[5] Peptidylglycine α-amidating monooxygenase: An ascorbate-requiring enzyme
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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 [148]
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 [148]
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 [148]
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 [148]
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 [148]
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References 24 · Cited by 50
- Authors
- Kolhekar, A. S., Mains, R. E., & Eipper, B. A.
- Affiliations
- Johns Hopkins University (US)
- Venue
- Methods in Enzymology
- Publisher
- Elsevier
- Published
- 1997
- Volume
- 279
- Pages
- 35-43
- ISSN
- 0076-6879 (ISSN-L)
- OpenAlex
- W2030506502
- Cited by
- 50
- References
- 24
- Citations by year
- 2026: 2 · 2025: 1 · 2023: 3 · 2021: 3 · 2020: 2 · 2019: 1 · 2018: 3 · 2017: 1 · 2016: 1 · 2015: 1 · 2014: 1 · 2013: 2 · 2012: 2
- FWCI
- 4.01
- Type
- book chapter
- Language
- en
- Open access
- closed
- Locations
- Methods in enzymology on CD-ROM/Methods in enzymology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (DK32949)
- Topics
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuropeptides and Animal Physiology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Keywords
- peptidylglycine alpha-amidating monooxygenase, vitamin C, peptidylglycine alpha-hydroxylating monooxygenase, alternative splicing, endoproteolytic cleavage, dopamine beta-monooxygenase
- MeSH terms
- Animals, Ascorbic Acid, Humans, Mixed Function Oxygenases, Multienzyme Complexes, Recombinant Proteins
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