Leishmania major thialysine Nε‐acetyltransferase: Identification of amino acid residues crucial for substrate binding
- 16 September 2005
- journal article
- Published by Wiley in FEBS Letters
- Vol. 579 (24) , 5347-5352
- https://doi.org/10.1016/j.febslet.2005.08.063
Abstract
Thialysine N ε‐acetyltransferases and spermidine/spermine N‐acetyltransferases (SSAT) are closely related members of the GCN5‐related N‐acetyltransferase superfamily. Accordingly, a putative orthologue from the human protozoan parasite Leishmania major exhibits an almost equal similarity to human SSAT and thialysine N ε‐acetyltransferase. Characterisation of the recombinantly expressed L. major protein indicated that it represents a thialysine N ε‐acetyltransferase, preferring thialysine (S‐aminoethyl‐l‐cysteine) and structurally related amino acids as acceptor molecules. The known thialysine N ε‐acetyltransferases contain five conserved amino acid residues that are replaced in SSAT sequences. Kinetic analyses of the respective recombinant mutant proteins suggest that Ser82 and Thr83 of L. major thialysine N ε‐acetyltransferase are key residues for acceptor binding. In addition, the conserved Leu130 is tentatively involved in specific interaction with the sulphur‐containing side chain of thialysine. The presence of these three amino acid residues is suggested to be a means by which thialysine N ε‐acetyltransferases can be distinguished from SSAT sequences.Keywords
This publication has 28 references indexed in Scilit:
- The Crystal Structure of Rv1347c, a Putative Antibiotic Resistance Protein from Mycobacterium tuberculosis, Reveals a GCN5-related Fold and Suggests an Alternative Function in Siderophore BiosynthesisJournal of Biological Chemistry, 2005
- A novel member of the GCN5-related N-acetyltransferase superfamily from Caenorhabditis elegans preferentially catalyses the N-acetylation of thialysine [S-(2-aminoethyl)-L-cysteine]Biochemical Journal, 2004
- Genomic identification and biochemical characterization of a second spermidine/spermine N1-acetyltransferaseBiochemical Journal, 2003
- GCN5-Related N-Acetyltransferases: A Structural OverviewAnnual Review of Biophysics, 2000
- RGFGIGS Is an Amino Acid Sequence Required for Acetyl Coenzyme A Binding and Activity of Human Spermidine/Spermine N1AcetyltransferasePublished by Elsevier ,1996
- Alteration in the conformational stability of collagen caused by the incorporation of the lysine analogue S-2-aminoethylcysteineBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1996
- Identification of N-acetylspermidine in Leishmania amazonensisMolecular and Biochemical Parasitology, 1996
- Role of the carboxyl terminal MATEE sequence of spermidine/spermine N1-acetyltransferase in the activity and stabilization by the polyamine analog N1,N12-bis(ethyl)spermineBiochemistry, 1995
- Enzymatic synthesis of
aminoethyl- from pantetheinel -cysteineBiochimica et Biophysica Acta (BBA) - General Subjects, 1992 - A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976