Difference between revisions of "Part:BBa K4613001"

Revision as of 17:32, 8 October 2023

Mature Carboxypeptidase A（M-CPA）

Carboxypeptidase A (CPA), derived from bovine pancreas, is a 47 kDa zinc-dependent metal carboxypeptidase. Mature Carboxypeptidase A (M-CPA) removed the signal peptide composed of 16 amino acid residues and the leading peptide composed of 94 amino acid residues and contains a mature peptide of composed of 309 amino acid residues (35kDa). Mature Carboxypeptidase A has an efficient capacity to hydrolyze ochratoxin α (OTA) into the non-toxic product ochratoxin α and L-α-phenylalanine (Phe). The degradation rate was up to 93.36%. Compared with commercial CPA (S-CPA), M-CPA obtained better thermal tolerance and stability at a wider range of pH.

Fig.1 Enzymatic properties of Mature Carboxypeptidase A(M-CPA) and commercial Carboxypeptidase A (S-CPA) (a) The optimum temperature of M-CPA and S-CPA; (b) The thermal tolerance of M-CPA and S-CPA; (c) The optimum pH of M-CPA and S-CPA; (d) enzymatic dynamic response curve of M-CPA and S-CPA.

Due to its high efficiency and stability, M-CPA can be an ideal enzyme for our project.

Reference

Xiong L, Peng M, Zhao M, et al. Truncated expression of a carboxypeptidase a from bovine improves its enzymatic properties and detoxification efficiency of ochratoxin A[J]. Toxins, 2020, 12(11): 680.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
INCOMPATIBLE WITH RFC[21]
Illegal BglII site found at 88
23
COMPATIBLE WITH RFC[23]
25
INCOMPATIBLE WITH RFC[25]
Illegal AgeI site found at 198
1000
COMPATIBLE WITH RFC[1000]

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 <partinfo>BBa_K4613001 short</partinfo>
-Carboxypeptidase A&#65288;CPA), derived from bovine pancreas, is a 47 kDa zinc-dependent metal carboxypeptidase. Mature Carboxypeptidase A(M-CPA) removed the signal peptide composed of 16 amino acid residues and the leading peptide composed of 94 amino acid residues and contains a mature peptide of composed of 309 amino acid residues(35kDa).
+Carboxypeptidase A (CPA), derived from bovine pancreas, is a 47 kDa zinc-dependent metal carboxypeptidase. Mature Carboxypeptidase A (M-CPA) removed the signal peptide composed of 16 amino acid residues and the leading peptide composed of 94 amino acid residues and contains a mature peptide of composed of 309 amino acid residues (35kDa).
-Mature Carboxypeptidase A has an efficient capacity to hydrolyze OTA into the non-toxic product ochratoxin &#945; and L-&#945;-phenylalanine (Phe). The degradation rate was up to 93.36%. Compared with commercial CPA(S-CPA), M-CPA obtained better thermal tolerance and stability at a wider range of pH.
+Mature Carboxypeptidase A has an efficient capacity to hydrolyze ochratoxin α (OTA) into the non-toxic product ochratoxin &#945; and L-&#945;-phenylalanine (Phe). The degradation rate was up to 93.36%. Compared with commercial CPA (S-CPA), M-CPA obtained better thermal tolerance and stability at a wider range of pH.
+<html>
+<center><img src="https://static.igem.wiki/teams/4613/wiki/parts/parts/mcpa-wenxian-wendingxingduibi.png"with="1000" height="" width="500" height=""/></center>
+</html>
+<p style="text-align: center!important;"><b>Fig.1 Enzymatic properties of Mature Carboxypeptidase A(M-CPA) and commercial Carboxypeptidase A (S-CPA)
+(a) The optimum temperature of M-CPA and S-CPA;
+(b) The thermal tolerance of M-CPA and S-CPA;
+(c) The optimum pH of M-CPA and S-CPA;
+(d) enzymatic dynamic response curve of M-CPA and S-CPA.</b></p>
+Due to its high efficiency and stability, M-CPA can be an ideal enzyme for our project.
+==== Reference ====
+#Xiong L, Peng M, Zhao M, et al. Truncated expression of a carboxypeptidase a from bovine improves its enzymatic properties and detoxification efficiency of ochratoxin A[J]. Toxins, 2020, 12(11): 680.
 <!-- Add more about the biology of this part here