overexpression of the Clostridium butanol pathway with different aldehyde dehydrogenases PduP | Synechococcus elongatus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | no Michaelis-Menten behaviour | Clostridium saccharoperbutylacetonicum | |
| 0.076 | - |
acetyl-CoA | recombinant enzyme, pH 7.15, 30°C | Levilactobacillus brevis |  |
| 0.534 | - |
butanoyl-CoA | recombinant enzyme, pH 7.15, 30°C | Levilactobacillus brevis | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl-CoA + NADH + H+ | Levilactobacillus brevis | - |
acetaldehyde + CoA + NAD+ | - |
r | |
| acetyl-CoA + NADH + H+ | Clostridium saccharoperbutylacetonicum | low activity | acetaldehyde + CoA + NAD+ | - |
r | |
| butanoyl-CoA + NADH + H+ | Levilactobacillus brevis | - |
butanal + CoA + NAD+ | - |
r | |
| butanoyl-CoA + NADH + H+ | Synechococcus elongatus | - |
butanal + CoA + NAD+ | - |
? | |
| butanoyl-CoA + NADH + H+ | Clostridium saccharoperbutylacetonicum | best substrate | butanal + CoA + NAD+ | - |
r | |
| butanoyl-CoA + NADH + H+ | Synechococcus elongatus PCC 7942 | - |
butanal + CoA + NAD+ | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Clostridium saccharoperbutylacetonicum | - |
- |
- |
| Levilactobacillus brevis | - |
- |
- |
| Synechococcus elongatus | - |
- |
- |
| Synechococcus elongatus PCC 7942 | - |
- |
- |
Oxidation Stability
| Oxidation Stability | Organism |
|---|---|
| oxygen sensitivity of CoA-acylating aldehyde dehydrogenase | Synechococcus elongatus |
| the enzyme is oxygen-tolerant | Levilactobacillus brevis |
| the enzyme is oxygen-tolerant | Clostridium saccharoperbutylacetonicum |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.49 | - |
with butanoyl-CoA, pH 7.15, 30°C | Clostridium saccharoperbutylacetonicum |
| 2.5 | - |
with butanoyl-CoA, pH 7.15, 30°C | Levilactobacillus brevis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl-CoA + NADH + H+ | - |
Levilactobacillus brevis | acetaldehyde + CoA + NAD+ | - |
r | |
| acetyl-CoA + NADH + H+ | low activity | Clostridium saccharoperbutylacetonicum | acetaldehyde + CoA + NAD+ | - |
r | |
| butanoyl-CoA + NADH + H+ | - |
Levilactobacillus brevis | butanal + CoA + NAD+ | - |
r | |
| butanoyl-CoA + NADH + H+ | - |
Synechococcus elongatus | butanal + CoA + NAD+ | - |
? | |
| butanoyl-CoA + NADH + H+ | best substrate | Clostridium saccharoperbutylacetonicum | butanal + CoA + NAD+ | - |
r | |
| butanoyl-CoA + NADH + H+ | - |
Synechococcus elongatus PCC 7942 | butanal + CoA + NAD+ | - |
? | |
| additional information | substrate chain length specificity of the enzyme is C2-C12, highest activity with C6 substrate, overview | Levilactobacillus brevis | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Bldh | - |
Synechococcus elongatus |
| Bldh | - |
Clostridium saccharoperbutylacetonicum |
| CoA-acylating aldehyde dehydrogenase | - |
Levilactobacillus brevis |
| CoA-acylating aldehyde dehydrogenase | - |
Synechococcus elongatus |
| CoA-acylating aldehyde dehydrogenase | - |
Clostridium saccharoperbutylacetonicum |
| CoA-acylating butyraldehyde dehydrogenase | - |
Synechococcus elongatus |
| coenzyme A-acylating aldehyde dehydrogenase | - |
Levilactobacillus brevis |
| coenzyme A-acylating aldehyde dehydrogenase | - |
Synechococcus elongatus |
| coenzyme A-acylating aldehyde dehydrogenase | - |
Clostridium saccharoperbutylacetonicum |
| PduP | - |
Levilactobacillus brevis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Levilactobacillus brevis |
| 30 | - |
assay at | Clostridium saccharoperbutylacetonicum |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.26 | - |
acetyl-CoA | recombinant enzyme, pH 7.15, 30°C | Levilactobacillus brevis | |
| 3.37 | - |
butanoyl-CoA | recombinant enzyme, pH 7.15, 30°C | Levilactobacillus brevis | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.15 | - |
assay at | Levilactobacillus brevis |
| 7.15 | - |
assay at | Clostridium saccharoperbutylacetonicum |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADH | - |
Levilactobacillus brevis | |
| NADH | - |
Synechococcus elongatus | |
| NADH | - |
Clostridium saccharoperbutylacetonicum | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | the oxygen sensitivity of CoA-acylating aldehyde dehydrogenase appears to be a key limiting factor for cyanobacteria to produce alcohols through the CoA-dependent route | Levilactobacillus brevis |
| metabolism | the oxygen sensitivity of CoA-acylating aldehyde dehydrogenase appears to be a key limiting factor for cyanobacteria to produce alcohols through the CoA-dependent route | Synechococcus elongatus |
| metabolism | the oxygen sensitivity of CoA-acylating aldehyde dehydrogenase appears to be a key limiting factor for cyanobacteria to produce alcohols through the CoA-dependent route | Clostridium saccharoperbutylacetonicum |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 3 | - |
acetyl-CoA | recombinant enzyme, pH 7.15, 30°C | Levilactobacillus brevis | |
| 6 | - |
butanoyl-CoA | recombinant enzyme, pH 7.15, 30°C | Levilactobacillus brevis | |
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
