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Infection and Immunity, February 2005, p. 1256-1259, Vol. 73, No. 2
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.2.1256-1259.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Characterization of an Extracellular Dipeptidase from Streptococcus gordonii FSS2

J. M. Goldstein,1,{dagger} T. Kordula,2 J. L. Moon,1 J. A. Mayo,1* and J. Travis1

Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia,1 Department of Biochemistry, Medical College of Virginia Campus, Virginia Commonwealth University, Richmond, Virginia2

Received 10 May 2004/ Returned for modification 14 June 2004/ Accepted 30 September 2004

PepV, a dipeptidase found in culture fluids of Streptococcus gordonii FSS2, was purified and characterized, and its gene was cloned. PepV is a monomeric metalloenzyme of approximately 55 kDa that preferentially degrades hydrophobic dipeptides. The gene encodes a polypeptide of 467 amino acids, with a theoretical molecular mass of 51,114 Da and a calculated pI of 4.8. The S. gordonii PepV gene is homologous to the PepV gene family from Lactobacillus and Lactococcus spp.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602-7229. Phone: (706) 542-1713. Fax: (706) 542-3719. E-mail: jmayo{at}uga.edu.

Editor: J. T. Barbieri

{dagger} Present address: Elan Pharmaceuticals, South San Francisco, Calif.

Infection and Immunity, February 2005, p. 1256-1259, Vol. 73, No. 2
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.2.1256-1259.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.





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