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Literature summary for 3.4.11.18 extracted from

  • Zheng, Y.; Roberts, R.J.; Kasif, S.; Guan, C.
    Characterization of two new aminopeptidases in Escherichia coli (2005), J. Bacteriol., 187, 3671-3677.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ required Escherichia coli
Mn2+ may substitute for Co2+ Escherichia coli
Ni2+ may substitute for Co2+ Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
39600
-
x * 39600, calculated, x * 41000, SDS-PAGE Escherichia coli
41000
-
x * 39600, calculated, x * 41000, SDS-PAGE Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
isoform YpdF, showing Xaa-Pro aminopeptidase activity and limited methionine aminopeptidase activity
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme hydrolyzes N-terminal L-methionine when the next amino acid is L-alanine, L-proline, or L-serine with substrate preference in decreasing order: proloine, alanine, serine. enzyme hydrolyzes the Xaa-Po peptide bond when the first amino acid is L-alanine, L-asparagine, or L-methionine Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
? x * 39600, calculated, x * 41000, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
YpdF
-
Escherichia coli