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Literature summary for 2.3.1.28 extracted from
- Thermoadaptation-directed evolution of chloramphenicol acetyltransferase in an error-prone thermophile using improved procedures (2015), Appl. Microbiol. Biotechnol., 99, 5563-5572.
Application
| Application | Comment | Organism |
|---|---|---|
| molecular biology | the enzyme mutant CATA138T may be useful as a genetic marker in Geobacillus spp. | Staphylococcus aureus |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene cat, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21-CodonPlus(DE3)-RIPL and in Geobacillus kaustophilus strain MK480 | Staphylococcus aureus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| A138S | site-directed mutagenesis, the enzyme mutant shows increased thermostability at 60-65°C for 24 h compared to the wild-type enzyme, thermostability enhancement results from the A138T replacement and can attributed to both the presence of a hydroxyl group and the bulk of the threonine side chain. CAT A138S mutation confers chloramphenicol resistance to Geobacillus kaustophilus cells at high temperature more efficiently than the wild-type enzyme | Staphylococcus aureus |
| A138T | site-directed mutagenesis, the enzyme mutant shows increased thermostability at 60-65°C for 24 h compared to the wild-type enzyme, thermostability enhancement results from the A138T replacement and can attributed to both the presence of a hydroxyl group and the bulk of the threonine side chain. CAT A138T mutation confers chloramphenicol resistance to Geobacillus kaustophilus cells at high temperature more efficiently than the wild-type enzyme. The A138T substitution has no effect on CAT activity | Staphylococcus aureus |
| A138V | site-directed mutagenesis, the enzyme mutant shows highly increased thermostability at 60-65°C for 24 h compared to the wild-type enzyme, thermostability enhancement results from the A138T replacement and can attributed to both the presence of a hydroxyl group and the bulk of the threonine side chain. CAT A138V mutation confers chloramphenicol resistance to Geobacillus kaustophilus cells at high temperature more efficiently than the wild-type enzyme | Staphylococcus aureus |
| additional information | thermoadaptation-directed enzyme evolution approach for generation of mutant genes encoding enzyme variants that are more thermostable than the parent enzyme using an error-prone thermophile strain MK480 derived from Geobacillus kaustophilus strain HTA426, increase of the thermostability of the chloramphenicol acetyltransferase (CAT) from Staphylococcus aureus and successfully generation of a CAT variant with an A138 replacement (CATA138X), method, overview | Staphylococcus aureus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.153 | - |
chloramphenicol | pH 7.0, 60°C, recombinant mutant A138T | Staphylococcus aureus |  |
| 0.162 | - |
chloramphenicol | pH 7.0, 60°C, recombinant wild-type enzyme | Staphylococcus aureus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 25000 | - |
3 * 25000, about, SDS-PAGE | Staphylococcus aureus |
| 75000 | - |
recombinant enzyme, gel filtration | Staphylococcus aureus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl-CoA + chloramphenicol | Staphylococcus aureus | - |
CoA + chloramphenicol 3-acetate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Staphylococcus aureus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21-CodonPlus(DE3)-RIPL by nickel affinity chromatography and gel filtration | Staphylococcus aureus |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 140 | - |
pH 7.0, 60°C, purified recombinant mutant A138T | Staphylococcus aureus |
| 240 | - |
pH 7.0, 60°C, purified recombinant mutant A138V | Staphylococcus aureus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl-CoA + chloramphenicol | - |
Staphylococcus aureus | CoA + chloramphenicol 3-acetate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homotrimer | 3 * 25000, about, SDS-PAGE | Staphylococcus aureus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CAT | - |
Staphylococcus aureus |
| chloramphenicol acetyltransferase | - |
Staphylococcus aureus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | 60 | - |
Staphylococcus aureus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 75 | activity range, inactivation at 77°C | Staphylococcus aureus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 193 | - |
chloramphenicol | pH 7.0, 60°C, recombinant mutant A138T | Staphylococcus aureus | |
| 209 | - |
chloramphenicol | pH 7.0, 60°C, recombinant wild-type enzyme | Staphylococcus aureus | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Staphylococcus aureus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| acetyl-CoA | - |
Staphylococcus aureus | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | CAT members are currently classified into three types on the basis of their substrate specificities. Staphylococcus aureus CAT is classified as type III | Staphylococcus aureus |
| additional information | homology modeling of enzyme CAT structures using the crystal structure of Escherichia coli CAT, PDB ID 3CLA, overview. Residue A138 resides on beta-sheet 7 and is located on the protein surfaces far from the active center. Although the side chains of I134, P135, and L164 surround this residue, no hydrophobic interactions are observed within 4 A. Modeling of CATA138T, overview | Staphylococcus aureus |
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