L to D amino acid isomerization in a peptide hormone is a late post-translational event occurring in specialized neurosecretory cells.
J Biol Chem
; 275(48): 37870-5, 2000 Dec 01.
Article
em En
| MEDLINE
| ID: mdl-10993902
ABSTRACT
Modification of the chirality of a single amino acid residue within a peptide chain appears to be novel additional mechanism leading to structural and functional diversification of eukaryotic bioactive peptides. This phenomenon has been studied at the cellular level in a neuroendocrine organ which elaborates a mixture of diastereoisomers of a 72-residue neuropeptide, crustacean hyperglycemic hormone. For the first time, amino acid isomerization has been shown to occur in the perikarya of fully specialized neurosecretory cells, as a late step of the maturation of the hyperglycemic hormone precursor and after propeptide cleavage. The specificity and efficiency of this phenomenon indicates the existence of a new enzyme family involved in the biogenesis of peptide hormones.
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Base de dados:
MEDLINE
Assunto principal:
Processamento de Proteína Pós-Traducional
/
Proteínas do Tecido Nervoso
Limite:
Animals
Idioma:
En
Revista:
J Biol Chem
Ano de publicação:
2000
Tipo de documento:
Article
País de afiliação:
França