ε-poly-L-lysine dispersity is controlled by a highly unusual nonribosomal peptide synthetase

Nature Chemical Biology

Volumn 4, Issue 12, 2008, Pages 766-772

  Yamanaka, Kazuya ^a   Maruyama, Chitose ^b,c   Takagi, Hiroshi ^b,d   Hamano, Yoshimitsu ^b  

^a CHISSO CORPORATION   (Japan)

^b FUKUI PREFECTURAL UNIVERSITY   (Japan)

^c UNIVERSITY OF FUKUI   (Japan)

^d NARA INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

EPSILON POLYLYSINE; EPSILON POLYLYSINE SYNTHETASE; PEPTIDE SYNTHASE; POLYLYSINE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; EPSILON POLY L LYSINE SYNTHETHASE, STREPTOMYCES ALBULUS; EPSILON-POLY-L-LYSINE SYNTHETHASE, STREPTOMYCES ALBULUS; MEMBRANE PROTEIN;

ADENYLATION; ANIMAL CELL; ARTICLE; CHEMICAL BOND; CHEMICAL MODIFICATION; CONTROLLED STUDY; ENZYME ANALYSIS; ENZYME MECHANISM; ENZYME PURIFICATION; ENZYME SPECIFICITY; MOLECULAR CLONING; NONHUMAN; POLYMERIZATION; PRIORITY JOURNAL; STREPTOMYCES; STREPTOMYCES ALBULUS; THIOLATION; BIOSYNTHESIS; CATALYSIS; ENZYMOLOGY; METABOLISM; MOLECULAR GENETICS; NONRIBOSOMAL PEPTIDE SYNTHESIS; PROTEIN CONFORMATION;

STREPTOMYCES ALBULUS;

BACTERIAL PROTEINS; CATALYSIS; CLONING, MOLECULAR; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; PEPTIDE BIOSYNTHESIS, NUCLEIC ACID-INDEPENDENT; PEPTIDE SYNTHASES; POLYLYSINE; PROTEIN CONFORMATION; STREPTOMYCES; SUBSTRATE SPECIFICITY;

EID: 56249145109     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.125     Document Type: Article

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