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Literature summary for 3.4.11.18 extracted from

  • Liao, Y.D.; Jeng, J.C.; Wang, C.F.; Wang, S.C.; Chang, S.T.
    Removal of N-terminal methionine from recombinant proteins by engineered E. coli methionine aminopeptidase (2004), Protein Sci., 13, 1802-1810.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.11.18

Protein Variants

Protein Variants Comment Organism
M206G/Q233G removes L-Met from bulky or acidic penultimate residues Escherichia coli
M206T removes L-Met from bulky or acidic penultimate residues Escherichia coli
M206T/Q233G removes L-Met from bulky or acidic penultimate residues Escherichia coli
M206T/Q233T removes L-Met from bulky or acidic penultimate residues Escherichia coli
M206V/Q233T removes L-Met from bulky or acidic penultimate residues Escherichia coli
Q233G removes L-Met from bulky or acidic penultimate residues Escherichia coli
Y1268G removes L-Met from bulky or acidic penultimate residues Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Met-L-Gln-L-Asp-onconase + H2O wild-type, no substrate, mutant M206G/Q233G, 96% of Met removal, mutant M206T/Q233G, 91% of removal, mutant M206T/Q233T, 93% of removal Escherichia coli L-Met + L-Gln-L-Asp-onconase
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additional information detailed analysis of mutants specificity on oligo- and protein substrates Escherichia coli ?
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