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3.4.11.4: tripeptide aminopeptidase

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

Word Map on EC 3.4.11.4

Reaction

release of the N-terminal residue from a tripeptide =

Synonyms

alanine-phenylalanine-proline arylamidase, alpha-aminoacyl-dipeptide hydrolase, aminoexotripeptidase, aminopeptidase, human liver, aminotripeptidase, arginyl tri-peptidase, ec 3.4.1.3, EC 3.4.14.10, imidoendopeptidase, lymphopeptidase, PepB, PepT, peptidase B, peptidase T, prolyl tripeptidyl aminopeptidase, PTP, PTP39, TPP I, TPP II, TPPII, tripeptidase, tripeptidyl aminopeptidase, tripeptidyl exopeptidase II, tripeptidyl peptidase II, tripeptidyl-peptidase I, tripeptidyl-peptidase II

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.4 tripeptide aminopeptidase

Crystallization

Crystallization on EC 3.4.11.4 - tripeptide aminopeptidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method with 100 mM Ches (pH 9.0), 1.1 M potassium/sodium tartrate, 200 mM lithium sulfate
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hanging-drop vapour diffusion method at 20°C. Crystallization of aminotripeptidase and a derivative carrying a C-terminal His tag. Native peptidase diffracts to 2.9 A, His-tag peptidase T diffracts to 2.6 A, the selenomethionine derivative of the enzyme does not yield good crystals. His-tag derivatives not only facilitates protein purification but can also result in crystals of improved quality
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selenomethionine His-tagged peptidase T, determination of structure by multiple wavelength anomalous dispersion methodology and refined to 2.4 A resolution
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