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PRISEs (progesterone 5β-reductase and/or iridoid synthase-like 1,4-enone reductases): Catalytic and substrate promiscuity allows for realization of multiple pathways in plant metabolism

https://doi.org/10.1016/j.phytochem.2018.08.012

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1038/nprot.2007.287zenodo-depositor-declared

Procedure for reductive methylation of protein to improve crystallizability

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Underground metabolism

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Recombinant Δ 4,5 ‐Steroid 5 β‐Reductases as Biocatalysts for the Reduction of Activated CC‐Double Bonds in Monocyclic and Acyclic Molecules

inferredcites →https://doi.org/10.1002/anie.201508310openalex-snapshot

Structures of Iridoid Synthase from Cantharanthus roseus with Bound NAD+, NADPH, or NAD+/10‐Oxogeranial: Reaction Mechanisms

inferredcites →https://doi.org/10.1002/ejoc.201200776openalex-snapshot

Nicotinamide‐Dependent Ene Reductases as Alternative Biocatalysts for the Reduction of Activated Alkenes

inferredcites →https://doi.org/10.1006/abio.1976.9999openalex-snapshot

A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding

inferredcites →https://doi.org/10.1007/978-1-4614-4063-5_29openalex-snapshot

Cardenolide Aglycone Formation in Digitalis

inferredcites →https://doi.org/10.1016/j.biochi.2008.12.005openalex-snapshot

The VEP1 gene (At4g24220) encodes a short-chain dehydrogenase/reductase with 3-oxo-Δ4,5-steroid 5β-reductase activity in Arabidopsis thaliana L.

inferredcites →https://doi.org/10.1016/j.jmb.2007.05.022openalex-snapshot

Inference of Macromolecular Assemblies from Crystalline State

inferredcites →https://doi.org/10.1016/j.jsb.2016.02.010openalex-snapshot

Structure of iridoid synthase in complex with NADP + /8-oxogeranial reveals the structural basis of its substrate specificity

inferredcites →https://doi.org/10.1016/j.molp.2014.11.005openalex-snapshot

Iridoid Synthase Activity Is Common among the Plant Progesterone 5β-Reductase Family

inferredcites →https://doi.org/10.1016/j.phytochem.2005.11.013openalex-snapshot

Molecular cloning and heterologous expression of progesterone 5β-reductase from Digitalis lanata Ehrh.

inferredcites →https://doi.org/10.1016/j.phytochem.2006.11.019openalex-snapshot

Plant progesterone 5β-reductase is not homologous to the animal enzyme. Molecular evolutionary characterization of P5βR from Digitalis purpurea

inferredcites →https://doi.org/10.1016/j.phytochem.2010.06.004openalex-snapshot

Highly conserved progesterone 5β-reductase genes (P5βR) from 5β-cardenolide-free and 5β-cardenolide-producing angiosperms

inferredcites →https://doi.org/10.1016/j.phytochem.2011.06.007openalex-snapshot

Progesterone 5β-reductase of Erysimum crepidifolium: cDNA cloning, expression in Escherichia coli, and reduction of enones with the recombinant protein

inferredcites →https://doi.org/10.1016/j.phytochem.2012.01.022openalex-snapshot

Vein Patterning 1-encoded progesterone 5β-reductase: Activity-guided improvement of catalytic efficiency

inferredcites →https://doi.org/10.1016/j.tibs.2014.12.004openalex-snapshot

An evolutionary biochemist's perspective on promiscuity

inferredcites →https://doi.org/10.1016/j.tibtech.2007.03.002openalex-snapshot

Enzyme promiscuity: mechanism and applications

inferredcites →https://doi.org/10.1016/s1016-8478(23)13368-1openalex-snapshot

Structure and Expression of the AWI 31 Gene Specifically Induced by Wounding in Arabidopsis thaliana

inferredcites →https://doi.org/10.1038/nature11692openalex-snapshot

An alternative route to cyclic terpenes by reductive cyclization in iridoid biosynthesis

inferredcites →https://doi.org/10.1038/nchembio.1955openalex-snapshot

Structural determinants of reductive terpene cyclization in iridoid biosynthesis

inferredcites →https://doi.org/10.1046/j.1365-313x.2003.01718.xopenalex-snapshot

Reactive electrophile species activate defense gene expression in Arabidopsis

inferredcites →https://doi.org/10.1055/s-2007-981537openalex-snapshot

Δ5-3β-Hydroxysteroid Dehydrogenase (3βHSD) from Digitalis lanata. Heterologous Expression and Characterisation of the Recombinant Enzyme

inferredcites →https://doi.org/10.1073/pnas.1406102111openalex-snapshot

Network-level architecture and the evolutionary potential of underground metabolism

inferredcites →https://doi.org/10.1074/jbc.m117.800979openalex-snapshot

Inverted stereocontrol of iridoid synthase in snapdragon

inferredcites →https://doi.org/10.1074/jbc.m706185200openalex-snapshot

The Crystal Structure of Progesterone 5β-Reductase from Digitalis lanata Defines a Novel Class of Short Chain Dehydrogenases/Reductases

inferredcites →https://doi.org/10.1080/07391102.2015.1088797openalex-snapshot

Progesterone 5β-reductases/iridoid synthases (PRISE): gatekeeper role of highly conserved phenylalanines in substrate preference and trapping is supported by molecular dynamics simulations

inferredcites →https://doi.org/10.1093/molbev/msm092openalex-snapshot

MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) Software Version 4.0

inferredcites →https://doi.org/10.1093/nar/gkq313openalex-snapshot

A new bioinformatics analysis tools framework at EMBL-EBI

inferredcites →https://doi.org/10.1093/nar/gku1214openalex-snapshot

The RCSB Protein Data Bank: views of structural biology for basic and applied research and education

inferredcites →https://doi.org/10.1093/pcp/pcf042openalex-snapshot

Involvement of the VEP1 Gene in Vascular Strand Development in Arabidopsis thaliana

inferredcites →https://doi.org/10.1107/s0021889807021206openalex-snapshot

Phaser crystallographic software

inferredcites →https://doi.org/10.1107/s0021889812011715openalex-snapshot

XDSAPP : a graphical user interface for the convenient processing of diffraction data using XDS

inferredcites →https://doi.org/10.1107/s0907444904026460openalex-snapshot

Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions

inferredcites →https://doi.org/10.1107/s0907444909052925openalex-snapshot

PHENIX : a comprehensive Python-based system for macromolecular structure solution

inferredcites →https://doi.org/10.1107/s0907444910007493openalex-snapshot

Features and development of Coot

inferredcites →https://doi.org/10.1110/ps.26902openalex-snapshot

Short‐chain dehydrogenase/reductase (SDR) relationships: A large family with eight clusters common to human, animal, and plant genomes

inferredcites →https://doi.org/10.1111/boj.12385openalex-snapshot

An update of the Angiosperm Phylogeny Group classification for the orders and families of flowering plants: APG IV

inferredcites →https://doi.org/10.1111/j.1432-1033.1994.1125b.xopenalex-snapshot

Purification, Characterization and Partial Peptide Microsequencing of Progesterone 5β‐Reductase from Shoot Cultures of Digitalis purpurea

inferredcites →https://doi.org/10.1111/j.1469-8137.2009.03080.xopenalex-snapshot

Digitalis purpurea P5βR2, encoding steroid 5β‐reductase, is a novel defense‐related gene involved in cardenolide biosynthesis

inferredcites →https://doi.org/10.1111/plb.12361openalex-snapshot

Progesterone 5β‐reductase genes of the B rassicaceae family as function‐associated molecular markers

inferredcites →https://doi.org/10.1146/annurev-biochem-030409-143718openalex-snapshot

Enzyme Promiscuity: A Mechanistic and Evolutionary Perspective

inferredcites →https://doi.org/10.1186/1471-2229-12-219openalex-snapshot

The Plant Short-Chain Dehydrogenase (SDR) superfamily: genome-wide inventory and diversification patterns

inferredcites →https://doi.org/10.1186/s40490-016-0063-1openalex-snapshot

The occurrence of progesterone 5β-reductase is not limited to the angiosperms: a functional gene was identified in Picea sitchensis and expressed in Escherichia coli

inferredcites →https://doi.org/10.1371/journal.pone.0022279openalex-snapshot

The Vein Patterning 1 (VEP1) Gene Family Laterally Spread through an Ecological Network

inferredcites →https://doi.org/10.3390/molecules22081387openalex-snapshot

Cloning and Characterization of Two Iridoid Synthase Homologs from Swertia Mussotii

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1002/mbo3.925openalex-snapshot

Biosynthetic approach to combine the first steps of cardenolide formation in Saccharomyces cerevisiae

inferred← citeshttps://doi.org/10.1007/s00299-021-02707-3openalex-snapshot

RNAi-mediated gene knockdown of progesterone 5β-reductases in Digitalis lanata reduces 5β-cardenolide content

inferred← citeshttps://doi.org/10.1007/s00425-022-03824-3openalex-snapshot

Identification and functional characterization of three iridoid synthases in Gardenia jasminoides

inferred← citeshttps://doi.org/10.1007/s00425-023-04287-wopenalex-snapshot

A fused hybrid enzyme of 8-hydroxygeraniol oxidoreductase (8HGO) from Gardenia jasminoides and iridoid synthase (ISY) from Catharanthus roseus significantly enhances nepetalactol and iridoid production

inferred← citeshttps://doi.org/10.1007/s11103-021-01220-1openalex-snapshot

Using interdisciplinary, phylogeny-guided approaches to understand the evolution of plant metabolism

inferred← citeshttps://doi.org/10.1016/j.enzmictec.2019.109483openalex-snapshot

Identification of key sites determining the cofactor specificity and improvement of catalytic activity of a steroid 5β-reductase from Capsella rubella

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Functional evidence for the partial conservation of arsenic tolerance mechanisms in Marchantia polymorpha and Arabidopsis thaliana

inferred← citeshttps://doi.org/10.1016/j.jsbmb.2022.106236openalex-snapshot

A novel steroid hydroxylase from Nigrospora sphaerica with various hydroxylation capabilities to different steroid substrates

inferred← citeshttps://doi.org/10.1016/j.ymben.2020.05.006openalex-snapshot

Cell-free prototyping of limonene biosynthesis using cell-free protein synthesis

inferred← citeshttps://doi.org/10.1021/acscatal.5c04685openalex-snapshot

Engineered Bacterial Progesterone 5β-Reductase: Tunable Substrate Preference and Synthesis of 5β-Dihydrosteroids

inferred← citeshttps://doi.org/10.1021/acschembio.0c00220openalex-snapshot

The Progesterone 5β-Reductase/Iridoid Synthase Family: A Catalytic Reservoir for Specialized Metabolism across Land Plants

inferred← citeshttps://doi.org/10.1039/d5np00050eopenalex-snapshot

Cardiac glycosides: structural diversity, chemical ecology, bioactivity, and artificial synthesis

inferred← citeshttps://doi.org/10.1093/jxb/erz025openalex-snapshot

Exploiting enzyme promiscuity to shape plant specialized metabolism

inferred← citeshttps://doi.org/10.1093/pcp/pcac144openalex-snapshot

Cardenolide Increase in Foxglove after 2,1,3-Benzothiadiazole Treatment Reveals a Potential Link between Cardenolide and Phytosterol Biosynthesis

inferred← citeshttps://doi.org/10.1093/pcp/pcae006openalex-snapshot

Progesterone Metabolism in Digitalis and Other Plants—60 Years of Research and Recent Results

inferred← citeshttps://doi.org/10.1093/plphys/kiad550openalex-snapshot

Citronellol biosynthesis in pelargonium is a multistep pathway involving progesterone 5β-reductase and/or iridoid synthase-like enzymes

inferred← citeshttps://doi.org/10.1101/2024.04.10.588904openalex-snapshot

Four enzymes control natural variation in the steroid core of Erysimum cardenolides

inferred← citeshttps://doi.org/10.1186/s12870-020-02529-7openalex-snapshot

Unveiling the genetic basis of Sclerotinia head rot resistance in sunflower

inferred← citeshttps://doi.org/10.3390/metabo12010011openalex-snapshot

Knockout of Arabidopsis thaliana VEP1, Encoding a PRISE (Progesterone 5β-Reductase/Iridoid Synthase-Like Enzyme), Leads to Metabolic Changes in Response to Exogenous Methyl Vinyl Ketone (MVK)

inferred← citeshttps://doi.org/10.3390/molecules29235788openalex-snapshot

Addressing the Evolution of Cardenolide Formation in Iridoid-Synthesizing Plants: Site-Directed Mutagenesis of PRISEs (Progesterone-5β-Reductase/Iridoid Synthase-like Enzymes) of Plantago Species

inferred← citeshttps://doi.org/10.70675/02a20883zee26z4f1dz84fcz2fac436faa25openalex-snapshot

Étude de la biosynthèse des terpènes et de leur régulation chez Pelargonium x hybridum

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