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Literature summary for 3.4.11.18 extracted from

  • Wingfield, P.; Graber, P.; Turcatti, G.; Movva, N.R.; Pelletier, M.; Craig, S.; Rose, K.; Miller, C.G.
    Purification and characterization of a methionine-specific aminopeptidase from Salmonella typhimurium (1989), Eur. J. Biochem., 180, 23-32.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Salmonella enterica subsp. enterica serovar Typhimurium

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ stimulates Salmonella enterica subsp. enterica serovar Typhimurium
Co2+ loosely associated with the enzyme protein Salmonella enterica subsp. enterica serovar Typhimurium
additional information the purified preparations do not contain significant amounts of any metal. Enzymatically important metal is loosely associated and lost during enzyme purification Salmonella enterica subsp. enterica serovar Typhimurium

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
29140
-
sedimentation equilibrium measurement Salmonella enterica subsp. enterica serovar Typhimurium
29290
-
calculation from nucleotide sequence Salmonella enterica subsp. enterica serovar Typhimurium
35500
-
1 * 35500, SDS-PAGE Salmonella enterica subsp. enterica serovar Typhimurium

Organism

Organism UniProt Comment Textmining
Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-
Salmonella enterica subsp. enterica serovar Typhimurium TN2529
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant peptidase M is also purified from Escherichia coli Salmonella enterica subsp. enterica serovar Typhimurium

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Salmonella enterica subsp. enterica serovar Typhimurium

Subunits

Subunits Comment Organism
monomer 1 * 35500, SDS-PAGE Salmonella enterica subsp. enterica serovar Typhimurium