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3.4.23.23: Mucorpepsin

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

Word Map on EC 3.4.23.23

Reaction

Hydrolysis of proteins, favouring hydrophobic residues at P1 and P1'. Clots milk. Does not accept Lys at P1, and hence does not activate trypsinogen =

Synonyms

acid proteinase, aspartic protease, Aspartic proteinase, aspartyl proteinase, EC 3.4.23.6, EC 3.4.4.17, fibrinolytic enzyme, Fromase 100, Fromase 46TL, MCAP, MMP, MPR, Mucor acid protease, Mucor acid proteinase, Mucor aspartic proteinase, Mucor miehei aspartic protease, Mucor miehei aspartic proteinase, Mucor miehei rennin, Mucor pusillus emporase, Mucor pusillus pepsin, Mucor pusillus rennin, Mucor rennin, Proteinase, Mucor aspartic, R. pusillus pepsin, rennin, RMP

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.23 Mucorpepsin

Crystallization

Crystallization on EC 3.4.23.23 - Mucorpepsin

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallizes in the orthorhombic space group P2(1)2(1)2(1), a : 41.86 A, b : 51.21 A, c : 174.24 A
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hanging-drop method, orthorhombic space group P2(1)2(1)2(1), cell dimensions a : 41.86 A, b : 51.21 A, c : 174.24 A
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small thin needle-like seed crystals of the native enzyme grown by the hanging-drop vapour-diffusion method, unit-cell dimensions a : 41.82 A, 51.21 A, c : 174.24 A, in complex with inhibitor pepstatin A, orthorhombic space group P2(1)2(1)2(1), isomorphous to native RMP crystals, unit-cell dimensions are a : 41.52 A, b : 50.82 A, c : 172.71 A
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mutant Y75N in complex with human renin inhibitor CP-113972
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structure and refinement at 2.0 A resolution
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