The X-prolyl dipeptidyl-peptidase PepX of Streptococcus thermophilus initially described as intracellular is also responsible for peptidase extracellular activity
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منابع مشابه
Novel extracellular x-prolyl dipeptidyl-peptidase (DPP) from Streptococcus gordonii FSS2: an emerging subfamily of viridans Streptococcal x-prolyl DPPs.
Streptococcus gordonii is generally considered a benign inhabitant of the oral microflora, and yet it is a primary etiological agent in the development of subacute bacterial endocarditis (SBE), an inflammatory state that propagates thrombus formation and tissue damage on the surface of heart valves. Strain FSS2 produced several extracellular aminopeptidase and fibrinogen-degrading activities du...
متن کاملAmylase-binding protein B of Streptococcus gordonii is an extracellular dipeptidyl-peptidase.
The oral commensal bacterium Streptococcus gordonii interacts with salivary amylase via two amylase-binding proteins, AbpA and AbpB. Based on sequence analysis, the 20-kDa AbpA protein is unique to S. gordonii, whereas the 82-kDa AbpB protein appears to share sequence homology with other bacterial dipeptidases. The aim of this study was to verify the peptidase activity of AbpB and further explo...
متن کاملPurification and characterization of an X-prolyl-dipeptidyl peptidase from Lactobacillus sakei.
An X-prolyl-dipeptidyl peptidase has been purified from Lactobacillus sakei by ammonium sulfate fractionation and five chromatographic steps, which included hydrophobic interaction, anion-exchange chromatography, and gel filtration chromatography. This procedure resulted in a recovery yield of 7% and an increase in specificity of 737-fold. The enzyme appeared to be a dimer with a subunit molecu...
متن کاملDipeptidyl-Peptidase IV Activity Is Correlated with Colorectal Cancer Prognosis
BACKGROUND Dipeptidyl-peptidase IV (EC 3.4.14.5) (DPPIV) is a serine peptidase involved in cell differentiation, adhesion, immune modulation and apoptosis, functions that control neoplastic transformation. Previous studies have demonstrated altered expression and activity of tissue and circulating DPPIV in several cancers and proposed its potential usefulness for early diagnosis in colorectal c...
متن کاملDipeptidyl peptidase IV of Streptococcus anginosus: purification and characterization.
We found that N-unblocked nine p-nitroanilde derivatives of amino acids or peptides were hydrolyzed by the crude cell extracts of Streptococcus anginosus NCTC 10713. Then dipeptidyl peptidase IV was purified 323-fold by the procedures including ammonium sulfate concentration, anion exchange chromatography (twice), gel filtration (twice), hydrophobic interaction chromatography, and isoelectric f...
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ژورنال
عنوان ژورنال: Journal of Dairy Science
سال: 2019
ISSN: 0022-0302
DOI: 10.3168/jds.2018-14823