Structural determinants of reductive terpene cyclization in iridoid biosynthesis

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

Standard

Structural determinants of reductive terpene cyclization in iridoid biosynthesis. / Kries, Hajo; Caputi, Lorenzo; Stevenson, Clare E M; Kamileen, Mohammed O; Sherden, Nathaniel H; Geu-Flores, Fernando; Lawson, David M; O'Connor, Sarah E.

In: Nature Chemical Biology, Vol. 12, No. 1, 2016, p. 6-8.

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

Harvard

Kries, H, Caputi, L, Stevenson, CEM, Kamileen, MO, Sherden, NH, Geu-Flores, F, Lawson, DM & O'Connor, SE 2016, 'Structural determinants of reductive terpene cyclization in iridoid biosynthesis', Nature Chemical Biology, vol. 12, no. 1, pp. 6-8. https://doi.org/10.1038/nchembio.1955

APA

Kries, H., Caputi, L., Stevenson, C. E. M., Kamileen, M. O., Sherden, N. H., Geu-Flores, F., Lawson, D. M., & O'Connor, S. E. (2016). Structural determinants of reductive terpene cyclization in iridoid biosynthesis. Nature Chemical Biology, 12(1), 6-8. https://doi.org/10.1038/nchembio.1955

Vancouver

Kries H, Caputi L, Stevenson CEM, Kamileen MO, Sherden NH, Geu-Flores F et al. Structural determinants of reductive terpene cyclization in iridoid biosynthesis. Nature Chemical Biology. 2016;12(1):6-8. https://doi.org/10.1038/nchembio.1955

Author

Kries, Hajo ; Caputi, Lorenzo ; Stevenson, Clare E M ; Kamileen, Mohammed O ; Sherden, Nathaniel H ; Geu-Flores, Fernando ; Lawson, David M ; O'Connor, Sarah E. / Structural determinants of reductive terpene cyclization in iridoid biosynthesis. In: Nature Chemical Biology. 2016 ; Vol. 12, No. 1. pp. 6-8.

Bibtex

@article{67b861927a8c48b6814cc8c5315cc0c1,
title = "Structural determinants of reductive terpene cyclization in iridoid biosynthesis",
abstract = "The carbon skeleton of ecologically and pharmacologically important iridoid monoterpenes is formed in a reductive cyclization reaction unrelated to canonical terpene cyclization. Here we report the crystal structure of the recently discovered iridoid cyclase (from Catharanthus roseus) bound to a mechanism-inspired inhibitor that illuminates substrate binding and catalytic function of the enzyme. Key features that distinguish iridoid synthase from its close homolog progesterone 5β-reductase are highlighted.",
keywords = "Catharanthus, Crystallography, X-Ray, Cyclization, Iridoids, Models, Molecular, Oxidoreductases, Plant Proteins, Protein Conformation, Terpenes, Journal Article, Research Support, Non-U.S. Gov't",
author = "Hajo Kries and Lorenzo Caputi and Stevenson, {Clare E M} and Kamileen, {Mohammed O} and Sherden, {Nathaniel H} and Fernando Geu-Flores and Lawson, {David M} and O'Connor, {Sarah E}",
year = "2016",
doi = "10.1038/nchembio.1955",
language = "English",
volume = "12",
pages = "6--8",
journal = "Nature Chemical Biology",
issn = "1552-4450",
publisher = "nature publishing group",
number = "1",

}

RIS

TY - JOUR

T1 - Structural determinants of reductive terpene cyclization in iridoid biosynthesis

AU - Kries, Hajo

AU - Caputi, Lorenzo

AU - Stevenson, Clare E M

AU - Kamileen, Mohammed O

AU - Sherden, Nathaniel H

AU - Geu-Flores, Fernando

AU - Lawson, David M

AU - O'Connor, Sarah E

PY - 2016

Y1 - 2016

N2 - The carbon skeleton of ecologically and pharmacologically important iridoid monoterpenes is formed in a reductive cyclization reaction unrelated to canonical terpene cyclization. Here we report the crystal structure of the recently discovered iridoid cyclase (from Catharanthus roseus) bound to a mechanism-inspired inhibitor that illuminates substrate binding and catalytic function of the enzyme. Key features that distinguish iridoid synthase from its close homolog progesterone 5β-reductase are highlighted.

AB - The carbon skeleton of ecologically and pharmacologically important iridoid monoterpenes is formed in a reductive cyclization reaction unrelated to canonical terpene cyclization. Here we report the crystal structure of the recently discovered iridoid cyclase (from Catharanthus roseus) bound to a mechanism-inspired inhibitor that illuminates substrate binding and catalytic function of the enzyme. Key features that distinguish iridoid synthase from its close homolog progesterone 5β-reductase are highlighted.

KW - Catharanthus

KW - Crystallography, X-Ray

KW - Cyclization

KW - Iridoids

KW - Models, Molecular

KW - Oxidoreductases

KW - Plant Proteins

KW - Protein Conformation

KW - Terpenes

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1038/nchembio.1955

DO - 10.1038/nchembio.1955

M3 - Journal article

C2 - 26551396

VL - 12

SP - 6

EP - 8

JO - Nature Chemical Biology

JF - Nature Chemical Biology

SN - 1552-4450

IS - 1

ER -

ID: 164345624