This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hirrlinger, B.
Right arrow Articles by Knackmuss, H. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hirrlinger, B.
Right arrow Articles by Knackmuss, H. J.

 Previous Article  |  Next Article 

J. Bacteriol., Jun 1996, 3501-3507, Vol 178, No. 12
Copyright © 1996, American Society for Microbiology

Purification and properties of an amidase from Rhodococcus erythropolis MP50 which enantioselectively hydrolyzes 2-arylpropionamides

B Hirrlinger, A Stolz and HJ Knackmuss
Institut fur Mikrobiologie, Universitat Stuttgart, Germany.

An enantioselective amidase from Rhodococcus erythropolis MP50 was purified to homogeneity. The enzyme has a molecular weight of about 480,000 and is composed of identical subunits with molecular weights of about 61,000. The NH2-terminal amino acid sequence was significantly different from previously published sequences of bacterial amidases. The purified amidase hydrolyzed a wide range of aliphatic and aromatic amides, The highest enzyme activities were found with amides carrying hydrophobic residues, such as pentyl or naphthoyl. The purified enzyme converted racemic 2-phenylpropionamide, naproxen amide [2-(6-methoxy-2- naphthyl) propionamide], and ketoprofen amide [2-(3'- benzoylphenyl)propionamide] to the corresponding S-acids with an enantiomeric excess of >99% and an almost 50% conversion of the racemic amides. The enzyme also hydrolyzed different alpha-amino amides but without significant enantioselectivity.


This article has been cited by other articles:

  • Wang, P.-F., Yep, A., Kenyon, G. L., McLeish, M. J. (2009). Using directed evolution to probe the substrate specificity of mandelamide hydrolase. Protein Eng Des Sel 22: 103-110 [Abstract] [Full Text]  
  • McLeish, M. J., Kneen, M. M., Gopalakrishna, K. N., Koo, C. W., Babbitt, P. C., Gerlt, J. A., Kenyon, G. L. (2003). Identification and Characterization of a Mandelamide Hydrolase and an NAD(P)+-Dependent Benzaldehyde Dehydrogenase from Pseudomonas putida ATCC 12633. J. Bacteriol. 185: 2451-2456 [Abstract] [Full Text]  
  • Trott, S., Burger, S., Calaminus, C., Stolz, A. (2002). Cloning and Heterologous Expression of an Enantioselective Amidase from Rhodococcus erythropolis Strain MP50. Appl. Environ. Microbiol. 68: 3279-3286 [Abstract] [Full Text]  
  • Trott, S., Bauer, R., Knackmuss, H.-J., Stolz, A. (2001). Genetic and biochemical characterization of an enantioselective amidase from Agrobacterium tumefaciens strain d3. Microbiology 147: 1815-1824 [Abstract] [Full Text]  
  • Soong, C.-L., Ogawa, J., Shimizu, S. (2000). A Novel Amidase (Half-Amidase) for Half-Amide Hydrolysis Involved in the Bacterial Metabolism of Cyclic Imides. Appl. Environ. Microbiol. 66: 1947-1952 [Abstract] [Full Text]  
  • Fournand, D., Bigey, F., Arnaud, A. (1998). Acyl Transfer Activity of an Amidase from Rhodococcus sp. Strain R312: Formation of a Wide Range of Hydroxamic Acids. Appl. Environ. Microbiol. 64: 2844-2852 [Abstract] [Full Text]