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3.4.23.22: Endothiapepsin

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

Word Map on EC 3.4.23.22

Reaction

hydrolysis of proteins with specificity similar to that of pepsin A; prefers hydrophobic residues at P1 and P1', but does not cleave Ala14-Leu in the B chain of insulin or Z-Glu-Tyr. Clots milk =

Synonyms

Aspartate protease, Aspartic proteinase, EC 3.4.23.10, EC 3.4.23.6, EC 3.4.4.17, Endothia acid proteinase, Endothia aspartic proteinase, Endothia parasitica acid proteinase, Endothia parasitica aspartic proteinase, Proteinase, Endothia aspartic

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.22 Endothiapepsin

Crystallization

Crystallization on EC 3.4.23.22 - Endothiapepsin

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complexes of pepstatin A and a statine-containing human renin inhibitor with endothiapepsin
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crystal structure of enzyme bound to inhibitor Pd130328, inhibitor binding structure and analysis
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in complex with gem-diol inhibitor PD-135,040, hanging-drop vapour-diffusion method, space group P2(1), unit-cell parameters a : 53.20, b : 73.25, c : 46.00
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of inhibition of endothiapepsin by cyclohexyl renin inhibitors
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of the complex between endothiapepsin and an oligopeptide inhibitor
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sitting drop vapor diffusion method, using 0.1 M NH4Ac, 0.1 M acetate buffer, pH 4.6, and 26% (w/v) PEG 4000
space group P2(1), in complex with H189 unit cell parameters a : 42.48, b : 75.78, c : 42.99, in complex with CP-80,794 unit cell parameters a : 42.55, b : 74.62, c : 44.43, in complex with CP-129,541 unit cell parameters a : 42.47, b : 74.31, c : 42.81, in complex with PD-130,328 unit cell parameters a : 43.88, b : 75.44, c : 43.23, in complex with H256 unit cell parameters a : 43.88, b : 75.44, c : 43.23
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three-dimensional structure of endothiapepsin complexed with a transition-state isostere inhibitor of renin
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using ammonium sulfate as precipitant at pH 4.6, X-ray diffraction structure determination and analysis at 2.1 A resolution, multiple isomorphous replacement
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X-ray crystallographic analysis
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complexed with H261, crystals grow in two different crystal forms with the same monoclinic sopace group, P2(1), unit cell parameters a : 43.0A, b : 75.7A, c : 42.9A
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structure studied by neutron crystallography, crystals are monocliic, P2(1), unit cell dimensions a : 43.1 A, b : 75.7 A, c : 42.9 A, endothiapepsin-H261 complex
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