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Literature summary extracted from

  • Modak, J.K.; Roujeinikova, A.
    Cloning, purification and preliminary crystallographic analysis of the Helicobacter pylori leucyl aminopeptidase-bestatin complex (2013), Acta Crystallogr. Sect. F, 69, 1011-1014.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.11.1 expressed in Escherichia coli Helicobacter pylori
3.4.11.10 expressed in Escherichia coli as a His-tagged fusion protein Helicobacter pylori

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.11.1 using the hanging-drop vapour-diffusion method using polyethylene glycol as a precipitating agent. The crystals belong to the primitive triclinic space group P1, with unit-cell parameters a: 97.5, b: 100.2, c: 100.4, alpha: 75.4°, beta: 60.9°, gamma: 81.8°. An X-ray diffraction data set is collected to 2.8 A resolution from a single crystal Helicobacter pylori
3.4.11.10 LAP in complex with bestatin is crystallized to 2.8 A resolution using the hanging-drop vapour-diffusion method Helicobacter pylori

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.11.1 53000
-
 SDS-PAGE Helicobacter pylori
3.4.11.1 260000
-
 gel filtration Helicobacter pylori
3.4.11.10 260000
-
 gel filtration Helicobacter pylori

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.1 Helicobacter pylori
-
-
-
3.4.11.10 Helicobacter pylori
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.11.10 using Ni-NTA chromatography Helicobacter pylori

Subunits

EC Number Subunits Comment Organism
3.4.11.1 oligomer
-
 Helicobacter pylori
3.4.11.10 hexamer crystal structure Helicobacter pylori

Synonyms

EC Number Synonyms Comment Organism
3.4.11.1 LAP
-
 Helicobacter pylori
3.4.11.1 Leucyl aminopeptidase
-
 Helicobacter pylori
3.4.11.10 LAP
-
 Helicobacter pylori
3.4.11.10 Leucyl aminopeptidase
-
 Helicobacter pylori