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={K. Mino and K. Ishikawa},
  journal={FEBS Letters},
  year={2003},
  volume={551}
}
O‐Acetylserine sulfhydrylase (OASS), a pyridoxal 5′‐phosphate (PLP)‐dependent enzyme, catalyzes the synthesis of L‐cysteine from O‐acetyl‐L‐serine and sulfide. O‐Acetyl‐L‐serine is labile at high temperatures at which hyperthermophilic archaea live. Herein, a study of the substrate specificity of OASS from Aeropyrum pernix K1 with respect to O‐acetyl‐L‐serine in L‐cysteine synthesis is described. L‐Azaserine, 3‐chloro‐L‐alanine, and O‐phospho‐L‐serine reacted with A. pernix OASS in a PLP… Expand
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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.
Structural analysis of the substrate recognition mechanism in O-phosphoserine sulfhydrylase from the hyperthermophilic archaeon Aeropyrum pernix K1.
Thermostability and reactivity in organic solvent of O-phospho-l-serine sulfhydrylase from hyperthermophilic archaeon Aeropyrum pernix K1
O-phospho-L-serine and the thiocarboxylated sulfur carrier protein CysO-COSH are substrates for CysM, a cysteine synthase from Mycobacterium tuberculosis.
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The multifaceted pyridoxal 5'-phosphate-dependent O-acetylserine sulfhydrylase.
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