Enniatin synthetase is a monomer with extended structure: Evidence for an intramolecular reaction mechanism

Archives of Microbiology

Volumn 178, Issue 4, 2002, Pages 267-273

  Glinski, Mirko ^a   Urbanke, Claus ^b   Hornbogen, Till ^a   Zocher, Rainer ^a  

^a TECHNISCHE UNIVERSITÄT BERLIN   (Germany)

^b HANNOVER MEDICAL SCHOOL   (Germany)

Author keywords

Analytical ultracentrifugation; Enniatin synthetase; Fusarium scirpi; N methylcyclopeptides; Nonribosomal peptide synthesis; Thiol template mechanism

Indexed keywords

2 HYDROXYISOVALERIC ACID; ADENOSINE TRIPHOSPHATE; ENNIATIN SYNTHETASE; FATTY ACID SYNTHASE; MONOMER; SYNTHETASE; UNCLASSIFIED DRUG; VALERIC ACID DERIVATIVE;

ARTICLE; CALCULATION; CATALYST; CONTROLLED STUDY; ENZYME ANALYSIS; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SYNTHESIS; FUSARIUM; FUSARIUM SCIRPI; MOLECULAR WEIGHT; MOLECULE; NONHUMAN; OPEN READING FRAME; PRIORITY JOURNAL; REACTION ANALYSIS; SEDIMENTATION RATE; ULTRACENTRIFUGATION;

ANTI-BACTERIAL AGENTS; DEPSIPEPTIDES; FUSARIUM; PEPTIDE SYNTHASES; PEPTIDES; PEPTIDES, CYCLIC; ULTRACENTRIFUGATION;

FUSARIUM; FUSARIUM EQUISETI;

EID: 0036037587     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00203-002-0451-1     Document Type: Article

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