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3.4.11.1: leucyl aminopeptidase

This is an abbreviated version!
For detailed information about leucyl aminopeptidase, go to the full flat file.

Word Map on EC 3.4.11.1

Reaction

release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low =

Synonyms

A-LAP, acidic M17 leucine aminopeptidase, AcLAP, adipocyte-derived leucine aminopeptidase, Aminopeptidase, aminopeptidase A, Aminopeptidase A/I, aminopeptidase I, aminopeptidase II, Aminopeptidase III, aminopeptidase LAP2, aminopeptidase N, AP 28, AP 56, APDkam589, APN, b/LAP, bovine lens/leucine aminopeptidase, BSAP, cathepsin III, CsLAP1, CsLAP2, cysteinyl-glycine hydrolysing activity, cysteinylglycine-hydrolysing activity, cytosol aminopeptidase, DR57, EC 3.4.1.1, Eg-LAP, endoplasmic reticulum aminopeptidase, ER-aminopeptidase-1, ERAP, ERAP1, ERAP2, FgLAP, FrvX, FTBL protein, FTBL proteins, HSA, L-leucine aminopeptidase, la, LAP, LAP yspII, LAP-A, LAP-N, LAP1, LAP2, lap3, LapA, LAPc, LeuAP, leucinamide aminopeptidase, leucinaminopeptidase, leucine amino peptidase, leucine aminopeptidase, leucine aminopeptidase 1, leucine aminopeptidase 2, leucine aminopeptidase 3, leucine aminopeptidase A, leucine aminopeptidase LAP-N, leucine aminopeptidase N, leucine aminopeptidase,, leucine aminopeptidase-A, Leucyl aminopeptidase, leucyl aminopeptidase (animal), leucyl aminopeptidase (plant), leucyl aminopeptidase yspII, leucyl peptidase, leucylaminopeptidase, leucylpeptidase, LmLAP-A, M17 family leucyl aminopeptidase metalloprotease, M17 LAP, M17 leucine amino peptidase, M17 leucine aminopeptidase, M17 leucyl aminopeptidase, M42 aminopeptidase, major leucyl aminopeptidase, More, PA2939, PaAP, PepA, PepA peptidase A, PepB, peptidase B, peptidase II, peptidase S, pepZ, PfLAP, PH1527, PhTET2, PILS-AP, PILSAP, Placental leucine aminopeptidase, PLAP, proline aminopeptidase, Prolyl aminopeptidase, proteins, specific or class, FTBL, PtLAP, puromycin insensitive leucyl-specific aminopeptidase, puromycin-insensitive leucine specific aminopeptidase, puromycin-insensitive leucyl-specific aminopeptidase, PVX_118180, rLAP, rMHJ_0461, S-Lap1, S-Lap2, S-Lap3, S-Lap4, S-Lap5, S-Lap6, S-Lap7, S-Lap8, SmLAP1, SmLAP2, Smp_03000, Smp_083870, sperm-leucylaminopeptidase, TbLAP-A, TbLAP1, TcLAP-A, TM0042, TpLAP, XoLAP

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.1 leucyl aminopeptidase

Crystallization

Crystallization on EC 3.4.11.1 - leucyl aminopeptidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization in presence of ZnSO4, NaCl, and 2-methyl-2,4-pentanediol, at pH 7.8 in Tris buffer, X-ray diffraction crystal structure determination and analysis at 1.6 A resolution
-
hanging drop vapour diffusion method. The crystal structure of microginin FR1 from Microcystis sp. bound to bovine lens leucine aminopeptidase is established at 1.73 A resolution
Zn2+-Zn2+-enzyme in complex with the peptidomimetic derivative zofenoprilat, soaking of crystals in 20 mM zofenoprilat, X-ray diffraction structure determination and analysis at 1.85 A resolution
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
-
purified recombinant His-tagged enzyme LmLAP-A, in the presence of Mn2+, X-ray diffraction structure determination and analysis at 2.5 A resolution, molecular replacement, modelling
sitting drop vapor diffusion method. The quaternary structure is built by dimers with a length of 100 A that form the edges of the tetrahedron. All 12 active sites are located on the inside of the tetrahedron. Substrate access is granted by pores with a maximal diameter of 10 A, allowing only small peptides and unfolded proteins access to the active site
the crystal structure of of the enzyme is determined at 1.6 A resolution in native form and in complex with the inhibitor amastatin, hanging drop, vapour-diffusion method
unliganded crystal structure of LAP-A is determined to 2.20 A resolution
purified recombinant His-tagged enzyme TbLAP-A in complex with inhibitor bestatin, in the presence of ZnCl2 and Mn2+, X-ray diffraction structure determination and analysis, molecular replacement, modelling
purified recombinant His-tagged enzyme LmLAP-A, X-ray diffraction structure determination and analysis at 2.5 A resolution, molecular replacement, modelling. TcLAP-A crystallizes exclusively under citratecontaining conditions, which leads to the absence of one or both Mn2x02 ions from the active site and hence no electron density for the inhibitors
crystal structure of XoLAP is determined at 2.6 A resolution. The XoLAP crystal contains two complete monomers in its asymmetric unit