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Literature summary for 3.4.11.1 extracted from

  • Duprez, K.; Scranton, M.A.; Walling, L.L.; Fan, L.
    Structure of tomato wound-induced leucine aminopeptidase sheds light on substrate specificity (2014), Acta Crystallogr. Sect. D, 70, 1649-1658.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli as a His-tagged fusion protein Solanum lycopersicum

Crystallization (Commentary)

Crystallization (Comment) Organism
unliganded crystal structure of LAP-A is determined to 2.20 A resolution Solanum lycopersicum

Organism

Organism UniProt Comment Textmining
Solanum lycopersicum Q10712
-
-

Purification (Commentary)

Purification (Comment) Organism
using Ni2+-NTA chromatography Solanum lycopersicum

Subunits

Subunits Comment Organism
dimer LAP-A is a dimer of trimers containing six monomers of bilobal structure. Each trimer is formed by the interactions of the C-terminal domains of three LAP-A monomers at the center with the N-termini stretching out to form a triangular shape Solanum lycopersicum

Synonyms

Synonyms Comment Organism
LAP-A
-
Solanum lycopersicum
leucine aminopeptidase
-
Solanum lycopersicum