A novel O‐phospho‐L‐serine sulfhydrylation reaction catalyzed by O‐acetylserine sulfhydrylase from Aeropyrum pernix K1
@article{Mino2003ANO, title={A novel O‐phospho‐L‐serine sulfhydrylation reaction catalyzed by O‐acetylserine sulfhydrylase from Aeropyrum pernix K1}, author={Koshiki Mino and Kazuhiko Ishikawa}, journal={FEBS Letters}, year={2003}, volume={551} }
40 Citations
Three-dimensional structure of a new enzyme, O-phosphoserine sulfhydrylase, involved in l-cysteine biosynthesis by a hyperthermophilic archaeon, Aeropyrum pernix K1, at 2.0A resolution.
- Chemistry, BiologyJournal of molecular biology
- 2005
Structural analysis of the substrate recognition mechanism in O-phosphoserine sulfhydrylase from the hyperthermophilic archaeon Aeropyrum pernix K1.
- ChemistryJournal of molecular biology
- 2012
Thermostability and reactivity in organic solvent of O-phospho-l-serine sulfhydrylase from hyperthermophilic archaeon Aeropyrum pernix K1
- Chemistry, BiologyBioscience, biotechnology, and biochemistry
- 2015
Comparison of thermal stability and reactivity in organic solvent of OPSS with those of O-acetyl-l-serine sulfhydrylase B from Escherichia coli indicates that OPSS is more superior to OASS-B for the industrial production of l-cysteine and unnatural amino acids that are useful pharmaceuticals in the presence of organic solvent.
O-phospho-L-serine and the thiocarboxylated sulfur carrier protein CysO-COSH are substrates for CysM, a cysteine synthase from Mycobacterium tuberculosis.
- Biology, ChemistryBiochemistry
- 2008
This study represents the first detailed kinetic characterization of sulfide transfer from a sulfide carrier protein and interpret this finding to suggest that the CysM active site with the bound aminoacrylate intermediate is protected from solvent and that binding of CysO-COSH produces a conformational change allowing rapid sulfur transfer.
Cysteine Synthase (CysM) of Mycobacterium tuberculosis Is an O-Phosphoserine Sulfhydrylase
- Biology, ChemistryJournal of Biological Chemistry
- 2008
The specificity of CysM toward O-phosphoserine together with the previously established novel mode of sulfur delivery via thiocarboxylated CysO provide strong evidence for an O- phosphoserine-based cysteine biosynthesis pathway in M. tuberculosis that is independent of both O-acetylserine and the sulfate reduction pathway.
Increased Production of Recombinant O-Phospho-L-Serine Sulfhydrylase from the Hyperthermophilic Archaeon Aeropyrum pernix K1 Using Escherichia coli
- BiologyCurrent Biotechnology
- 2019
It is found that the optimal culture conditions along with codon optimization were essential for the increased ApOPSS production, and this method may facilitate the industrial production of cysteine and non-natural amino acids using ApopSS.
Role of F225 in O-phosphoserine sulfhydrylase from Aeropyrum pernix K1
- Chemistry, BiologyExtremophiles
- 2016
The results suggest that F225 in ApOPSS plays important roles in maintaining the hydrophobic environment of AA from solvent water and in controlling the orientation of leaving groups.
Identification of amino acid residues important for recognition of O-phospho-l-serine substrates by cysteine synthase.
- Biology, ChemistryJournal of bioscience and bioengineering
- 2021
Cysteine Biosynthesis in Trichomonas vaginalis Involves Cysteine Synthase Utilizing O-Phosphoserine*
- BiologyJournal of Biological Chemistry
- 2006
Overall, TvCS1 has substrate specificities similar to those reported for cysteine synthases of Aeropyrum pernix and Escherichia coli, and this is reflected by sequence similarities around the active site, and it is hypothesize that the use of O-phosphoserine is a common characteristic of these cysteined synthases.
Biochemical properties of nematode O-acetylserine(thiol)lyase paralogs imply their distinct roles in hydrogen sulfide homeostasis.
- BiologyBiochimica et biophysica acta
- 2013
References
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ABSTRACT An O-acetylserine sulfhydrylase (OASS) from the hyperthermophilic archaeon Aeropyrum pernix K1, which shares the pyridoxal 5′-phosphate binding motif with both OASS and cystathionine…
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Equilibrium sedimentation studies on native and carboxymethylated enzyme, analytical polyacrylamide disc gel electrophoresis in urea, pyridoxal phosphate analysis, tryptic peptide mapping, and amino acid analysis have shown that O-acetylserine sulfhydrylase-A consists of two identical subunits of molecular weight 34,000.
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Sensitivity of the enzyme to carbonyl reagents was very low, although it was shown to have pyridoxal 5′-phosphate as a cofactor by examination of its absorption spectrum and the novelty of this enzyme among analogous sulfhydrylases purified from other organisms was discussed.
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Enzyme activities in extracts of Methanosarcina thermophila grown with combinations of cysteine and sulfide as sulfur sources indicated that this archaeon utilizes the pathway found in the Bacteria domain.
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O-Acetyl-L-serine sulfhydrylase was first purified from an extremely thermophilic bacterium in order to ascertain that it is responsible for the cysteine synthesis in this organism cultured with either sulfate or methionine given as a sole sulfur source.
Cysteine Biosynthesis Pathway in the ArchaeonMethanosarcina barkeri Encoded by Acquired Bacterial Genes?
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Analysis of recent genome data revealed the presence of bacteria-like cysM genes in Pyrococcus spp.
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