The leader peptide is not required for post-translational modification by lacticin 481 synthetase

Journal of the American Chemical Society

Volumn 129, Issue 34, 2007, Pages 10314-10315

  Levengood, Matthew R ^a   Patton, Gregory C ^a   Van Der Donk, Wilfred A ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LACTICIN 481 SYNTHETASE; LANTIBIOTIC; NISIN; SYNTHETASE; UNCLASSIFIED DRUG;

ARTICLE; CYCLOADDITION; ENZYME ACTIVITY; PROTEIN PHOSPHORYLATION; TANDEM MASS SPECTROMETRY; TRANSLATION INITIATION;

BACTERIOCINS; MOLECULAR SEQUENCE DATA; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN SORTING SIGNALS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

EID: 34548245086     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja072967+     Document Type: Article

References (16)

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11. See the Supporting Information. Most experiments in this study were performed on a fully active mutant of LctA (N39R/F45H) that has much improved solubility compared to that of the wild-type LctA. See ref 14.
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14. 3a we reported that removing the leader peptide of LctA abolished dehydration activity by LctM, which appears to be at odds with the results presented here. A possible explanation lies in the presence of a His-tag on the leaderless substrate in ref 3a located immediately N-terminal to the structural region, which may have had a deleterious effect.
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