The dehydratase activity of lacticin 481 synthetase is highly processive

Journal of the American Chemical Society

Volumn 128, Issue 5, 2006, Pages 1420-1421

  Miller, Leah M ^a   Chatterjee, Champak ^a   Van Der Donk, Wilfred A ^a   Kelleher, Neu L ^a  

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

Author keywords

[No Author keywords available]

Indexed keywords

HYDROLYASE; LACTICIN 481 SYNTHETASE; UNCLASSIFIED DRUG;

ARTICLE; CYCLIZATION; DERIVATIZATION; DISSOCIATION; ELECTROSPRAY MASS SPECTROMETRY; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY;

AMINO ACID SEQUENCE; BACTERIOCINS; CYCLIZATION; ENZYMES; HYDRO-LYASES; MOLECULAR SEQUENCE DATA; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;

EID: 32244446657     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja057203d     Document Type: Article

References (12)

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7. cat for each consecutive dehydration step. This model can be tested using the isotope trapping method (Rose, I. A. Methods Enzymol. 1980, 64, 47-59), and experiments along these lines are underway.
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10. CDAP treatment of the assay mixtures at 0 min, 20 min, 40 min, and 2 h time points gave rise to the spectra shown in Figure S5.
11. Marshall, A. G.; Wang, T. C. L.; Ricca, T. L. J. Am. Chem. Soc. 1985, 107, 7893-7897.
12. 2O species prevented dehydration at Ser42 cannot be ruled out from the results obtained here. However, the conversion of some of the partially processed species to the completely processed peptide does occur in a slower process that likely represents a minor distributive pathway for LctM action like that in other processive enzymes, such as DNA polymerase beta: Osheroff, W. P.; Jung, H. K.; Beard, W. A.; Wilson, S. H.; Kunkel, T. A., J. Biol. Chem. 1999, 274, 3642-3650.