PMID:11055390
| Citation |
Mino, K, Hiraoka, K, Imamura, K, Sakiyama, T, Eisaki, N, Matsuyama, A and Nakanishi, K (2000) Characteristics of serine acetyltransferase from Escherichia coli deleting different lengths of amino acid residues from the C-terminus. Biosci. Biotechnol. Biochem. 64:1874-80 |
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| Abstract |
Some properties of serine acetyltransferases (SATs) from Escherichia coli, deleting 10-25 amino acid residues from the C-terminus (SATdeltaC10-deltaC25) were investigated. The specific activity depended only slightly on the length of the C-terminal region deleted. Although the sensitivity of SATdeltaC10 to inhibition by L-cysteine was similar to that for the wild-type SAT, it became less with further increases in the length of the amino acid residues deleted. SATdeltaC10 was inactivated on cooling to 0 degrees C and dissociated into dimers or trimers in the same manner as the wild-type SAT, but Met-256-le mutant SAT as well as SATdeltaC14, SATdeltaC20, and SATdeltaC25 were stable. Since SATdeltaC10, SATdeltaC14, and SATdeltaC25 did not form a complex with O-acetylserine sulfhydrylase-A (OASS-A) in a way similar to SATdeltaC20, it was indicated that 10 amino acid residues or fewer from the C-terminus of the wild-type SAT are responsible for the complex formation with OASS-A. The C-terminal peptide of the 10 amino acid residues interacted competitively with OASS-A with respect to OAS although its affinity was much lower than that for the wild-type SAT. |
| Links | |
| Keywords |
Acetyltransferases/chemistry; Acetyltransferases/genetics; Acetyltransferases/metabolism; Amino Acid Sequence; Animals; Arabidopsis/enzymology; Dimerization; Entamoeba histolytica/enzymology; Escherichia coli/enzymology; Kinetics; Macromolecular Substances; Molecular Sequence Data; Peptide Fragments/chemistry; Recombinant Proteins/chemistry; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism; Salmonella typhimurium/enzymology; Sequence Alignment; Sequence Deletion; Sequence Homology, Amino Acid; Serine O-Acetyltransferase |
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