The serine acetyltransferase fromEscherichia coli
نویسندگان
چکیده
منابع مشابه
Serine acetyltransferase of Escherichia coli: substrate specificity and feedback control by cysteine.
Although SAT (serine acetyltransferase) of Escherichia coli, which catalyses the first step in cysteine synthesis, proceeds via a random-order ternary complex reaction mechanism [Hindson and Shaw (2003) Biochemistry 42, 3113-3119], it has been suggested that the nearly identical enzyme from Salmonella typhimurium might involve an acetyl-enzyme intermediate [Leu and Cook (1994) Protein Peptide L...
متن کاملIncrease in the stability of serine acetyltransferase from Escherichia coli against cold inactivation and proteolysis by forming a bienzyme complex.
Cysteine synthetase from Escherichia coli is a bienzyme complex composed of serine acetyltransferase (SAT) and O-acetylserine sulfhydrylase-A (OASS). The effects of the complex formation on the stability of SAT against cold inactivation and proteolysis were investigated. SAT was reversibly inactivated on cooling to 0 degrees C. Ultracentrifugal analysis showed that SAT (a hexamer) was dissociat...
متن کاملOverproduction of L-cysteine and L-cystine by Escherichia coli strains with a genetically altered serine acetyltransferase.
Organisms that overproduced L-cysteine and L-cystine from glucose were constructed by using Escherichia coli K-12 strains. cysE genes coding for altered serine acetyltransferase, which was genetically desensitized to feedback inhibition by L-cysteine, were constructed by replacing the methionine residue at position 256 of the serine acetyltransferase protein with 19 other amino acid residues or...
متن کاملChemotaxis of Escherichia coli to L-serine.
A novel experimental technique was used to quantify the motion of E. coli to varying serine concentrations and gradients so as to capture the spatial and temporal variation of the chemotactic response. The average run speed and the cell diffusivity are found to be dependent on the serine concentration. The measured diffusivities were in the range of 1.2-2.5 x 10 (-10) m(2) s(-1). The study reve...
متن کاملL-serine deaminase of Escherichia coli.
The native l-serine deaminase (l-serine hydrolyase, deaminating, EC 4.2.1.13) of Escherichia coli K-12, which seems to be a very labile protein, is rather stable in concentrated solution. Dilution rapidly inactivates it, but in the presence of a saturating concentration of l-serine the molecule is protected from inactivation. It is a very specific enzyme; l-serine is the sole substrate with a K...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1990
ISSN: 0014-5793
DOI: 10.1016/0014-5793(90)80862-d