Newly discovered penicillin acylase activity of aculeacin A acylase from Actinoplanes utahensis

Appl Environ Microbiol. 2007 Aug;73(16):5378-81. doi: 10.1128/AEM.00452-07. Epub 2007 Jun 22.

Abstract

Aculeacin A acylase from Actinoplanes utahensis produced by Streptomyces lividans revealed acylase activities that are able to hydrolyze penicillin V and several natural aliphatic penicillins. Penicillin K was the best substrate, showing a catalytic efficiency of 34.79 mM(-1) s(-1). Furthermore, aculeacin A acylase was highly thermostable, with a midpoint transition temperature of 81.5 degrees C.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actinomycetales / enzymology*
  • Actinomycetales / genetics
  • Amidohydrolases / genetics
  • Amidohydrolases / metabolism*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Circular Dichroism
  • Enzyme Stability
  • Molecular Structure
  • Penicillin Amidase / genetics
  • Penicillin Amidase / metabolism*
  • Penicillin V / chemistry
  • Penicillin V / metabolism
  • Peptides, Cyclic / chemistry
  • Peptides, Cyclic / metabolism
  • Recombinant Proteins / metabolism
  • Substrate Specificity
  • Temperature

Substances

  • Bacterial Proteins
  • Peptides, Cyclic
  • Recombinant Proteins
  • aculeacin A
  • Amidohydrolases
  • aculeacin A acylase
  • Penicillin Amidase
  • Penicillin V