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Research Communications |
-amidating enzyme precursor that generates five distinct enzymes
a Department of Molecular and Cellular Neurobiology, Graduate School Neurosciences Amsterdam, Research Institute Neurosciences Vrije Universiteit, 1081 HV Amsterdam, The Netherlands; and
b Department of Neuroscience, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
Mechanisms underlying the specificity and efficiency of
enzymes,which modify peptide messengers, especially with the variable
requirements of synthesis in the neuronal secretory pathway, are poorly
understood. Here, we examine the process of peptide 
-amidation in
individually identifiable Lymnaea neurons that synthesize
multiple proproteins, yielding complex mixtures of structurally diverse
peptide substrates. The -amidation of these peptide substrates is
efficiently controlled by a multifunctional Lymnaea
peptidyl glycine -amidating monooxygenase (LPAM), which contains
four different copies of the rate-limiting Lymnaea peptidyl
glycine -hydroxylating monooxygenase (LPHM) and a single
Lymnaea peptidyl -hydroxyglycine -amidating lyase.
Endogenously, this zymogen is converted to yield a mixture of
monofunctional isoenzymes. In vitro, each LPHM displays a
unique combination of substrate affinity and reaction velocity,
depending on the penultimate residue of the substrate. This suggests
that the different isoenzymes are generated in order to efficiently
amidate the many peptide substrates that are present in molluscan
neurons. The cellular expression of the LPAM gene is
restricted to neurons that synthesize amidated peptides, which
underscores the critical importance of regulation of peptide
-amidation.—Spijker, S., Smit, A. B., Eipper, B. A.,
Malik, A., Mains, R. E., Geraerts, W. P M. A molluscan peptide
-amidating enzyme precursor that generates five distinct enzymes.
Key Words: posttranslational modification • neuropeptide -amidation • PAM • mono-oxygenase • mollusk Lymnaea stagnalis
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