The dehydratase activity of lacticin 481 synthetase is highly processive

Leah M. Miller; Champak Chatterjee; Wilfred A. Van Der Donk; Neu L. Kelleher

doi:10.1021/ja057203d

The dehydratase activity of lacticin 481 synthetase is highly processive

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

Research output: Contribution to journal › Article › peer-review

Abstract

Lacticin 481 synthetase (LctM) is a bifunctional enzyme that undertakes dehydration and cyclization in the structural region of the pre-lacticin peptide (LctA) to introduce three thioether rings and one dehydrobutyrine residue. The order and timing of these events has been investigated employing high-resolution ESI-FTMS-based tandem MS/MS techniques and chemical derivatization. LctM demonstrates highly processive behavior as seen by MS analysis of the reaction course of dehydration. Furthermore, cyclization is not tightly coupled to dehydration and follows at a later stage of the enzymatic reaction.

Original language	English (US)
Pages (from-to)	1420-1421
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	128
Issue number	5
DOIs	https://doi.org/10.1021/ja057203d
State	Published - Feb 8 2006

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

Online availability

10.1021/ja057203d

Library availability

Discover UIUC Full Text

Cite this

@article{3f96dd715ccc45108b5252423fb328e3,

title = "The dehydratase activity of lacticin 481 synthetase is highly processive",

abstract = "Lacticin 481 synthetase (LctM) is a bifunctional enzyme that undertakes dehydration and cyclization in the structural region of the pre-lacticin peptide (LctA) to introduce three thioether rings and one dehydrobutyrine residue. The order and timing of these events has been investigated employing high-resolution ESI-FTMS-based tandem MS/MS techniques and chemical derivatization. LctM demonstrates highly processive behavior as seen by MS analysis of the reaction course of dehydration. Furthermore, cyclization is not tightly coupled to dehydration and follows at a later stage of the enzymatic reaction.",

author = "Miller, {Leah M.} and Champak Chatterjee and {Van Der Donk}, {Wilfred A.} and Kelleher, {Neu L.}",

year = "2006",

month = feb,

day = "8",

doi = "10.1021/ja057203d",

language = "English (US)",

volume = "128",

pages = "1420--1421",

journal = "Journal of the American Chemical Society",

issn = "0002-7863",

publisher = "American Chemical Society",

number = "5",

}

TY - JOUR

T1 - The dehydratase activity of lacticin 481 synthetase is highly processive

AU - Miller, Leah M.

AU - Chatterjee, Champak

AU - Van Der Donk, Wilfred A.

AU - Kelleher, Neu L.

PY - 2006/2/8

Y1 - 2006/2/8

N2 - Lacticin 481 synthetase (LctM) is a bifunctional enzyme that undertakes dehydration and cyclization in the structural region of the pre-lacticin peptide (LctA) to introduce three thioether rings and one dehydrobutyrine residue. The order and timing of these events has been investigated employing high-resolution ESI-FTMS-based tandem MS/MS techniques and chemical derivatization. LctM demonstrates highly processive behavior as seen by MS analysis of the reaction course of dehydration. Furthermore, cyclization is not tightly coupled to dehydration and follows at a later stage of the enzymatic reaction.

AB - Lacticin 481 synthetase (LctM) is a bifunctional enzyme that undertakes dehydration and cyclization in the structural region of the pre-lacticin peptide (LctA) to introduce three thioether rings and one dehydrobutyrine residue. The order and timing of these events has been investigated employing high-resolution ESI-FTMS-based tandem MS/MS techniques and chemical derivatization. LctM demonstrates highly processive behavior as seen by MS analysis of the reaction course of dehydration. Furthermore, cyclization is not tightly coupled to dehydration and follows at a later stage of the enzymatic reaction.

UR - http://www.scopus.com/inward/record.url?scp=32244446657&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=32244446657&partnerID=8YFLogxK

U2 - 10.1021/ja057203d

DO - 10.1021/ja057203d

M3 - Article

C2 - 16448091

AN - SCOPUS:32244446657

SN - 0002-7863

VL - 128

SP - 1420

EP - 1421

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 5

ER -

The dehydratase activity of lacticin 481 synthetase is highly processive

Abstract

ASJC Scopus subject areas

Online availability

Library availability

Related links

Fingerprint

Cite this