Biology:Carboxypeptidase A inhibitor
| Carboxypeptidase A inhibitor | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 refined crystal structure of the potato inhibitor complex of carboxypeptidase a at 2.5 angstroms resolution | |||||||||
| Identifiers | |||||||||
| Symbol | ? | ||||||||
| Pfam | PF02977 | ||||||||
| Pfam clan | CL0096 | ||||||||
| InterPro | IPR004231 | ||||||||
| SCOP2 | 4cpa / SCOPe / SUPFAM | ||||||||
| |||||||||
In molecular biology, the carboxypeptidase A inhibitor family is a family of proteins which is represented by the well-characterised metallocarboxypeptidase A inhibitor (MCPI) from potatoes, which belongs to the MEROPS inhibitor family I37, clan IE. It inhibits metallopeptidases belonging to MEROPS peptidase family M14, carboxypeptidase A. In Russet Burbank potatoes, it is a mixture of approximately equal amounts of two polypeptide chains containing 38 or 39 amino acid residues. The chains differ in their amino terminal sequence only [1] and are resistant to fragmentation by proteases.[2] The structure of the complex between bovine carboxypeptidase A and the 39-amino-acid carboxypeptidase A inhibitor from potatoes has been determined at 2.5-Angstrom resolution.[3]
The potato inhibitor is synthesised as a precursor, having a 29 amino acid N-terminal signal peptide, a 27 amino acid pro-peptide, the 39 amino acid mature inhibitor region and a 7 amino acid C-terminal extension. The 7 amino acid C-terminal extension is involved in inhibitor inactivation and may be required for targeting to the vacuole where the mature active inhibitor accumulates.[4]
The N-terminal region and the mature inhibitor are weakly related to other solananaceous proteins found in this family, from potato, tomato and henbane, which have been incorrectly described as metallocarboxypeptidase inhibitors.[5]
References
- ↑ "The amino acid sequence of a carboxypeptidase inhibitor from potatoes". Biochemistry 14 (6): 1334–42. March 1975. doi:10.1021/bi00677a036. PMID 1122280.
- ↑ "Structure of potato carboxypeptidase inhibitor: disulfide pairing and exposure of aromatic residues". Biochemistry 18 (11): 2252–6. May 1979. doi:10.1021/bi00578a018. PMID 444453.
- ↑ "Structure of the potato inhibitor complex of carboxypeptidase A at 2.5-A resolution". Proc. Natl. Acad. Sci. U.S.A. 77 (8): 4633–7. August 1980. doi:10.1073/pnas.77.8.4633. PMID 6933511.
- ↑ "Characterization of the wound-induced metallocarboxypeptidase inhibitor from potato. cDNA sequence, induction of gene expression, subcellular immunolocalization and potential roles of the C-terminal propeptide". FEBS Lett. 440 (1–2): 175–82. November 1998. doi:10.1016/S0014-5793(98)01447-1. PMID 9862450.
- ↑ "Tissue-specific signal(s) activate the promoter of a metallocarboxypeptidase inhibitor gene family in potato tuber and berry". Plant Mol. Biol. 46 (3): 301–11. June 2001. doi:10.1023/A:1010649503229. PMID 11488477.
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