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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

Engineering

Engineering on EC 3.4.23.23 - Mucorpepsin

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N331Q
A101T
-
the proteolytic activity of the mutant is similar to the non-mutant enzyme. The milk clotting activity of the mutant is increased compared to the non-mutant enzyme
A101T/G186D
-
the proteolytic activity of the mutant is similar to the non-mutant enzyme. The milk clotting activity of the mutant is increased compared to the non-mutant enzyme
E13A
-
the proteolytic activity of the mutant decreases remarkably to almost a half of that of non-mutant enzyme
E13D
-
the proteolytic activity of the mutant decreases remarkably to almost a half of that of non-mutant enzyme
E13P
-
the proteolytic activity of the mutant decreases remarkably to almost a half of that of non-mutant enzyme
E13Q
-
the proteolytic activity of the mutant decreases remarkably to almost a half of that of non-mutant enzyme
G186D
-
the proteolytic activity of the mutant is similar to the non-mutant enzyme. The milk clotting activity of the mutant is increased compared to the non-mutant enzyme
G186D/E13D
-
the mutant shows a significant milk-clotting activity. The mutant rennet can decrease hydrolysis of protein during ripening of cheese. The mutant has a reduction in thermostability along with a sharp decrease in proteolytic activity
G186D/E13Q
L287G
-
the mutant shows an increase in the ratio of clotting activity to proteolytic activity as compared to the wild type enzyme
T218A/T218S/L287G
-
the mutations lead to a significant decrease in proteolytic activity compared to the wild type enzyme
T218S
-
the mutation causes a low thermostability and moderate increase in the clotting activity compared to the wild type enzyme. The mutant shows a 3.34fold increase in the ratio of clotting activity to proteolytic activity as compared to the wild type enzyme. The mutant can serve as a promising milk coagulant that contributes to an optimal flavor development in mature cheese
Y75N
-
crystallization data