3.4.22.B78: endopepidase PH1704
This is an abbreviated version!
For detailed information about endopepidase PH1704, go to the full flat file.
Reaction
the enzyme prefers substrates with an Arg residue at the P1 site =
Synonyms
PH1704, PH1704 protease, PhpI
ECTree
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General Information
General Information on EC 3.4.22.B78 - endopepidase PH1704
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evolution
additional information
the enzyme is a member of DJ-1/ThiJ/PfpI superfamily that has diverse functional subclasses
evolution
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the enzyme is a member of DJ-1/ThiJ/PfpI superfamily that has diverse functional subclasses
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evolution
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the enzyme is a member of DJ-1/ThiJ/PfpI superfamily that has diverse functional subclasses
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the enzyme has both aminopeptidase and endopeptidase activities, Cys100 is the catalytic nucleophilic residue, residue Tyr120 is important in substrate binding and is involved in enzyme activity to form a hydrogen bond with Cys100 and as an entrance gate of the substrate with Lys43, active site pocket structure, molecular docking study, overview. Cys100, His101, and Glu474 function as a catalytic triad. Active residues are Glu12, Glu15, Lys43, Gly70, Arg71, Cys100, His101, Tyr120, Val150, Arg471, Glu474, and Arg475
additional information
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the enzyme has both aminopeptidase and endopeptidase activities, Cys100 is the catalytic nucleophilic residue, residue Tyr120 is important in substrate binding and is involved in enzyme activity to form a hydrogen bond with Cys100 and as an entrance gate of the substrate with Lys43, active site pocket structure, molecular docking study, overview. Cys100, His101, and Glu474 function as a catalytic triad. Active residues are Glu12, Glu15, Lys43, Gly70, Arg71, Cys100, His101, Tyr120, Val150, Arg471, Glu474, and Arg475
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additional information
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the enzyme has both aminopeptidase and endopeptidase activities, Cys100 is the catalytic nucleophilic residue, residue Tyr120 is important in substrate binding and is involved in enzyme activity to form a hydrogen bond with Cys100 and as an entrance gate of the substrate with Lys43, active site pocket structure, molecular docking study, overview. Cys100, His101, and Glu474 function as a catalytic triad. Active residues are Glu12, Glu15, Lys43, Gly70, Arg71, Cys100, His101, Tyr120, Val150, Arg471, Glu474, and Arg475
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