Deregulation of allosteric response of Lactococcus lactis prolidase and its effects on enzyme activity
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry
Reference39 articles.
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2. Lactobacilli carry cryptic genes encoding peptidase-related proteins: characterization of a prolidase gene (pepQ) and a related cryptic gene (orfZ) from Lactobacillus delbrueckii subsp. bulgaricus;Rantanen;Microbiology UK,1997
3. Characterization of recombinant prolidase from Lactococcus lactis: changes in substrate specificity by metal cations, and allosteric behaviour of the peptidase;Yang;FEBS J.,2008
4. Cloning and DNA-sequence analysis of PepQ, a prolidase gene from Lactobacillus delbrueckii subsp lactis DSM7290 and partial characterization of Its product;Stucky;Mol. Gen. Genet.,1995
5. Relationship between carbon catabolite repression and the biosynthesis regulation of the prolidase PepQ from Lactobacillus delbrueckii ssp bulgaricus CNRZ 397;Lamarque;Lait,2001
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1. Structural basis for the allosteric behaviour and substrate specificity of Lactococcus lactis Prolidase;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2024-05
2. Prolidase – A protein with many faces;Biochimie;2021-04
3. Crystallographic structure of recombinant Lactococcus lactis prolidase to support proposed structure-function relationships;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2017-05
4. Crystal structure and biochemical investigations reveal novel mode of substrate selectivity and illuminate substrate inhibition and allostericity in a subfamily of Xaa-Pro dipeptidases;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2017-02
5. Xaa-Pro Dipeptidase (Bacteria);Handbook of Proteolytic Enzymes;2013
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