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3.4.11.7: glutamyl aminopeptidase

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

Word Map on EC 3.4.11.7

Reaction

release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide =

Synonyms

acid aminopeptidase, acidic alpha-aminopeptidase, Aminopeptidase, aminopeptidase A, aminopeptidase A ectopeptidase, aminopeptidase, aspartate, aminopeptidase-A, angiotensinase, angiotensinase A, antigen BP-1/6C3 of mouse B lymphocytes, AP A, APA, Asp-AP, aspartate aminopeptidase, aspartyl aminopeptidase, aspartyl-aminopeptidase, BP-1, BP-1/6C3 antigen, BP1/6C3, Ca2+-activated glutamate aminopeptidase, Differentiation antigen gp160, EAP, ENPEP, GAP, GluAP, glutamyl (aspartyl)-specific aminopeptidase A, glutamyl aminopeptidase, glutamyl aminopeptidase (Lactococcus), glutamyl peptidase, glutamyl-aminopeptidase, glutamyl-AP, hAPA, L-alpha-aspartyl(L-alpha-glutamyl)-peptide hydrolase, L-aspartate aminopeptidase, LAP-A, Lb-PepA, Lc-PepA, leucine aminopeptidase A, M18 aspartyl aminopeptidase, mAPA, membrane aminopeptidase II, membrane-bound aspartyl-AP, MHJ_0125, More, N-terminal acidic amino acid-specific aminopeptidase, PepA, tricorn interacting factor F3, tricorn protease-interacting factor F3, type II Zn2+ membrane-bound aminopeptidase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.7 glutamyl aminopeptidase

Crystallization

Crystallization on EC 3.4.11.7 - glutamyl aminopeptidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hexagonal crystals of F3 are grown from 0.1 M Tris-HCl (pH 8.5), 18% (w/w) PEG 2000 and 0.2 M Li2SO4 at 18°C using the sitting-drop, vapor-diffusion technique. Crystal structure of the tricorn interacting factor F3 in free form and in three different conformations, depending on the crystal form in which they are crystallized, give insights into the molecular dynamics of F3 relating to substrate binding and mechanistic aspects of substrate processing. The structure adumbrates how F3 might assemble with the tricorn protease and how the substrate transfer from the tricorn protease to F3 might proceed