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Literature summary for 3.4.11.10 extracted from

  • Bzymek, K.P.; Swierczek, S.I.; Bennett, B.; Holz, R.C.
    Spectroscopic and thermodynamic characterization of the E151D and E151A altered leucine aminopeptidases from Aeromonas proteolytica (2005), Inorg. Chem., 44, 8574-8580.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant E151HA and E151D enzymes in Escherichia coli strain BL21(DE3) Vibrio proteolyticus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics of apoenzyme and metal-bound wild-type and mutant enzymes, isothermal titration measurement, thermodynamics, overview Vibrio proteolyticus

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ can substitute for one or both Zn2+ ions Vibrio proteolyticus
additional information detailed metal binding structure and kinetic analysis with recombinant wild-type and mutant enzymes, overview Vibrio proteolyticus
Zn2+ dinuclear Zn2+ metal center Vibrio proteolyticus

Organism

Organism UniProt Comment Textmining
Vibrio proteolyticus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation, dialysis, hydrophobic interaction and anion exchange chromatography Vibrio proteolyticus

Reaction

Reaction Comment Organism Reaction ID
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. active site residue Glu151 is essential for activity acting as a general acid/base during the catalytic reaction, mechanism of peptide hydrolysis Vibrio proteolyticus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Leu-4-nitroanilide + H2O
-
Vibrio proteolyticus L-Leu + 4-nitroaniline
-
?

Synonyms

Synonyms Comment Organism
leucine aminopeptidase
-
Vibrio proteolyticus