Biochemical and molecular characterization of PepR, a dipeptidase, from Lactobacillus helveticus CNRZ32.

A dipeptidase with prolinase activity from Lactobacillus helveticus CNRZ32, which was designated PepR, was purified to gel electrophoretic homogeneity and characterized. The NH2-terminal amino acid sequence of the purified protein had 96% identity to the deduced NH2-terminal amino acid sequence of t...

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Bibliografske podrobnosti

izdano v:	Appl Environ Microbiol
Principais autores:	Shao, W, Yüksel, G U, Dudley, E G, Parkin, K L, Steele, J L
Format:	Artigo
Jezik:	Inglês
Izdano:	American Society for Microbiology (ASM) 1997
Teme:	Research Article
Online dostop:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC168651/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/9292995/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/aem.63.9.3438-3443.1997
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