Characterization of an Extracellular Dipeptidase from Streptococcus gordonii FSS2-Reference-Cited by-同舟云学术

Characterization of an Extracellular Dipeptidase from Streptococcus gordonii FSS2

Published:2005-02 Issue:2 Volume:73 Page:1256-1259
ISSN:0019-9567
Container-title:Infection and Immunity
language:en
Short-container-title:Infect Immun

Author:

Goldstein J. M.¹,Kordula T.²,Moon J. L.¹,Mayo J. A.¹,Travis J.¹

Affiliation:

1. Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia

2. Department of Biochemistry, Medical College of Virginia Campus, Virginia Commonwealth University, Richmond, Virginia

Abstract

ABSTRACT 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.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Immunology,Microbiology,Parasitology

Link

https://journals.asm.org/doi/pdf/10.1128/IAI.73.2.1256-1259.2005

Reference16 articles.

1. Blum, H., H. Beier, and H. J. Gross. 1987. Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis8:93-99.

2. Doi, E., D. Shibota, and T. Matoba. 1981. Modified colorimetric ninhydrin methods for peptidase assay. Anal. Biochem.118:173-184.

3. Sequencing, distribution, and inactivation of the dipeptidase A gene (pepDA) from Lactobacillus helveticus CNRZ32

4. Novel Extracellular x-Prolyl Dipeptidyl-Peptidase (DPP) from Streptococcus gordonii FSS2: an Emerging Subfamily of Viridans Streptococcal x-Prolyl DPPs

5. Goldstein, J. M., D. Nelson, T. Kordula, J. A. Mayo, and J. Travis. 2002. Extracellular arginine aminopeptidase from Streptococcus gordonii. Infect. Immun.70:835-843.

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