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3.4.11.3: cystinyl aminopeptidase

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

Word Map on EC 3.4.11.3

Reaction

Release of an N-terminal amino acid, Cys-/-Xaa-, in which the half-cystine residue is involved in a disulfide loop, notably in oxytocin or vasopressin. Hydrolysis rates on a range of aminoacyl arylamides exceed that for the cystinyl derivative, however =

Synonyms

alpha-Aminoacyl-peptide hydrolase, aminopeptidase, cystyl, AT4 receptor, CAP, CAP-I, CAP-II, CysAP, cysteine aminopeptidase, cystine aminopeptidase, Cystinyl aminopeptidase, cystinylaminopeptidase, cystyl aminopeptidase, cystyl-aminopeptidase, GP160, insulin regulated aminopeptidase, insulin-regulated aminopeptidase, insulin-regulated aminopeptidase IRAP, Insulin-regulated membrane aminopeptidase, Insulin-responsive aminopeptidase, IRAP, IRAP/P-LAP, L-cystine aminopeptidase, LCAP, LeuAP, leucine aminopeptidase/oxytocinase, leucyl-aminopeptidase, leucyl-cystinyl aminopeptidase, LNPEP, M1 aminopeptidase, OTase, oxytocin peptidase, oxytocinase, oxytocinase/insulin-regulated aminopeptidase, oxytocinase/vasopressinase-like leucyl-cystinyl aminopeptidase LNPEP, P-LAP, P-LAP/IRAP, P-LAP/OTase, placental leucil aminopeptidase, Placental leucine aminopeptidase, placental leucine aminopeptidase/oxytocinase, placental leucine aminopeptidase/oxytocinase/insulin-regulated membrane aminopeptidase, vasopressinase, vasopresssinase, Vesicle protein of 165 kDa, Vp165, yscXVI

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.3 cystinyl aminopeptidase

Crystallization

Crystallization on EC 3.4.11.3 - cystinyl aminopeptidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme free or in complex with inhibitory antigenic peptide precursor analogue N2-(2- 8[(1-amino-3-phenylpropyl)(hydroxy)phosphoryl]methyl]-4-methylpentanoyl)-L-lysyl-L-histidyl-L-histidyl-L-alanyl-L-phenylalanyl-L-seryl-L-phenylalanyl-L-lysine, sitting drop vapor diffusion, mixing of 100 nl of 10 mg/ml protein in 150 mM NaCl and 10 mM HEPES, pH 7.4, with 100 nl of crystallization solution containing 10% w/v PEG 4000, 20% v/v glycerol, 53.4 mM bicine, 46.6 mM Trizma base, pH 8.5, and 0.02 M each of sodium L-glutamate, DL-alanine, glycine, DL-lysine, and DL-serine, method optimization, X-ray diffraction structure determination and analysis at 3.31-3.37 A resolution, molecular replacement using the highly homologous ERAP1 open structure (PDB ID 3QNF) as a search model, and modelling
purified recombinant enzyme in complex with inhibitory peptide [(5R)-6-amino-5-benzyl-2-(2,2-diphenylethyl)-3,6-dioxohexyl][(1R)-1-amino-3-phenylpropyl]phosphinic acid, sitting drop vapor diffusion, mixing of 5 mg/ml protein in 150 mM NaCl, and 10 mM HEPES, pH 7.5, with 100 nl of crystallization solution containing 18.8% w/v PEG 20000, 37.6% v/v PEG monomethyl ether 500, 50.2 mM bicine, 43.8 mM Trizma base, pH 8.5, and 0.282 M of each of sodium fluoride, sodium bromide, and sodium iodide, 21°C, method optimization, X-ray diffraction structure determination and analysis at 2.53 A resolution, molecular replacement using the highly homologous aminopeptidase ERAP1 structure (PDB ID 2YD0) as a search model, and modelling
several crystal structures of enzyme IRAP in apo and ligand boudn states are available, PDB IDs 4P8Q, 4PJ6, 4Z7I, 5C97, and 5MJ6