The processing of peptide precursors

FEBS Letters

Schwartz, Thue W.¹ 

[1] Laboratory of Molecular Endocrinology, University Department of Clinical Chemistry, Rigshospitalet 6321, DK-2100 Copenhagen, Denmark

关键词: Post-translational modification Hormone Neuropeptide Growth factor cDNA deduced precursor Tissue-specific processing;   

DOI  :  10.1016/0014-5793(86)80500-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The classical conversion site in precursors of regulatory peptides is a sequence of two basic amino acids. During recent years, however, a group of monobasic cleavage sites has emerged. In certain cell systems it has been shown that the monobasic cleavage mechanism is both a specific mechanism which only attacks a particular basic residue, and a distinct mechanism which can be separated from the dibasic cleaving mechanism within the same cell. The vast majority of monobasic cleavages occur at single arginines although cleavage after a lysine residue has also been demonstrated. There is no ‘consensus sequence’ of amino acids surrounding the single basic residue which is the apparent signal for proteolytic processing. However, in approximately one third of the cases, a proline residue is found either just before or just after the basic residue. On the basis of this ‘proline-directed arginyl cleavage’ it is discussed how the conformation of the peptide backbone might be important for this type of cleavage. Finally, it is suggested that tissue-specific expression of different processing enzymes, e.g. dibasic and monobasic specific forms, might explain the tissue-specific processing of precursors like the pro-opiomelanocortin and the CKK. and somatostatin precursor.

【 授权许可】

Unknown