scholarly journals Cysteine Biosynthesis inTrichomonas vaginalisInvolves Cysteine Synthase UtilizingO-Phosphoserine

2006 ◽  
Vol 281 (35) ◽  
pp. 25062-25075 ◽  
Author(s):  
Gareth D. Westrop ◽  
Gordon Goodall ◽  
Jeremy C. Mottram ◽  
Graham H. Coombs
Keyword(s):  
Cysteine Biosynthesis ◽  
Cysteine Synthase

scholarly journals Allosterically Gated Enzyme Dynamics in the Cysteine Synthase Complex Regulate Cysteine Biosynthesis in Arabidopsis thaliana

Structure ◽  
2012 ◽  
Vol 20 (2) ◽  
pp. 292-302 ◽  
Author(s):  
Anna Feldman-Salit ◽  
Markus Wirtz ◽  
Esther D. Lenherr ◽  
Christian Throm ◽  
Michael Hothorn ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Cysteine Biosynthesis ◽  
Enzyme Dynamics ◽  
Cysteine Synthase

scholarly journals Structure ofLeishmania majorcysteine synthase

2012 ◽  
Vol 68 (7) ◽  
pp. 738-743 ◽  
Author(s):  
Paul K. Fyfe ◽  
Gareth D. Westrop ◽  
Tania Ramos ◽  
Sylke Müller ◽  
Graham H. Coombs ◽  
...  
Keyword(s):  
Active Site ◽  
Pyridoxal Phosphate ◽  
Biochemical Study ◽  
Molecular Replacement ◽  
Cysteine Biosynthesis ◽  
Asymmetric Unit ◽  
Serine Acetyltransferase ◽  
Cysteine Synthase ◽  
Enzyme Active Site ◽  
C Terminus

Cysteine biosynthesis is a potential target for drug development against parasiticLeishmaniaspecies; these protozoa are responsible for a range of serious diseases. To improve understanding of this aspect ofLeishmaniabiology, a crystallographic and biochemical study ofL. majorcysteine synthase has been undertaken, seeking to understand its structure, enzyme activity and modes of inhibition. Active enzyme was purified, assayed and crystallized in an orthorhombic form with a dimer in the asymmetric unit. Diffraction data extending to 1.8 Å resolution were measured and the structure was solved by molecular replacement. A fragment of γ-poly-D-glutamic acid, a constituent of the crystallization mixture, was bound in the enzyme active site. Although a D-glutamate tetrapeptide had insignificant inhibitory activity, the enzyme was competitively inhibited (Ki= 4 µM) by DYVI, a peptide based on the C-terminus of the partner serine acetyltransferase with which the enzyme forms a complex. The structure surprisingly revealed that the cofactor pyridoxal phosphate had been lost during crystallization.

scholarly journals Modulation of Cysteine Biosynthesis in Chloroplasts of Transgenic Tobacco Overexpressing Cysteine Synthase [O-Acetylserine(thiol)-Iyase]

1994 ◽  
Vol 106 (3) ◽  
pp. 887-895 ◽  
Author(s):  
K. Saito ◽  
M. Kurosawa ◽  
K. Tatsuguchi ◽  
Y. Takagi ◽  
I. Murakoshi
Keyword(s):  
Transgenic Tobacco ◽  
Cysteine Biosynthesis ◽  
Cysteine Synthase

Structure-based mutational studies of O-acetylserine sulfhydrylase reveal the reason for the loss of cysteine synthase complex formation in Brucella abortus

2017 ◽  
Vol 474 (7) ◽  
pp. 1221-1239 ◽  
Author(s):  
Sudhaker Dharavath ◽  
Isha Raj ◽  
Samudrala Gourinath
Keyword(s):  
Surface Plasmon Resonance ◽  
Complex Formation ◽  
Surface Plasmon ◽  
Brucella Abortus ◽  
Active Site ◽  
Cysteine Biosynthesis ◽  
Protozoan Parasites ◽  
Serine Acetyltransferase ◽  
Cysteine Synthase ◽  
Active Site Pocket

Cysteine biosynthesis takes place via a two-step pathway in bacteria, fungi, plants and protozoan parasites, but not in humans, and hence, the machinery of cysteine biosynthesis is an opportune target for therapeutics. The decameric cysteine synthase complex (CSC) is formed when the C-terminal tail of serine acetyltransferase (SAT) binds in the active site of O-acetylserine sulfydrylase (OASS), playing a role in the regulation of this pathway. Here, we show that OASS from Brucella abortus (BaOASS) does not interact with its cognate SAT C-terminal tail. Crystal structures of native BaOASS showed that residues Gln96 and Tyr125 occupy the active-site pocket and interfere with the entry of the SAT C-terminal tail. The BaOASS (Q96A–Y125A) mutant showed relatively strong binding (Kd = 32.4 μM) to BaSAT C-terminal peptides in comparison with native BaOASS. The mutant structure looks similar except that the active-site pocket has enough space to bind the SAT C-terminal end. Surface plasmon resonance results showed a relatively strong (7.3 μM Kd) interaction between BaSAT and the BaOASS (Q96A–Y125A), but no interaction with native BaOASS. Taken together, our observations suggest that the CSC does not form in B. abortus.

scholarly journals A molecular switch in sulfur metabolism to reduce arsenic and enrich selenium in rice grain

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Sheng-Kai Sun ◽  
Xuejie Xu ◽  
Zhong Tang ◽  
Zhu Tang ◽  
Xin-Yuan Huang ◽  
...  
Keyword(s):  
Grain Quality ◽  
Sulfur Metabolism ◽  
Physical Interaction ◽  
Rice Grain ◽  
Yield Losses ◽  
Serine Acetyltransferase ◽  
Cysteine Synthase ◽  
Arsenic Tolerance ◽  
Arsenic Accumulation ◽  
Low Levels

AbstractRice grains typically contain high levels of toxic arsenic but low levels of the essential micronutrient selenium. Anthropogenic arsenic contamination of paddy soils exacerbates arsenic toxicity in rice crops resulting in substantial yield losses. Here, we report the identification of the gain-of-function arsenite tolerant 1 (astol1) mutant of rice that benefits from enhanced sulfur and selenium assimilation, arsenic tolerance, and decreased arsenic accumulation in grains. The astol1 mutation promotes the physical interaction of the chloroplast-localized O-acetylserine (thiol) lyase protein with its interaction partner serine-acetyltransferase in the cysteine synthase complex. Activation of the serine-acetyltransferase in this complex promotes the uptake of sulfate and selenium and enhances the production of cysteine, glutathione, and phytochelatins, resulting in increased tolerance and decreased translocation of arsenic to grains. Our findings uncover the pivotal sensing-function of the cysteine synthase complex in plastids for optimizing stress resilience and grain quality by regulating a fundamental macronutrient assimilation pathway.

scholarly journals Spermatogonial Gene Networks Selectively Couple to Glutathione and Pentose Phosphate Metabolism but not Cysteine Biosynthesis

iScience ◽  
2020 ◽  
pp. 101880
Author(s):  
David Prokai ◽  
Ashutosh Pudasaini ◽  
Mohammed Kanchwala ◽  
Andrew T. Moehlman ◽  
Alexandrea E. Waites ◽  
...  
Keyword(s):  
Gene Networks ◽  
Pentose Phosphate ◽  
Phosphate Metabolism ◽  
Cysteine Biosynthesis
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