Putative "acylaminoacyl" peptidases from Streptomyces griseus and S. coelicolor display "aminopeptidase" activities with distinct substrate specificities and sensitivities to reducing reagent

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1794, Issue 3, 2009, Pages 468-475

  Usuki, Hirokazu ^a   Uesugi, Yoshiko ^a   Iwabuchi, Masaki ^a   Hatanaka, Tadashi ^a  

^a Research Institute for Biological Science OKAYAMA   (Japan)

Author keywords

Actinomycete; Phenylalanylaminopeptidase; Prolyl oligopeptidase; Serine peptidase; Substrate recognition property

Indexed keywords

AMINOPEPTIDASE; ANILIDE; DITHIOTHREITOL; OLIGOPEPTIDE; PHENYLALANINE 4 NITROANILIDE; REDUCING AGENT; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; ENZYME ACTIVITY; ENZYME SPECIFICITY; PH; PRIORITY JOURNAL; SENSITIVITY AND SPECIFICITY; SEQUENCE HOMOLOGY; STREPTOMYCES COELICOLOR; STREPTOMYCES GRISEUS;

AMINO ACID SEQUENCE; AMINOPEPTIDASES; CLONING, MOLECULAR; DITHIOTHREITOL; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; PEPTIDE HYDROLASES; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; STREPTOMYCES COELICOLOR; STREPTOMYCES GRISEUS; SUBSTRATE SPECIFICITY;

STREPTOMYCES GRISEUS;

EID: 59349106830     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.12.013     Document Type: Article

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