Can I read Determination of the sites required for the allosteric inhibition of serine acetyltransferase by L-cysteine in plants on EtoBox?

Determination of the sites required for the allosteric inhibition of serine acetyltransferase by L-cysteine in plants by Kenji Inoue; Masaaki Noji; Kazuki Saito is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Determination of the sites required for the allosteric inhibition of serine acetyltransferase by L-cysteine in plants about?

Serine acetyltransferase (SATase; EC 2.3.1.30) catalyzes the formation of __O__‐acetylserine from l‐Ser and acetyl‐CoA in plants and bacteria. In plants, two types of SATase have been described. One is allosterically inhibited by l‐Cys, and the second is not sensitive to l‐Cys inhibition. However, the allosteric site in SATase has not been identified. To understand better the mechanism of l‐Cys inhibition of plant SATases, we constructed several chimeric SATase enzymes from watermelon SATase (WaSATase) (sensitive type) and __Arabidopsis__ SAT‐p (insensitive type). These enzymes were expressed in __Escherichia coli__, and inhibition of the mutated SATase activity by l‐Cys was analyzed. Mutated WaSATase, in which Met280 was changed to Ile, was no longer inhibited by l‐Cys. Analysis of the inhibition the chimeric enzymes indicated that the C‐terminal region of WaSATase from Pro276 to Phe285, in which five amino acids are different from those of SAT‐p, was responsible for the determination of the sensitivity to l‐Cys. In particular, Gly277 in the C‐terminal region of WaSATase was primarily responsible for the l‐Cys inhibition. The N‐terminal half of the protein, which does not contain

Who reads Determination of the sites required for the allosteric inhibition of serine acetyltransferase by L-cysteine in plants?

Author

Kenji Inoue; Masaaki Noji; Kazuki Saito

Publisher

John Wiley and Sons; Springer; Wiley (Blackwell Publishing); Springer-Verlag; Blackwell Publishing Inc.; Springer Verlag; Wiley; Springer Science and Business Media LLC (ISSN 1432-1327)

Published

1999

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)