'Methionine'에 해당되는 글 1건
2007. 4. 14. 00:59
MAP (Methionine Aminopeptidase) is involved in protein maturation and is responsible for removal of N-terminal Met. The cleavage is dependent on the second amino acid residue. The substrate specificities of yeast and E. coli MAPs were identified as below.
Gonzales and Robert-Baudouy showed a table in their review paper (FEMS Microbiol Rev. 1996 Jul;18(4):319-44) about MAP.
In Prokaryotes, there are two steps for protein maturation. Because the first amino acid is N-formylmethionine in prokaryotes, the removal of Met was followed by deformylation and these are the stepwise process (Adams JM., J Mol Biol. 1968 May 14;33(3):571-89) Almost half of E. coli proteins has Met in their N-terminus (Waller JP. J Mol Biol. 1963 Nov;62:483-96; Miller CG etal., Proc Natl Acad Sci U S A. 1987 May;84(9):2718-22.)
Amino-terminal processing of mutant forms of yeast iso-1-cytochrome c. The specificities of methionine aminopeptidase and acetyltransferase. Tsunasawa S, Stewart JW, Sherman F.J Biol Chem. 1985 May 10;260(9):5382-91
... Amino-terminal processing in the yeast Saccharomyces cerevisiae has been investigated by examining numerous mutationally altered forms of iso-1-cytochrome c. Amino-terminal residues of methionine were retained in sequences having penultimate residues of arginine, asparagine, glutamine, isoleucine, leucine, lysine, and methionine; in contrast, the amino-terminal methionine residues were exercised from residues of alanine, glycine, and threonine and were partially excised from residues of valine. ...
... Amino-terminal processing in the yeast Saccharomyces cerevisiae has been investigated by examining numerous mutationally altered forms of iso-1-cytochrome c. Amino-terminal residues of methionine were retained in sequences having penultimate residues of arginine, asparagine, glutamine, isoleucine, leucine, lysine, and methionine; in contrast, the amino-terminal methionine residues were exercised from residues of alanine, glycine, and threonine and were partially excised from residues of valine. ...
Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure. Ben-Bassat A, Bauer K, Chang SY, Myambo K, Boosman A, Chang S. J Bacteriol. 1987 Feb;169(2):751-7
This conclusion is consistent, in general, with the deduced specificity of the enzyme based on the analysis of known amino-terminal sequences of intracellular proteins (S. Tsunasawa, J. W. Stewart, and F. Sherman, J. Biol. Chem. 260:5382-5391, 1985).
This conclusion is consistent, in general, with the deduced specificity of the enzyme based on the analysis of known amino-terminal sequences of intracellular proteins (S. Tsunasawa, J. W. Stewart, and F. Sherman, J. Biol. Chem. 260:5382-5391, 1985).
Gonzales and Robert-Baudouy showed a table in their review paper (FEMS Microbiol Rev. 1996 Jul;18(4):319-44) about MAP.
