Faculty Opinions recommendation of Identification and biochemical characterization of Arabidopsis thaliana sulfite oxidase. A new player in plant sulfur metabolism.

2002 ◽  
Author(s):  
Thomas Leustek
Keyword(s):  
Arabidopsis Thaliana ◽  
Biochemical Characterization ◽  
Sulfur Metabolism ◽  
Sulfite Oxidase

scholarly journals Biochemical characterization of the novel endo -β-mannanase At Man5-2 from Arabidopsis thaliana

Plant Science ◽  
2015 ◽  
Vol 241 ◽  
pp. 151-163 ◽  
Author(s):  
Yang Wang ◽  
Shoaib Azhar ◽  
Rosaria Gandini ◽  
Christina Divne ◽  
Ines Ezcurra ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Biochemical Characterization ◽  
The Novel

scholarly journals Discovery and characterization of a novel family of prokaryotic nanocompartments involved in sulfur metabolism

2020 ◽  
Author(s):  
Robert J. Nichols ◽  
Benjamin LaFrance ◽  
Naiya R. Phillips ◽  
Luke M. Oltrogge ◽  
Luis E. Valentin-Alvarado ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Biochemical Characterization ◽  
Sulfur Metabolism ◽  
Physiological Role ◽  
Enzymatic Characterization ◽  
Cysteine Desulfurase ◽  
Future Studies ◽  
Pcc 7942

AbstractProkaryotic nanocompartments, also known as encapsulins, are a recently discovered proteinaceous organelle in prokaryotes that compartmentalize cargo enzymes. While initial studies have begun to elucidate the structure and physiological roles of encapsulins, bioinformatic evidence suggests that a great diversity of encapsulin nanocompartments remains unexplored. Here, we describe a novel encapsulin in the freshwater cyanobacterium Synechococcus elongatus PCC 7942. This nanocompartment is upregulated upon sulfate starvation and encapsulates a cysteine desulfurase enzyme via an N-terminal targeting sequence. Using cryoelectron microscopy, we have determined the structure of the nanocompartment complex to 2.2 Å resolution. Lastly, biochemical characterization of the complex demonstrated that the activity of the cysteine desulfurase is enhanced upon encapsulation. Taken together, our discovery, structural analysis, and enzymatic characterization of this prokaryotic nanocompartment provide a foundation for future studies seeking to understand the physiological role of this encapsulin in various bacteria.

scholarly journals Functional and biochemical characterization of a recombinant Arabidopsis thaliana 3-deoxy-D-manno-octulosonate 8-phosphate synthase

2004 ◽  
Vol 381 (1) ◽  
pp. 185-193 ◽  
Author(s):  
Jing WU ◽  
Mayur A. PATEL ◽  
Appavu K. SUNDARAM ◽  
Ronald W. WOODARD
Keyword(s):  
Arabidopsis Thaliana ◽  
Molecular Mass ◽  
Biochemical Characterization ◽  
Dipicolinic Acid ◽  
Kinetic Studies ◽  
Maximum Activity ◽  
Reading Frame ◽  
Sequential Mechanism ◽  
Phosphate Synthase

An open reading frame, encoding for KDOPS (3-deoxy-D-manno-octulosonate 8-phosphate synthase), from Arabidopsis thaliana was cloned into a T7-driven expression vector. The protein was overexpressed in Escherichia coli and purified to homogeneity. Recombinant A. thaliana KDOPS, in solution, displays an apparent molecular mass of 76 kDa and a subunit molecular mass of 31.519 kDa. Unlike previously studied bacterial KDOPSs, which are tetrameric, A. thaliana KDOPS appears to be a dimer in solution. The optimum temperature of the enzyme is 65 °C and the optimum pH is 7.5, with a broad peak between pH 6.5 and 9.5 showing 90% of maximum activity. The enzyme cannot be inactivated by EDTA or dipicolinic acid treatment, nor it can be activated by a series of bivalent metal ions, suggesting that it is a non-metallo-enzyme, as opposed to the initial prediction that it would be a metallo-enzyme. Kinetic studies showed that the enzyme follows a sequential mechanism with Km=3.6 μM for phosphoenolpyruvate and 3.8 μM for D-arabinose 5-phosphate and kcat=5.9 s−1 at 37 °C. On the basis of the characterization of A. thaliana KDOPS and phylogenetic analysis, plant KDOPSs may represent a new, distinct class of KDOPSs.

scholarly journals Identification and biochemical characterization of the fructokinase gene family in Arabidopsis thaliana

2017 ◽  
Vol 17 (1) ◽  
Author(s):  
John W. Riggs ◽  
Philip C. Cavales ◽  
Sonia M. Chapiro ◽  
Judy Callis
Keyword(s):  
Arabidopsis Thaliana ◽  
Gene Family ◽  
Biochemical Characterization

Biochemical Characterization of Cytokinin Oxidases/Dehydrogenases from Arabidopsis thaliana Expressed in Nicotiana tabacum L.

2007 ◽  
Vol 26 (3) ◽  
pp. 255-267 ◽  
Author(s):  
Petr Galuszka ◽  
Hana Popelková ◽  
Tomáš Werner ◽  
Jitka Frébortová ◽  
Hana Pospíšilová ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Nicotiana Tabacum ◽  
Biochemical Characterization ◽  
Nicotiana Tabacum L

Biochemical characterization of Arabidopsis thaliana starch branching enzyme 2.2 reveals an enzymatic positive cooperativity

Biochimie ◽  
2017 ◽  
Vol 140 ◽  
pp. 146-158 ◽  
Author(s):  
A. Wychowski ◽  
C. Bompard ◽  
F. Grimaud ◽  
G. Potocki-Véronèse ◽  
C. D'Hulst ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Biochemical Characterization ◽  
Branching Enzyme ◽  
Starch Branching Enzyme ◽  
Positive Cooperativity

scholarly journals Biochemical Characterization of Plasma Membrane H+-ATPase Activation in Guard Cell Protoplasts of Arabidopsis thaliana in Response to Blue Light

2005 ◽  
Vol 46 (6) ◽  
pp. 955-963 ◽  
Author(s):  
Kumi Ueno ◽  
Toshinori Kinoshita ◽  
Shin-ichiro Inoue ◽  
Takashi Emi ◽  
Ken-ichiro Shimazaki
Keyword(s):  
Arabidopsis Thaliana ◽  
Plasma Membrane ◽  
Blue Light ◽  
Guard Cell ◽  
Biochemical Characterization ◽  
Guard Cell Protoplasts
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