Purification to homogeneity and characterization of acyl coenzyme A:6-aminopenicillanic acid acyltransferase of Penicillium chrysogenum.

@article{Alvarez1987PurificationTH,
  title={Purification to homogeneity and characterization of acyl coenzyme A:6-aminopenicillanic acid acyltransferase of Penicillium chrysogenum.},
  author={Estela M. Alvarez and Jes{\'u}s Manuel Cantoral and Jos{\'e} Barredo and B. Diez and Juan F. Martin},
  journal={Antimicrobial agents and chemotherapy},
  year={1987},
  volume={31 11},
  pages={1675-82}
}
The acyl coenzyme A (CoA):6-aminopenicillanic acid (6-APA) acyltransferase of Penicillium chrysogenum AS-P-78 was purified to homogeneity, as concluded by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and isoelectric focusing. The enzyme is a monomer with a molecular weight of 30,000 +/- 1,000 and a pI of about 5.5. The optimal pH and temperature were 8.0 and 25 degrees C, respectively. This enzyme converts 6-APA into penicillin by using phenylacetyl CoA or phenoxyacetyl CoA as acyl… CONTINUE READING
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