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- W2506873567 abstract "Publisher Summary This chapter elaborates the structural chemistry and the biological aspects of Met-X dipeptidase. This enzyme was first reported in the cell lysates of Escherichia coli strain B by Brown & Krall (1971) during a search for peptidases that could remove N-terminal Met residue of bacterial proteins once they underwent a deformylase reaction. The enzyme was purified and given the name dipeptidase M, based on facile cleavage of certain methionyl dipeptides and failure to cleave any peptides of length greater than two residues. The name methionyl dipeptidase has also been used, but the NC IUBMB adopted the name Met-X dipeptidase when the enzyme was added to 1975 Supplement. The enzyme is strictly a dipeptidase and has no aminopeptidase action on tripeptides. The amino group of the N-terminal amino acid must be free. The primary sequence of Met-X dipeptidase is unknown. The Mr determined by molecular sieving is approximately 94,000 and the enzyme comprises two identical subunits of Mr 47000." @default.
- W2506873567 created "2016-08-23" @default.
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- W2506873567 date "2004-01-01" @default.
- W2506873567 modified "2023-09-25" @default.
- W2506873567 title "Met-X dipeptidase" @default.
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- W2506873567 doi "https://doi.org/10.1016/b978-0-12-079611-3.50323-2" @default.
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