Activation of oligopeptidase B from Streptomyces griseus by thiol-reacting reagents is independent of the single reactive cysteine residue

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1794, Issue 11, 2009, Pages 1673-1683

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

^a Research Institute for Biological Science OKAYAMA   (Japan)

Author keywords

Actinomycete; Oligopeptidase B; Prolyl oligopeptidase; Serine peptidase; Substrate recognition property; Thiol reacting reagents

Indexed keywords

ASPARTIC ACID; CYSTEINE; CYSTEINE DERIVATIVE; DITHIOTHREITOL; GLUTATHIONE; GLUTATHIONE DISULFIDE; OLIGOPEPTIDASE B; PEPTIDASE; PROLYL ENDOPEPTIDASE; SODIUM CHLORIDE; THIOL REAGENT; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; CONCENTRATION (PARAMETERS); CONFORMATIONAL TRANSITION; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME SPECIFICITY; KNOWLEDGE; MOLECULAR CLONING; MOLECULAR RECOGNITION; MUTANT; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; STREPTOMYCES GRISEUS;

AMINO ACID SEQUENCE; ENZYME ACTIVATION; HYDROGEN-ION CONCENTRATION; PROTEIN CONFORMATION; SERINE ENDOPEPTIDASES; SODIUM CHLORIDE; STREPTOMYCES GRISEUS; SUBSTRATE SPECIFICITY; SULFHYDRYL REAGENTS;

STREPTOMYCES GRISEUS;

EID: 70249141558     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.07.024     Document Type: Article

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