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• W2027414230 abstract "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‐dependent manner. Sulfhydrylation reactions using these substrates reached a maximum in the pH range between 7.3 and 8.1. L ‐Azaserine and O ‐phospho‐ L ‐serine were found to be heat‐stable substrates. The presence of FeCl 3 or NiCl 2 strongly inhibited the O ‐acetyl‐ L ‐serine sulfhydrylation reaction, whereas the O ‐phospho‐ L ‐serine sulfhydrylation reaction was only slightly inhibited. Kinetic analyses revealed that the O ‐phospho‐ L ‐serine sulfhydrylation reaction as well as the O ‐acetyl‐ L ‐serine sulfhydrylation reaction for A. pernix OASS followed a ping‐pong bi‐bi mechanism. In the case of the O ‐phospho‐ L ‐serine sulfhydrylation reaction at 85°C, the K m values for O ‐phospho‐ L ‐serine and sulfide, and the rate constant were 250 mM, 12.5 mM, and 14 000 s −1 , respectively. The reactivity of O ‐phospho‐ L ‐serine in the L ‐cysteine synthetic reaction provides a key for understanding the biosynthesis of L ‐cysteine by hyperthermophilic archaea. This is the first report of an enzyme that catalyzes the O ‐phospho‐ L ‐serine sulfhydrylation reaction." @default.
• W2027414230 created "2016-06-24" @default.
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• W2027414230 date "2003-08-27" @default.
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• W2027414230 title "A novel<i>O</i>-phospho-<scp>L</scp>-serine sulfhydrylation reaction catalyzed by<i>O</i>-acetylserine sulfhydrylase from<i>Aeropyrum pernix</i>K1" @default.
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• W2027414230 doi "https://doi.org/10.1016/s0014-5793(03)00913-x" @default.
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