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J. Biol. Chem., Vol. 275, Issue 48, 37870-37875, December 1, 2000
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From the 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.
L to D Amino Acid Isomerization in a
Peptide Hormone Is a Late Post-translational Event Occurring in
Specialized Neurosecretory Cells*
§,
,
¶, and
Laboratoire Signaux Endocrines et Toxines
d'Invertébrés, CNRS EP2028-Univ. Paris 6, Ecole Normale
Supérieure, 46 rue d'Ulm, 75005 Paris and
Service
d'Imagerie, Institut Jacques Monod, CNRS-Univ. Paris 6 and Univ. P7, 2 place Jussieu, 75251 Paris cedex 05, France.
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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