3.4.22.B5: CPB protease
This is an abbreviated version!
For detailed information about CPB protease, go to the full flat file.
Reaction
good cleavage of the Arg-Phe bond. The best substrate ortho-aminobenzoyl-KLR-/-FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) is also well hydrolyzed by cathepsin L, however the best inhibitor of the parasite enzyme ortho-aminobenzoyl-KLRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) has low affinity to cathepsin L
=
Synonyms
C01.074, CPB, cpb-like, CPB1, CPB10, CPB11, CPB12, CPB13, CPB14, CPB15, CPB16, CPB17, CPB18, CPB19, CPB2, CPB2.3, CPB2.8, CPB3, CPB3.0, CPB4, CPB5, CPB6, CPB7, CPB8, CPB9, cystein protease CPB2.8, cysteine peptidase, cysteine peptidase B, cysteine protease B, cysteine protease CPB, cysteine proteinase B, cysteine proteinase type I, cysteine-proteinase B, LBRM_08_0810, LBRM_08_0820, LBRM_08_0830, LdcCys1, type I cysteine protease
ECTree
Cloned
Cloned on EC 3.4.22.B5 - CPB protease
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expressed in Escherichia coli
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expression in Escherichia coli
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expression of CPB2.3DELTACTE (truncated CPB2.3 lacking the C-terminal extension) in Escherichia coli
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overexpression of CPB2.8 as an inactive pro-form lacking the characteristic C-terminal extension, CPB2.8DELTACTE in Escherichia coli. Pro-region processing is initiated during protein refolding and proceeds through several intermediate stages. Maximum enzyme activity after removal of the entire pro-region. This is facilitated by acidification
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recombinant expression of the amastigote-specific isoform CPB2.8, expressed without the C-terminal extension, termed CPB2.8DEKTACTE
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subcloned into pET-23a for expression in Escherichia coli BL21 (DE3) pLysS cells
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