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}
}
Thermostability and reactivity in organic solvent of O-phospho-l-serine sulfhydrylase from hyperthermophilic archaeon Aeropyrum pernix K1
TLDR
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.
TLDR
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
TLDR
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
TLDR
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
TLDR
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.
Cysteine Biosynthesis in Trichomonas vaginalis Involves Cysteine Synthase Utilizing O-Phosphoserine*
TLDR
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.
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References

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Characterization of a Novel Thermostable O-Acetylserine Sulfhydrylase from Aeropyrum pernix K1
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
O-Acetylserine Sulfhydrylase fromMethanosarcina thermophila
TLDR
This study reports the purification and characterization of OASS from acetate-grown Methanosarcina thermophila, a moderately thermophilic methanoarchaeon, and provides the first biochemical evidence for a sulfur-fixing enzyme in the Archaea domain.
The purification and characterization of O-acetylserine sulfhydrylase-A from Salmonella typhimurium.
TLDR
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.
Characterization of O-Acetyl-L-serine Sulfhydrylase Purified from an Alkaliphilic Bacterium
TLDR
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.
Kinetic mechanisms of the A and B isozymes of O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2 using the natural and alternative reactants.
TLDR
The ping pong mechanism is corroborated by a qualitative and quantitative analysis of product and dead-end inhibition, and there may be some randomness to the mechanism at high concentrations of the nucleophilic substrate.
Cysteine biosynthesis in the Archaea: Methanosarcina thermophila utilizes O-acetylserine sulfhydrylase.
TLDR
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.
Cysteine Synthase of an Extremely Thermophilic Bacterium, Thermus thermophilus HB8
TLDR
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?
TLDR
Analysis of recent genome data revealed the presence of bacteria-like cysM genes in Pyrococcus spp.
Effects of Bienzyme Complex Formation of Cysteine Synthetase from Escherichia coli on Some Properties and Kinetics
TLDR
The role and significance of a complex formation for the cysteine synthetase is discussed and changes in the stability of the wild-type SAT by the complex formation are discussed.
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