Conversion of substrate analogs suggests a Michael cyclization in iridoid biosynthesis

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Conversion of substrate analogs suggests a Michael cyclization in iridoid biosynthesis. / Lindner, Stephanie; Geu Flores, Fernando; Bräse, Stefan; Sherden, Nathaniel H; O'Connor, Sarah E.

In: Chemistry & Biology, Vol. 21, No. 11, 2014, p. 1452-1456.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Lindner, S, Geu Flores, F, Bräse, S, Sherden, NH & O'Connor, SE 2014, 'Conversion of substrate analogs suggests a Michael cyclization in iridoid biosynthesis', Chemistry & Biology, vol. 21, no. 11, pp. 1452-1456. https://doi.org/10.1016/j.chembiol.2014.09.010

APA

Lindner, S., Geu Flores, F., Bräse, S., Sherden, N. H., & O'Connor, S. E. (2014). Conversion of substrate analogs suggests a Michael cyclization in iridoid biosynthesis. Chemistry & Biology, 21(11), 1452-1456. https://doi.org/10.1016/j.chembiol.2014.09.010

Vancouver

Lindner S, Geu Flores F, Bräse S, Sherden NH, O'Connor SE. Conversion of substrate analogs suggests a Michael cyclization in iridoid biosynthesis. Chemistry & Biology. 2014;21(11):1452-1456. https://doi.org/10.1016/j.chembiol.2014.09.010

Author

Lindner, Stephanie ; Geu Flores, Fernando ; Bräse, Stefan ; Sherden, Nathaniel H ; O'Connor, Sarah E. / Conversion of substrate analogs suggests a Michael cyclization in iridoid biosynthesis. In: Chemistry & Biology. 2014 ; Vol. 21, No. 11. pp. 1452-1456.

Bibtex

@article{66bb8f44b6d748d4b303b3fbdf82cf19,
title = "Conversion of substrate analogs suggests a Michael cyclization in iridoid biosynthesis",
abstract = "The core structure of the iridoid monoterpenes is formed by a unique cyclization reaction. The enzyme that catalyzes this reaction, iridoid synthase, is mechanistically distinct from other terpene cyclases. Here we describe the synthesis of two substrate analogs to probe the mechanism of iridoid synthase. Enzymatic assay of these substrate analogs along with clues from the product profile of the native substrate strongly suggest that iridoid synthase utilizes a Michael reaction to achieve cyclization. This improved mechanistic understanding will facilitate the exploitation of the potential of iridoid synthase to synthesize new cyclic compounds from nonnatural substrates.",
author = "Stephanie Lindner and {Geu Flores}, Fernando and Stefan Br{\"a}se and Sherden, {Nathaniel H} and O'Connor, {Sarah E}",
note = "Copyright {\textcopyright} 2014 The Authors. Published by Elsevier Ltd.. All rights reserved.",
year = "2014",
doi = "10.1016/j.chembiol.2014.09.010",
language = "English",
volume = "21",
pages = "1452--1456",
journal = "Chemistry and Biology",
issn = "2451-9448",
publisher = "Elsevier",
number = "11",

}

RIS

TY - JOUR

T1 - Conversion of substrate analogs suggests a Michael cyclization in iridoid biosynthesis

AU - Lindner, Stephanie

AU - Geu Flores, Fernando

AU - Bräse, Stefan

AU - Sherden, Nathaniel H

AU - O'Connor, Sarah E

N1 - Copyright © 2014 The Authors. Published by Elsevier Ltd.. All rights reserved.

PY - 2014

Y1 - 2014

N2 - The core structure of the iridoid monoterpenes is formed by a unique cyclization reaction. The enzyme that catalyzes this reaction, iridoid synthase, is mechanistically distinct from other terpene cyclases. Here we describe the synthesis of two substrate analogs to probe the mechanism of iridoid synthase. Enzymatic assay of these substrate analogs along with clues from the product profile of the native substrate strongly suggest that iridoid synthase utilizes a Michael reaction to achieve cyclization. This improved mechanistic understanding will facilitate the exploitation of the potential of iridoid synthase to synthesize new cyclic compounds from nonnatural substrates.

AB - The core structure of the iridoid monoterpenes is formed by a unique cyclization reaction. The enzyme that catalyzes this reaction, iridoid synthase, is mechanistically distinct from other terpene cyclases. Here we describe the synthesis of two substrate analogs to probe the mechanism of iridoid synthase. Enzymatic assay of these substrate analogs along with clues from the product profile of the native substrate strongly suggest that iridoid synthase utilizes a Michael reaction to achieve cyclization. This improved mechanistic understanding will facilitate the exploitation of the potential of iridoid synthase to synthesize new cyclic compounds from nonnatural substrates.

U2 - 10.1016/j.chembiol.2014.09.010

DO - 10.1016/j.chembiol.2014.09.010

M3 - Journal article

C2 - 25444551

VL - 21

SP - 1452

EP - 1456

JO - Chemistry and Biology

JF - Chemistry and Biology

SN - 2451-9448

IS - 11

ER -

ID: 130370571