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Literature summary for 4.2.1.59 extracted from
- Identification and characterization of FabA from the type II fatty acid synthase of Streptomyces coelicolor (2016), J. Nat. Prod., 79, 240-243 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli as soluble N-terminal His6-tag proteins | Streptomyces coelicolor |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptomyces coelicolor | Q9L0M4 AND Q9L0M3 | Q9L0M4: UPF0336 protein SCO4636, Q9L0M3: uncharacterized protein SCO4637 | - |
| Streptomyces coelicolor ATCC BAA-471 | Q9L0M4 AND Q9L0M3 | Q9L0M4: UPF0336 protein SCO4636, Q9L0M3: uncharacterized protein SCO4637 | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3-hydroxydecanoyl-N-acetylcysteamine | the N-acetylcysteamine group is structurally similar to the substrate binding end of the pantethine arm of acyl carrier proteins | Streptomyces coelicolor | ? + H2O | - |
? |  |
| 3-hydroxydecanoyl-N-acetylcysteamine | the N-acetylcysteamine group is structurally similar to the substrate binding end of the pantethine arm of acyl carrier proteins | Streptomyces coelicolor ATCC BAA-471 | ? + H2O | - |
? | |
| 3-hydroxyhexanoyl-N-acetylcysteamine | the N-acetylcysteamine group is structurally similar to the substrate binding end of the pantethine arm of acyl carrier proteins | Streptomyces coelicolor | ? + H2O | - |
? | |
| 3-hydroxyhexanoyl-N-acetylcysteamine | the N-acetylcysteamine group is structurally similar to the substrate binding end of the pantethine arm of acyl carrier proteins | Streptomyces coelicolor ATCC BAA-471 | ? + H2O | - |
? | |
| 3-hydroxyoctanoyl-N-acetylcysteamine | the N-acetylcysteamine group is structurally similar to the substrate binding end of the pantethine arm of acyl carrier proteins | Streptomyces coelicolor | ? + H2O | - |
? | |
| 3-hydroxyoctanoyl-N-acetylcysteamine | the N-acetylcysteamine group is structurally similar to the substrate binding end of the pantethine arm of acyl carrier proteins | Streptomyces coelicolor ATCC BAA-471 | ? + H2O | - |
? | |
| 5-methyl-3-hydroxyhexanoyl-N-acetylcysteamine | the N-acetylcysteamine group is structurally similar to the substrate binding end of the pantethine arm of acyl carrier proteins | Streptomyces coelicolor | ? + H2O | - |
? | |
| 5-methyl-3-hydroxyhexanoyl-N-acetylcysteamine | the N-acetylcysteamine group is structurally similar to the substrate binding end of the pantethine arm of acyl carrier proteins | Streptomyces coelicolor ATCC BAA-471 | ? + H2O | - |
? | |
| 6-methyl-3-hydroxyheptanoyl-N-acetylcysteamine | the N-acetylcysteamine group is structurally similar to the substrate binding end of the pantethine arm of acyl carrier proteins | Streptomyces coelicolor | ? + H2O | - |
? | |
| 6-methyl-3-hydroxyheptanoyl-N-acetylcysteamine | the N-acetylcysteamine group is structurally similar to the substrate binding end of the pantethine arm of acyl carrier proteins | Streptomyces coelicolor ATCC BAA-471 | ? + H2O | - |
? | |
| 7-methyl-3-hydroxyoctanoyl-N-acetylcysteamine | the N-acetylcysteamine group is structurally similar to the substrate binding end of the pantethine arm of acyl carrier proteins | Streptomyces coelicolor | ? + H2O | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heterodimer | 1 * 15000 + 1 * 20000, SDS-PAGE | Streptomyces coelicolor |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 3-hydroxyacyl-ACP dehydratase | - |
Streptomyces coelicolor |
| FabA | - |
Streptomyces coelicolor |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Streptomyces coelicolor |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
assay at | Streptomyces coelicolor |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | the enzyme also processes intermediates in both fatty acid and undecylprodiginine biosynthetic processes. It is capable of utilizing various chain lengths of straight- and branched-chain 3-hydroxyacyl-N-acetyl cysteamine substrates. FabA does not discriminate between acyl carrier proteins from primary and secondary metabolism. It processes intermediates for both biosynthetic pathways | Streptomyces coelicolor |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 144 | - |
7-methyl-3-hydroxyoctanoyl-N-acetylcysteamine | pH 7.2, 25°C | Streptomyces coelicolor | |
| 226 | - |
3-hydroxydecanoyl-N-acetylcysteamine | pH 7.2, 25°C | Streptomyces coelicolor | |
| 363 | - |
3-hydroxyoctanoyl-N-acetylcysteamine | pH 7.2, 25°C | Streptomyces coelicolor | |
| 484 | - |
3-hydroxyhexanoyl-N-acetylcysteamine | pH 7.2, 25°C | Streptomyces coelicolor | |
| 522 | - |
5-methyl-3-hydroxyhexanoyl-N-acetylcysteamine | pH 7.2, 25°C | Streptomyces coelicolor | |
| 527 | - |
6-methyl-3-hydroxyheptanoyl-N-acetylcysteamine | pH 7.2, 25°C | Streptomyces coelicolor | |
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