The Function of PAM
Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
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Top Gene-Substance Interactions
PAM Interacts with These Diseases
Disease | Score |
Substances That Increase PAM
Substances | Interaction | Organism | Category |
Substances That Decrease PAM
Substances | Interaction | Organism | Category |
Conditions with Increased Gene Activity
Condition | Change (log2fold) | Comparison | Species | Experimental variables | Experiment name |
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Conditions with Decreased Gene Activity
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Technical
The following transcription factors affect gene expression:
Enzyme Regulation:
Inhibited by EDTA, phenylglyoxal and diethyl pyrocarbonate.
Cofactor:
Binds 2 copper ions per subunit for the monoxygenase reaction.
Molecular Function:
- Calcium Ion Binding
- Copper Ion Binding
- L-Ascorbic Acid Binding
- Peptidylamidoglycolate Lyase Activity
- Peptidylglycine Monooxygenase Activity
- Zinc Ion Binding
Biological Processes:
- Central Nervous System Development
- Heart Development
- Lactation
- Limb Development
- Long-Chain Fatty Acid Metabolic Process
- Maternal Process Involved In Female Pregnancy
- Odontogenesis
- Ovulation Cycle Process
- Peptide Amidation
- Protein Amidation
- Protein Homooligomerization
- Regulation Of Actin Cytoskeleton Organization
- Regulation Of Protein Secretion
- Regulation Of Transcription From Rna Polymerase Ii Promoter
- Response To Copper Ion
- Response To Estradiol
- Response To Glucocorticoid
- Response To Hypoxia
- Response To Ph
- Toxin Metabolic Process
Drug Bank:
- Vitamin C