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Literature summary for 3.4.11.10 extracted from

  • Straeter, N.; Lipscomb, W.N.
    Leucine aminopeptidase (2004), Handbook of Metalloproteins (Messerschmidt, A. ; Huber, R. ; Wieghardt, K. ; Palos, T. , eds. ), 3, 199-207.
No PubMed abstract available

Activating Compound

Activating Compound Comment Organism Structure
bicarbonate activates Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallization at pH 8.0 of enzyme in high salt Tris buffer against low salt concentration, X-ray diffraction crystal structure determination and analysis at 2.5 A resolution Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ metallopeptidase, dimetal site structure, overview Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli PepA acts as DNA-binding protein in Xer site-specific DNA recombination serving as accessory protein ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. catalytic mechanism Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Leu-4-nitroanilide + H2O
-
Escherichia coli L-Leu + 4-nitroaniline
-
?
additional information PepA acts as DNA-binding protein in Xer site-specific DNA recombination serving as accessory protein Escherichia coli ?
-
?
additional information PepA binds DNA probably along the large groove that runs from the lower trimer face across the twofold molecular axis to the upper trimer face Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
hexamer lens enzyme three-dimensional structure and protein fold, overview Escherichia coli

Synonyms

Synonyms Comment Organism
LAP
-
Escherichia coli
leucine aminopeptidase
-
Escherichia coli
More the enzyme belongs to the peptidase family M17 Escherichia coli
PepA
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Escherichia coli