Plant nitrilase: a new job for an old enzyme

2019 ◽  
Vol 476 (7) ◽  
pp. 1105-1107
Author(s):  
Joseph M. Jez
Keyword(s):  
Arabidopsis Thaliana ◽  
Recent Work ◽  
Carboxylic Acids ◽  
Auxin Biosynthesis ◽  
Biological Functions ◽  
Repair Enzyme ◽  
Biochemical Journal ◽  
Metabolite Repair

Abstract Nitrilases are versatile enzymes that hydrolyze nitriles to carboxylic acids and ammonia, but many members of this family lack defined biological functions. In plants, nitrilases have been associated with detoxification of cyanide-containing compounds and auxin biosynthesis; however, recent work suggests that the chemical versatility of these proteins contributes to metabolite repair. In this issue of the Biochemical Journal, Niehaus et al. demonstrate that the Nit1 nitrilase from Arabidopsis thaliana functions as a metabolite repair enzyme that removes deaminated glutathione from the cytoplasm and plastids.

scholarly journals Crystal Structure of Nitrilase-Like Protein Nit2 from Kluyveromyces lactis

Crystals ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 499
Author(s):  
Chaewon Jin ◽  
Hyeonseok Jin ◽  
Byung-Cheon Jeong ◽  
Dong-Hyung Cho ◽  
Hang-Suk Chun ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Posttranslational Modifications ◽  
Tumor Suppressors ◽  
Kluyveromyces Lactis ◽  
Structural Features ◽  
Biological Functions ◽  
Repair Enzyme ◽  
Amidase Activity ◽  
Structural Relationships ◽  
Metabolite Repair

The nitrilase superfamily, including 13 branches, plays various biological functions in signaling molecule synthesis, vitamin metabolism, small-molecule detoxification, and posttranslational modifications. Most of the mammals and yeasts have Nit1 and Nit2 proteins, which belong to the nitrilase-like (Nit) branch of the nitrilase superfamily. Recent studies have suggested that Nit1 is a metabolite repair enzyme, whereas Nit2 shows ω-amidase activity. In addition, Nit1 and Nit2 are suggested as putative tumor suppressors through different ways in mammals. Yeast Nit2 (yNit2) is a homolog of mouse Nit1 based on similarity in sequence. To understand its specific structural features, we determined the crystal structure of Nit2 from Kluyveromyces lactis (KlNit2) at 2.2 Å resolution and compared it with the structure of yeast-, worm-, and mouse-derived Nit2 proteins. Based on our structural analysis, we identified five distinguishable structural features from 28 structural homologs. This study might potentially provide insights into the structural relationships of a broad spectrum of nitrilases.

Indole glucosinolate and auxin biosynthesis in Arabidopsis thaliana (L.) Heynh. glucosinolate mutants and the development of clubroot disease

Planta ◽  
1999 ◽  
Vol 208 (3) ◽  
pp. 409-419 ◽  
Author(s):  
Jutta Ludwig-Müller ◽  
Kerstin Pieper ◽  
Manfred Ruppel ◽  
Jerry D. Cohen ◽  
Ephraim Epstein ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Auxin Biosynthesis ◽  
Clubroot Disease ◽  
Indole Glucosinolate

scholarly journals Identification of phosphosites that alter protein thermal stability

2020 ◽  
Author(s):  
Ian R. Smith ◽  
Kyle N. Hess ◽  
Anna A. Bakhtina ◽  
Anthony S. Valente ◽  
Ricard A. Rodríguez-Mias ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Protein Structure ◽  
Protein Phosphorylation ◽  
Recent Work ◽  
Biochemical Changes ◽  
Phosphorylation Sites ◽  
Biological Functions ◽  
Protein Thermal Stability ◽  
The Difference

ABSTRACTProteomics has enabled the cataloguing of 100,000s of protein phosphorylation sites 1, however we lack methods to systematically annotate their function. Phosphorylation has numerous biological functions, yet biochemically all involve changes in protein structure and interactions. These biochemical changes can be recapitulated by measuring the difference in stability between the protein and the phosphoprotein. Building on recent work, we present a method to infer phosphosite functionality by reliably measuring such differences at the proteomic scale.

scholarly journals Ethylenediaminetetraacetic acid promotes the accumulation of nitric oxide

2020 ◽  
Author(s):  
Shizhong Zhang ◽  
Shasha Liu ◽  
Shenghui Xiao ◽  
Min Li ◽  
Jinguang Huang ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Arabidopsis Thaliana ◽  
Ethylenediaminetetraacetic Acid ◽  
Biological Systems ◽  
Chelating Agent ◽  
Current Understanding ◽  
Biological Functions ◽  
Chelating Activity

AbstractEthylenediaminetetraacetic acid (EDTA) is a well-established chelating agent used in industry, agriculture, food, and medicine. However, the analysis of an EDTA-sensitive Arabidopsis thaliana mutant revealed that EDTA can significantly promote nitric oxide (NO) accumulation, indicating that EDTA has unexpected biological functions beyond its chelating activity. This finding challenges our current understanding about the effects of EDTA on biological systems.One Sentence SummaryAn analysis of ethylenediaminetetraacetic acid (EDTA)-sensitive mutants suggests that EDTA can promote the accumulation of nitric oxide.

scholarly journals The Metabolite Repair Enzyme Phosphoglycolate Phosphatase Regulates Central Carbon Metabolism and Fosmidomycin Sensitivity in Plasmodium falciparum

mBio ◽  
2019 ◽  
Vol 10 (6) ◽  
Author(s):  
Laure Dumont ◽  
Mark B. Richardson ◽  
Phillip van der Peet ◽  
Danushka S. Marapana ◽  
Tony Triglia ◽  
...  
Keyword(s):  
Pentose Phosphate Pathway ◽  
Carbon Metabolism ◽  
Central Carbon Metabolism ◽  
Pentose Phosphate ◽  
Repair Enzyme ◽  
Content Type ◽  
Phosphoglycolate Phosphatase ◽  
Central Carbon ◽  
Metabolite Repair ◽  
By Products

ABSTRACT Members of the haloacid dehalogenase (HAD) family of metabolite phosphatases play an important role in regulating multiple pathways in Plasmodium falciparum central carbon metabolism. We show that the P. falciparum HAD protein, phosphoglycolate phosphatase (PGP), regulates glycolysis and pentose pathway flux in asexual blood stages via detoxifying the damaged metabolite 4-phosphoerythronate (4-PE). Disruption of the P. falciparum pgp gene caused accumulation of two previously uncharacterized metabolites, 2-phospholactate and 4-PE. 4-PE is a putative side product of the glycolytic enzyme, glyceraldehyde-3-phosphate dehydrogenase, and its accumulation inhibits the pentose phosphate pathway enzyme, 6-phosphogluconate dehydrogenase (6-PGD). Inhibition of 6-PGD by 4-PE leads to an unexpected feedback response that includes increased flux into the pentose phosphate pathway as a result of partial inhibition of upper glycolysis, with concomitant increased sensitivity to antimalarials that target pathways downstream of glycolysis. These results highlight the role of metabolite detoxification in regulating central carbon metabolism and drug sensitivity of the malaria parasite. IMPORTANCE The malaria parasite has a voracious appetite, requiring large amounts of glucose and nutrients for its rapid growth and proliferation inside human red blood cells. The host cell is resource rich, but this is a double-edged sword; nutrient excess can lead to undesirable metabolic reactions and harmful by-products. Here, we demonstrate that the parasite possesses a metabolite repair enzyme (PGP) that suppresses harmful metabolic by-products (via substrate dephosphorylation) and allows the parasite to maintain central carbon metabolism. Loss of PGP leads to the accumulation of two damaged metabolites and causes a domino effect of metabolic dysregulation. Accumulation of one damaged metabolite inhibits an essential enzyme in the pentose phosphate pathway, leading to substrate accumulation and secondary inhibition of glycolysis. This work highlights how the parasite coordinates metabolic flux by eliminating harmful metabolic by-products to ensure rapid proliferation in its resource-rich niche.

Structural insight into the biological functions of Arabidopsis thaliana ACHT1

2020 ◽  
Vol 158 ◽  
pp. 43-51
Author(s):  
Junchao Wang ◽  
Weimin Pan ◽  
Wenguang Cai ◽  
Mingzhu Wang ◽  
Lin Liu ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Biological Functions ◽  
Structural Insight ◽  
Insight Into

scholarly journals The Arabidopsis thaliana STYLISH1 Protein Acts as a Transcriptional Activator Regulating Auxin Biosynthesis

2010 ◽  
Vol 22 (2) ◽  
pp. 349-363 ◽  
Author(s):  
D. Magnus Eklund ◽  
Veronika Ståldal ◽  
Isabel Valsecchi ◽  
Izabela Cierlik ◽  
Caitriona Eriksson ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Transcriptional Activator ◽  
Auxin Biosynthesis

scholarly journals Adult Neurogenesis Supports Short-Term Olfactory Memory

2010 ◽  
Vol 103 (6) ◽  
pp. 2935-2937 ◽  
Author(s):  
Benjamin R. Arenkiel
Keyword(s):  
Recent Work ◽  
Adult Neurogenesis ◽  
Functional Role ◽  
Biological Functions ◽  
Short Term ◽  
Olfactory Memory ◽  
Brain Repair

Adult neurogenesis has captivated neuroscientists for decades, with hopes that understanding the programs underlying this phenomenon may provide unique insight toward avenues for brain repair. Interestingly, however, despite intense molecular and cellular investigation, the evolutionary roles and biological functions for ongoing neurogenesis have remained elusive. Here I review recent work published in the Journal of Neuroscience that reveals a functional role for continued neurogenesis toward forming short-term olfactory memories.

scholarly journals Crystal structure of Arabidopsis thaliana casein kinase 2 α1

2020 ◽  
Vol 76 (4) ◽  
pp. 182-191
Author(s):  
Manon Demulder ◽  
Lieven De Veylder ◽  
Remy Loris
Keyword(s):  
Crystal Structure ◽  
Arabidopsis Thaliana ◽  
Model System ◽  
Casein Kinase ◽  
Casein Kinase 2 ◽  
Body Motion ◽  
Biological Functions ◽  
Α Subunit ◽  
Crystal Forms

Casein kinase 2 (CK2) is a ubiquitous pleiotropic enzyme that is highly conserved across eukaryotic kingdoms. CK2 is singular amongst kinases as it is highly rigid and constitutively active. Arabidopsis thaliana is widely used as a model system in molecular plant research; the biological functions of A. thaliana CK2 are well studied in vivo and many of its substrates have been identified. Here, crystal structures of the α subunit of A. thaliana CK2 in three crystal forms and of its complex with the nonhydrolyzable ATP analog AMppNHp are presented. While the C-lobe of the enzyme is highly rigid, structural plasticity is observed for the N-lobe. Small but significant displacements within the active cleft are necessary in order to avoid steric clashes with the AMppNHp molecule. Binding of AMppNHp is influenced by a rigid-body motion of the N-lobe that was not previously recognized in maize CK2.

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