Removal of N-terminal methionine from recombinant proteins by engineeredE. colimethionine aminopeptidase
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چکیده
منابع مشابه
N-terminal methionine removal and methionine metabolism in Saccharomyces cerevisiae.
Methionine aminopeptidase (MetAP) catalyzes removal of the initiator methionine from nascent polypeptides. In eukaryotes, there are two forms of MetAP, type 1 and type 2, whose combined activities are essential, but whose relative intracellular roles are unclear. Methionine metabolism is an important aspect of cellular physiology, involved in oxidative stress, methylation, and cell cycle. Due t...
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Synthetic alphaT1 and betaT1, the N-terminal tryptic peptides of alpha-chain and beta-chain of hemoglobin, and MetalphaT1 and MetbetaT1, peptides in which N-terminal methionyl residues are peptide-bonded to alphaT1 and betaT1, were prepared by the solid-state method of Merrifield. These synthetic peptides were used to establish conditions for chromatographic purification and analysis. When tryp...
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The ability of natural clinoptilolite and its modified forms were studied for removal of PAHs from n-paraffin. Surfactant modified zeolite (SMZ) was obtained by modifying clinoptilolite with hexadecyltrimethylammonium ion. Homoionic forms of zeolite were obtained by ion exchange process using inorganic salts of desirable cations (e.g. Ag+, Fe3+…). Nat...
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Peptide deformylases (PDFs) have been discovered recently in eukaryotic genomes, and it appears that N-terminal methionine excision (NME) is a conserved pathway in all compartments where protein synthesis occurs. This work aimed at uncovering the function(s) of NME in a whole proteome, using the chloroplast-encoded proteins of both Arabidopsis thaliana and Chlamydomonas reinhardtii as model sys...
متن کاملThe proteomics of N-terminal methionine cleavage.
Methionine aminopeptidase (MAP) is a ubiquitous, essential enzyme involved in protein N-terminal methionine excision. According to the generally accepted cleavage rules for MAP, this enzyme cleaves all proteins with small side chains on the residue in the second position (P1'), but many exceptions are known. The substrate specificity of Escherichia coli MAP1 was studied in vitro with a large (>...
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ژورنال
عنوان ژورنال: Protein Science
سال: 2004
ISSN: 0961-8368,1469-896X
DOI: 10.1110/ps.04679104