Difference between revisions of "PMID:14009486"
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== Materials and Methods Used == | == Materials and Methods Used == | ||
{{LitMaterials}} | {{LitMaterials}} | ||
| + | *Strain: ML308 | ||
| + | *Hydroxamate assay | ||
| + | *Sulfhydryl assay | ||
==Phenotype Annotations== | ==Phenotype Annotations== | ||
Latest revision as of 17:11, 17 September 2012
| Citation |
ZABIN, I , KEPES, A and MONOD, J (1962) Thiogalactoside transacetylase. J. Biol. Chem. 237:253-7 |
|---|---|
| Abstract |
No abstract in PubMed |
| Links | |
| Keywords |
Transferases/chemistry |
| edit table |
Main Points of the Paper
Please summarize the main points of the paper.
- Thiogalactoside transacetylase is identified
- Characterization of the purified protein is also described
- rate of formation of acetyl-IPTG as a function of time- reaction is linear
- optimal pH is 7.0 in phosphate buffer, but 8.2 in Tris buffer
- KM<4x10-5 M for acetyl-CoA
- Butyryl-CoA was about 10% as effective as acetyl-CoA as donors
- catalyzes the transfer of acetyl from acetyl-CoA to thiogalactosides
- divalent cations are not required for the formation of acetyl-IPTG
- activity is slightly inhibited by 0.001 M p-Chloromercuribenzoate (31% inhibition)
- essentially all the activity present in the supernatant fraction
Materials and Methods Used
Please list the materials and methods used in this paper (strains, plasmids, antibodies, etc).
- Strain: ML308
- Hydroxamate assay
- Sulfhydryl assay
Phenotype Annotations
See Help:AnnotationTable for details on how to edit this table.
<protect>
| Phenotype of | Taxon Information | Genotype Information (if known) | Condition Information | OMP ID | OMP Term Name | ECO ID | ECO Term Name | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|
| edit table |
</protect>
Notes
References
See Help:References for how to manage references in omp dev.
