Bioinformatics analysis of enzymes involved in cysteine biosynthesis: first evidence for the formation of cysteine synthase complex in cyanobacteria

3 Biotech ◽  
2021 ◽  
Vol 11 (7) ◽  
Author(s):  
Surbhi Kharwar ◽  
Samujjal Bhattacharjee ◽  
Arun Kumar Mishra
Keyword(s):  
Bioinformatics Analysis ◽  
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 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 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.

Identification and Bioinformatics Analysis of Cysteine Synthase from the Filamentous Fungus, Monascus purpureus

2014 ◽  
Vol 522-524 ◽  
pp. 272-275
Author(s):  
Nan Qing Liao ◽  
Jiang Ning Yao ◽  
Hao Ming Li
Keyword(s):  
Amino Acid ◽  
Pyridoxal Phosphate ◽  
Structural Model ◽  
Bioinformatics Analysis ◽  
Tertiary Structure ◽  
Monascus Purpureus ◽  
Gene Encoding ◽  
Cysteine Synthase ◽  
Comparison Results ◽  
Alignment Analysis

A gene encoding a putative cysteine synthase was obtained by screening Monascus purpureus cDNA library. Bioinformatics analysis showed that this protein has Rhodanese Homology Domain in C-terminal, and Pyridoxal-phosphate dependent enzyme domain in N-terminal, and CBS-like structure. The deduced cysteine synthase protein of M. purpureus contained 517 amino acid, with molecular mass of 57,044Da. Sequence alignment analysis revealed that M. purpureus deduced cysteine synthase was closely related to cysteine synthase from Aspergillus, Ajellomyces and Paracoccidioides, and highly homologous to aforementioned and other known cysteine synthase. The structural model of the deduced cysteine synthase closely match the template with 100% confidence and 20-30% identity. The consistency of the comparison results of the primary structure, secondary structure and tertiary structure suggests that the dedued protein may well be cysteine synthase.

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