A Comprehensive Gene Inventory for Glucosinolate Biosynthetic Pathway in Arabidopsis thaliana

2020 ◽  
Vol 68 (28) ◽  
pp. 7281-7297
Author(s):  
Sarahani Harun ◽  
Muhammad-Redha Abdullah-Zawawi ◽  
Hoe-Han Goh ◽  
Zeti-Azura Mohamed-Hussein
Keyword(s):  
Arabidopsis Thaliana ◽  
Biosynthetic Pathway

Caffeoyl Shikimate Esterase (CSE) Is an Enzyme in the Lignin Biosynthetic Pathway in Arabidopsis

Science ◽  
2013 ◽  
Vol 341 (6150) ◽  
pp. 1103-1106 ◽  
Author(s):  
Ruben Vanholme ◽  
Igor Cesarino ◽  
Katarzyna Rataj ◽  
Yuguo Xiao ◽  
Lisa Sundin ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Cell Walls ◽  
Metabolite Profiling ◽  
Biosynthetic Pathway ◽  
Wild Type ◽  
Secondary Cell Walls ◽  
Phenolic Metabolite ◽  
In The Wild ◽  
Lignin Biosynthetic Pathway

Lignin is a major component of plant secondary cell walls. Here we describe caffeoyl shikimate esterase (CSE) as an enzyme central to the lignin biosynthetic pathway. Arabidopsis thaliana cse mutants deposit less lignin than do wild-type plants, and the remaining lignin is enriched in p-hydroxyphenyl units. Phenolic metabolite profiling identified accumulation of the lignin pathway intermediate caffeoyl shikimate in cse mutants as compared to caffeoyl shikimate levels in the wild type, suggesting caffeoyl shikimate as a substrate for CSE. Accordingly, recombinant CSE hydrolyzed caffeoyl shikimate into caffeate. Associated with the changes in lignin, the conversion of cellulose to glucose in cse mutants increased up to fourfold as compared to that in the wild type upon saccharification without pretreatment. Collectively, these data necessitate the revision of currently accepted models of the lignin biosynthetic pathway.

scholarly journals The Simultaneous Repression of CCR and CAD, Two Enzymes of the Lignin Biosynthetic Pathway, Results in Sterility and Dwarfism in Arabidopsis thaliana

2011 ◽  
Vol 4 (1) ◽  
pp. 70-82 ◽  
Author(s):  
Johanne Thévenin ◽  
Brigitte Pollet ◽  
Bruno Letarnec ◽  
Luc Saulnier ◽  
Lionel Gissot ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Biosynthetic Pathway ◽  
Lignin Biosynthetic Pathway

Inactivation of genes, encoding tocopherol biosynthetic pathway enzymes, results in oxidative stress in outdoor grown Arabidopsis thaliana

2009 ◽  
Vol 47 (5) ◽  
pp. 384-390 ◽  
Author(s):  
Nadia M. Semchuk ◽  
Oleh V. Lushchak ◽  
Jon Falk ◽  
Karin Krupinska ◽  
Volodymyr I. Lushchak
Keyword(s):  
Oxidative Stress ◽  
Arabidopsis Thaliana ◽  
Biosynthetic Pathway ◽  
Genes Encoding

scholarly journals Reconstruction of the Transcriptional Regulatory Network in Arabidopsis thaliana Aliphatic Glucosinolate Biosynthetic Pathway

2018 ◽  
Vol 47 (12) ◽  
pp. 2993-3002
Author(s):  
Khalidah-Syahirah Ashari ◽  
Muhammad-Redha Abdullah-Zawawi ◽  
Sarahani Harun ◽  
Zeti-Azura Mohamed-Hussein
Keyword(s):  
Arabidopsis Thaliana ◽  
Regulatory Network ◽  
Biosynthetic Pathway ◽  
Transcriptional Regulatory Network ◽  
Transcriptional Regulatory ◽  
Aliphatic Glucosinolate

The carnitine biosynthetic pathway in Arabidopsis thaliana shares similar features with the pathway of mammals and fungi

2012 ◽  
Vol 60 ◽  
pp. 109-114 ◽  
Author(s):  
Sonia Rippa ◽  
Yingjuan Zhao ◽  
Franck Merlier ◽  
Aurélie Charrier ◽  
Yolande Perrin
Keyword(s):  
Arabidopsis Thaliana ◽  
Biosynthetic Pathway

scholarly journals Expression and crystallographic studies of theArabidopsis thalianaGDP-D-mannose pyrophosphorylase VTC1

2016 ◽  
Vol 72 (10) ◽  
pp. 795-798 ◽  
Author(s):  
Shun Zhao ◽  
Lin Liu
Keyword(s):  
Arabidopsis Thaliana ◽  
Ascorbic Acid ◽  
Vitamin C ◽  
Biosynthetic Pathway ◽  
Unit Cell ◽  
X Rays ◽  
Unit Cell Parameters ◽  
Space Group ◽  
Cell Parameters ◽  
Ligand Free

GDP-D-mannose pyrophosphorylase catalyzes the production of GDP-D-mannose, an intermediate product in the plant ascorbic acid (AsA) biosynthetic pathway. This enzyme is a key regulatory target in AsA biosynthesis and is encoded byVITAMIN C DEFECTIVE 1(VTC1) in theArabidopsis thalianagenome. Here, recombinant VTC1 was expressed, purified and crystallized. Diffraction data were obtained from VTC1 crystals grown in the absence and presence of substrate using X-rays. The ligand-free VTC1 crystal diffracted X-rays to 3.3 Å resolution and belonged to space groupR32, with unit-cell parametersa=b= 183.6,c= 368.5 Å, α = β = 90, γ = 120°; the crystal of VTC1 in the presence of substrate diffracted X-rays to 1.75 Å resolution and belonged to space groupP21, with unit-cell parametersa= 70.8,b= 83.9,c= 74.5 Å, α = γ = 90.0, β = 114.9°.

scholarly journals The Arabidopsis AtGCD3 protein is a glucosylceramidase that preferentially hydrolyzes long-acyl-chain glucosylceramides

2019 ◽  
Vol 295 (3) ◽  
pp. 717-728 ◽  
Author(s):  
Guang-Yi Dai ◽  
Jian Yin ◽  
Kai-En Li ◽  
Ding-Kang Chen ◽  
Zhe Liu ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Fusion Proteins ◽  
Biosynthetic Pathway ◽  
Acyl Chain ◽  
Specific Inhibitor ◽  
Endoplasmic Reticulum Membrane ◽  
Growth Defects ◽  
The Common

Cellular membranes contain many lipids, some of which, such as sphingolipids, have important structural and signaling functions. The common sphingolipid glucosylceramide (GlcCer) is present in plants, fungi, and animals. As a major plant sphingolipid, GlcCer is involved in the formation of lipid microdomains, and the regulation of GlcCer is key for acclimation to stress. Although the GlcCer biosynthetic pathway has been elucidated, little is known about GlcCer catabolism, and a plant GlcCer-degrading enzyme (glucosylceramidase (GCD)) has yet to be identified. Here, we identified AtGCD3, one of four Arabidopsis thaliana homologs of human nonlysosomal glucosylceramidase, as a plant GCD. We found that recombinant AtGCD3 has a low Km for the fluorescent lipid C6-NBD GlcCer and preferentially hydrolyzes long acyl-chain GlcCer purified from Arabidopsis leaves. Testing of inhibitors of mammalian glucosylceramidases revealed that a specific inhibitor of human β-glucosidase 2, N-butyldeoxynojirimycin, inhibits AtGCD3 more effectively than does a specific inhibitor of human β-glucosidase 1, conduritol β-epoxide. We also found that Glu-499 and Asp-647 in AtGCD3 are vital for GCD activity. GFP-AtGCD3 fusion proteins mainly localized to the plasma membrane or the endoplasmic reticulum membrane. No obvious growth defects or changes in sphingolipid contents were observed in gcd3 mutants. Our results indicate that AtGCD3 is a plant glucosylceramidase that participates in GlcCer catabolism by preferentially hydrolyzing long-acyl-chain GlcCers.

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