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3.4.11.21: aspartyl aminopeptidase

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

Word Map on EC 3.4.11.21

Reaction

release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate =

Synonyms

AAP, acid aminopeptidase, acid peptidase, alpha-aspartyl dipeptidase, Aminopeptidase, aminopeptidase A, angiotensinase, APA, Ape4, Ape4 aspartyl aminopeptidase, Ape4 metalloprotease, Asp-AP, AspAP, aspartate aminopeptidase, aspartic aminopeptidase, aspartyl aminopeptidase, aspartyl(glutamyl)-specific aminopeptidase, aspartyl-AP, CNAG_01169, DAP, DNPEP, EC 3.4.11.7, glutamyl (aspartyl)-specific aminopeptidase A, glutamyl aminopeptidase, L-aspartate aminopeptidase, Lb-PepA, Lc-PepA, M18 aspartyl aminopeptidase, M18AAP, More, PepA, peptidase E, PfM18AAP, PvM18AAP, soluble acid aminopeptidase, TgAAP, TGGT1_297970, Yhr113w

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.21 aspartyl aminopeptidase

Crystallization

Crystallization on EC 3.4.11.21 - aspartyl aminopeptidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with zinc and substrate analogue aspartate-beta-hydroxamate, to 2.2 A resolution. Structure reveals a dodecameric machinery built by domain-swapped dimers, in agreement with electron microscopy data. For both Asp-Ala and Glu-Ala substrates, the Asp and Glu side chains fit into the P1 substrate pocket without steric constraints, while the main chain is modeled onto the hydroxamate group of aspartate-beta-hydroxamate in a position optimal for hydrolysis. The P1 substrate pocket is created by strand beta15 and the beta16-alpha12 and beta17-alpha13 loops, with the beta17-lpha13 loop lining the wall and restricting the dimensions of the pocket. This limited space disfavours bulky hydrophobic residues