Cloning of a novel prolidase gene from Aureobacterium esteraromaticum

Biochim Biophys Acta. 1999 Jan 11;1429(2):516-20. doi: 10.1016/s0167-4838(98)00256-8.


The prolidase gene from Aureobacterium esteraromaticum was cloned and expressed in Escherichia coli. The cloned enzyme had the same enzymatic properties as the wild-type enzyme. Kinetic analysis of the enzyme indicated that the best substrate was Pro-Hyp, which was not hydrolyzed by other prolidases. Interestingly, there was no homology between the deduced amino acid sequence of A. esteraromaticum prolidase and those of the other sources such as human E. coli and Lactobacillus. However, homology was seen with the yeast hypothetical protein YJL213w, the function of which is unknown. These findings indicate that the A. esteraromaticum prolidase is a novel enzyme different from other prolidases reported to date.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Cloning, Molecular
  • Dipeptidases / chemistry
  • Dipeptidases / genetics*
  • Gram-Positive Asporogenous Rods / enzymology
  • Gram-Positive Asporogenous Rods / genetics*
  • Molecular Sequence Data
  • Sequence Alignment


  • Dipeptidases
  • proline dipeptidase

Associated data

  • GENBANK/AB014613