Paenidase, a novel D-aspartyl endopeptidase from Paenibacillus sp. B38: Purification and substrate specificity

Journal of Biochemistry

Volumn 139, Issue 2, 2006, Pages 197-202

  Takahashi, Saori ^a   Ogasawara, Hironobu ^a   Hiwatashi, Kazuyuki ^a   Hori, Kazuyuki ^a   Hata, Keishi ^a   Tachibana, Tadanori ^a   Itoh, Yoshifumi ^a   Sugiyama, Toshihiro ^b  

^a Akita Research Institute of Food and Brewing   (Japan)

^b AKITA UNIVERSITY SCHOOL OF MEDICINE   (Japan)

Author keywords

D amino acid; D aspartic acid; Endopeptidase; Protease; Substrate specificity

Indexed keywords

4 NITROANILINE; 7 AMINO 4 METHYLCOUMARIN; AMYLOID BETA PROTEIN; ASPARTYLALANYLGLUTAMYLPHENYLALANYLARGINYLHISTIDYL DEXTRO ASPARTYLGLYCYLSERYLTYROSINE; COUMARIN DERIVATIVE; DEXTRO ASPARTYL ENDOPEPTIDASE; PAENIDASE; PROTEINASE; SUCCINYL DEXTRO ASPARTIC ACID ALPHA (4 METHYLCOUMARYL 7 AMIDE); SUCCINYL DEXTRO ASPARTIC ACID ALPHA (4 NITROANILIDE); SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL BOND; ENZYME MECHANISM; ENZYME MODIFICATION; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME SYNTHESIS; NONHUMAN; PAENIBACILLUS; PROTEIN DEGRADATION; SEQUENCE ANALYSIS;

ANILIDES; ANILINE COMPOUNDS; ASPARTIC ACID; ASPARTIC ACID ENDOPEPTIDASES; ASPARTIC ENDOPEPTIDASES; BACILLACEAE; COUMARINS; ENZYME ACTIVATION; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PROTEASE INHIBITORS; SUBSTRATE SPECIFICITY; TEMPERATURE;

BACTERIA (MICROORGANISMS); PAENIBACILLUS; PAENIBACILLUS SP.;

EID: 33645275474     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1587/elex.3.197     Document Type: Article

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