scholarly journals Theβ-cyanoalanine synthase pathway: beyond cyanide detoxification

2016 ◽  
Vol 39 (10) ◽  
pp. 2329-2341 ◽  
Author(s):  
Marylou Machingura ◽  
Eitan Salomon ◽  
Joseph M. Jez ◽  
Stephen D. Ebbs
Keyword(s):  
Cyanide Detoxification ◽  
Cyanoalanine Synthase

scholarly journals RETRACTED ARTICLE: Beta-cyanoalanine synthase pathway as a homeostatic mechanism for cyanide detoxification as well as growth and development in higher plants

Planta ◽  
2016 ◽  
Vol 245 (1) ◽  
pp. 235-235 ◽  
Author(s):  
Hafiz Mamoon Rehman ◽  
Zahid Hussain Shah ◽  
Muhammad Amjad Nawaz ◽  
Muhammad Qadir Ahmad ◽  
Seung Hwan Yang ◽  
...  
Keyword(s):  
Growth And Development ◽  
Higher Plants ◽  
Homeostatic Mechanism ◽  
Cyanide Detoxification ◽  
Retracted Article ◽  
Cyanoalanine Synthase

Quinclorac resistance in Echinochloa phyllopogon is associated with reduced ethylene synthesis rather than enhanced cyanide detoxification by β‐cyanoalanine synthase

2019 ◽  
Vol 76 (4) ◽  
pp. 1195-1204 ◽  
Author(s):  
Pattarasuda Chayapakdee ◽  
Yukari Sunohara ◽  
Masaki Endo ◽  
Takuya Yamaguchi ◽  
Longjiang Fan ◽  
...  
Keyword(s):  
Ethylene Synthesis ◽  
Cyanide Detoxification ◽  
Cyanoalanine Synthase ◽  
Echinochloa Phyllopogon

3-Mercaptopyruvate sulfurtransferase: an enzyme at the crossroads of sulfane sulfur trafficking

2020 ◽  
Vol 0 (0) ◽  
Author(s):  
Brandán Pedre ◽  
Tobias P. Dick
Keyword(s):  
Oxidative Stress ◽  
Metabolic Disease ◽  
Hydrogen Sulfide ◽  
Fatty Acid ◽  
Stress Resistance ◽  
Respiratory Function ◽  
Acid Metabolism ◽  
Cyanide Detoxification ◽  
Mercaptopyruvate Sulfurtransferase ◽  
Sulfur Trafficking

Abstract3-Mercaptopyruvate sulfurtransferase (MPST) catalyzes the desulfuration of 3-mercaptopyruvate to generate an enzyme-bound hydropersulfide. Subsequently, MPST transfers the persulfide’s outer sulfur atom to proteins or small molecule acceptors. MPST activity is known to be involved in hydrogen sulfide generation, tRNA thiolation, protein urmylation and cyanide detoxification. Tissue-specific changes in MPST expression correlate with ageing and the development of metabolic disease. Deletion and overexpression experiments suggest that MPST contributes to oxidative stress resistance, mitochondrial respiratory function and the regulation of fatty acid metabolism. However, the role and regulation of MPST in the larger physiological context remain to be understood.

scholarly journals Beta-cyanoalanine synthase: purification and characterization.

1975 ◽  
Vol 72 (4) ◽  
pp. 1617-1621 ◽  
Author(s):  
T. N. Akopyan ◽  
A. E. Braunstein ◽  
E. V. Goryachenkova
Keyword(s):  
Purification And Characterization ◽  
Cyanoalanine Synthase

Purification and biochemical characterization of a β-cyanoalanine synthase expressed in germinating seeds of Sorghum bicolor (L.) moench

2018 ◽  
Vol 43 (6) ◽  
pp. 638-650
Author(s):  
Ruth Ololade Amiola ◽  
Adedeji Nelson Ademakinwa ◽  
Zainab Adenike Ayinla ◽  
Esther Nkechi Ezima ◽  
Femi Kayode Agboola
Keyword(s):  
Kinetic Parameters ◽  
Biochemical Characterization ◽  
Catalytic Properties ◽  
Specific Activity ◽  
Biochemical Properties ◽  
Subunit Molecular Weight ◽  
Cyanoalanine Synthase ◽  
Germinating Seeds ◽  
Sorghum Bicolor L

Abstract Background β-Cyanoalanine synthase plays essential roles in germinating seeds, such as in cyanide homeostasis. Methods β-Cyanoalanine synthase was isolated from sorghum seeds, purified using chromatographic techniques and its biochemical and catalytic properties were determined. Results The purified enzyme had a yield of 61.74% and specific activity of 577.50 nmol H2S/min/mg of protein. The apparent and subunit molecular weight for purified β-cyanoalanine synthase were 58.26±2.41 kDa and 63.4 kDa, respectively. The kinetic parameters with sodium cyanide as substrate were 0.67±0.08 mM, 17.60±0.50 nmol H2S/mL/min, 2.97×10−1 s−1 and 4.43×102 M−1 s−1 for KM, Vmax, kcat and kcat/KM, respectively. With L-cysteine as substrate, the kinetic parameters were 2.64±0.37 mM, 63.41±4.04 nmol H2S/mL/min, 10.71×10−1 s−1 and 4.06×102 M−1 s−1 for KM, Vmax, kcat and kcat/KM, respectively. The optimum temperature and pH for activity were 35°C and 8.5, respectively. The enzyme retained more than half of its activity at 40°C. Inhibitors such as HgCl2, EDTA, glycine and iodoacetamide reduced enzyme activity. Conclusion The biochemical properties of β-cyanoalanine synthase in germinating sorghum seeds highlights its roles in maintaining cyanide homeostasis.

scholarly journals β-Cyanoalanine Synthase Is a Mitochondrial Cysteine Synthase-Like Protein in Spinach and Arabidopsis

2000 ◽  
Vol 123 (3) ◽  
pp. 1163-1172 ◽  
Author(s):  
Yves Hatzfeld ◽  
Akiko Maruyama ◽  
Ahlert Schmidt ◽  
Masaaki Noji ◽  
Kimiharu Ishizawa ◽  
...  
Keyword(s):  
Cysteine Synthase ◽  
Cyanoalanine Synthase
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