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Cited by 66Neuropeptides and Animal PhysiologyTrace Elements in HealthMetal-Catalyzed Oxygenation Mechanisms

Peptidylgycine α‐amidating monooxygenase and copper: A gene–nutrient interaction critical to nervous system function

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Bousquet‐Moore, Danielle, Mains, Richard E., Eipper, Betty A.·2010·Journal of Neuroscience Research
DOI 10.1002/jnr.22404PMC PMC3732055
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Abstract

Peptidylgycine alpha-amidating monooxygenase (PAM), a highly conserved copper-dependent enzyme, is essential for the synthesis of all amidated neuropeptides. Biophysical studies revealed that the binding of copper to PAM affects its structure, and cell biological studies demonstrated that the endocytic trafficking of PAM was sensitive to copper. We review data indicating that genetic reduction of PAM expression and mild copper deficiency in mice cause similar alterations in several physiological functions known to be regulated by neuropeptides: thermal regulation, seizure sensitivity, and anxiety-like behavior.

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  • Ascorbate likely enables conversion between a cupric and cuprous state and is reduced stoichiometrically to an ascorbyl radical in PAM.

    “Ascorbate likely enables conversion between a cupric and cuprous state and is reduced stoichiometrically to an ascorbyl radical.”

    From Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination (2021) · cites this paper as [149]

    In “The binding of copper to PAM allows it to function as a copper sensor” (page unavailable), the paper says that ascorbic acid normally catalyzes reduction of PAM’s copper ions from Cu(II) to Cu(I). It does not say that ascorbate is reduced stoichiometrically to an ascorbyl radical. (LLM, conf=0.87)

    Experimental — accuracy not yet measured

  • PAM catalyzes two-step carboxyterminal amidation of peptides.

    “PAM is a bifunctional enzyme catalyzing two-step carboxyterminal amidation of peptides.”

    From Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination (2021) · cites this paper as [149]

  • The hydroxylation active site of PAM is composed of two copper ions and the corresponding reaction is ascorbate-dependent.

    “The former active site is composed of two copper ions and the corresponding reaction is ascorbate-dependent.”

    From Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination (2021) · cites this paper as [149]

  • PAM is the only known human enzyme able to catalyze α-amidation of peptides.

    “It is the only known human enzyme able to catalyze α-amidation of peptides [72,147,148,149].”

    From Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination (2021) · cites this paper as [149]

  • Other reductants can replace ascorbic acid in PAM but are less potent.

    “Other reductants can replace ascorbic acid but are less potent [4,72,147,148,149].”

    From Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination (2021) · cites this paper as [149]

    The section “The binding of copper to PAM allows it to function as a copper sensor” says ascorbic acid normally reduces PAM’s copper residues. It does not address whether other reductants can replace ascorbic acid or whether they are less potent; searches for alternative reductants found no passage establishing either point. No page number is available in our copy. (LLM, conf=0.72)

    Experimental — accuracy not yet measured

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Cited by

Sorted by citations

Authors
Bousquet‐Moore, D., Mains, R. E., & Eipper, B. A.
Affiliations
UConn Health (US)
Corresponding author
Eipper, Betty A.
ORCID
Venue
Journal of Neuroscience Research
Publisher
Wiley
Published
2010-07-15
Volume
88
Issue
12
Pages
2535-2545
ISSN
  • 0360-4012 (ISSN-L)
  • 1097-4547
DOI
10.1002/jnr.22404
PMC
PMC3732055
OpenAlex
W2143880121
Cited by
66
References
0
Citations by year
2026: 1 · 2025: 3 · 2024: 8 · 2023: 5 · 2022: 4 · 2021: 5 · 2020: 3 · 2019: 3 · 2018: 3 · 2017: 5 · 2016: 5 · 2015: 7 · 2014: 7 · 2013: 4 · 2012: 3
FWCI
0.20
Type
journal article
Language
en
Open access
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations
  • Journal of Neuroscience Research (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • National Institute of Mental Health (F31MH080589, MH-80589)
  • National Institute of Diabetes and Digestive and Kidney Diseases (DK-32948, R01DK032948, DK32949, R01DK032949)
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuropeptides and Animal Physiology
  • Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
  • Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Keywords
peptidylglycine alpha-amidating monooxygenase, PAM, copper, gene-nutrient interactions, neuropeptide biosynthesis, copper deficiency, endosomal trafficking, temperature regulation, seizure susceptibility, anxiety-like behavior, nervous system function
MeSH terms
Animals, Copper, Cytosol, Disease Models, Animal, Endocytosis, Heart Atria, Humans, Mixed Function Oxygenases, Multienzyme Complexes, Nervous System Diseases, Neuropeptides, Pituitary Diseases, Gene Expression Regulation, Enzymologic, Protein Transport, Mice

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