Target type: biologicalprocess
The chemical reactions and pathways resulting in the breakdown of neuropeptides. Neuropeptides are signaling peptides that travel across a synaptic junction. [GOC:BHF, GOC:dph, GOC:tb]
Neuropeptide catabolic processes encompass the enzymatic breakdown of neuropeptides, which are short chains of amino acids that serve as signaling molecules in the nervous system. These processes play a crucial role in regulating neurotransmission, influencing a wide array of physiological functions, including mood, behavior, pain perception, and stress response.
The breakdown of neuropeptides typically begins with the action of peptidases, enzymes that specifically cleave peptide bonds. Different peptidases exhibit substrate specificity, targeting specific neuropeptide sequences and contributing to their inactivation.
Examples of peptidases involved in neuropeptide catabolism include:
* **Aminopeptidases**: These enzymes cleave amino acids from the N-terminus of a peptide chain.
* **Carboxypeptidases**: These enzymes remove amino acids from the C-terminus of a peptide chain.
* **Dipeptidyl peptidases**: These enzymes cleave dipeptides (two amino acid units) from the N-terminus of a peptide chain.
The catabolic process can occur in different cellular compartments:
* **Synapse**: Neuropeptides released from presynaptic neurons can be degraded in the synaptic cleft by peptidases, limiting their signaling duration.
* **Extracellular space**: Neuropeptides diffusing away from the synapse can also undergo catabolism in the extracellular environment.
* **Cellular compartments**: Neuropeptides internalized by cells can be targeted for degradation within lysosomes or other cellular compartments.
The breakdown products of neuropeptide catabolism are often inactive and can be further metabolized or excreted from the body.
Dysregulation of neuropeptide catabolic processes can contribute to various neurological and psychiatric disorders, highlighting the importance of maintaining proper neuropeptide homeostasis.'
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Protein | Definition | Taxonomy |
---|---|---|
Pro-cathepsin H | A cathepsin H that is encoded in the genome of human. [PRO:DNx, UniProtKB:P09668] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
---|---|---|---|
leupeptin | aldehyde; tripeptide | bacterial metabolite; calpain inhibitor; cathepsin B inhibitor; EC 3.4.21.4 (trypsin) inhibitor; serine protease inhibitor | |
e 64 | E 64: cysteine protease inhibitor of microbial origin, which inhibits cathepsin B (EC 3.4.22.1) and cathepsin L (EC 3.4.22.-) | dicarboxylic acid monoamide; epoxy monocarboxylic acid; guanidines; L-leucine derivative; zwitterion | antimalarial; antiparasitic agent; protease inhibitor |
pepstatin | pepstatin: inhibits the aspartic protease endothiapepsin | pentapeptide; secondary carboxamide | bacterial metabolite; EC 3.4.23.* (aspartic endopeptidase) inhibitor |
ca 074 | |||
odanacatib | odanacatib: a selective inhibitor of cathepsin K for the treatment of post-menopausal osteoporosis; structure in first source | ||
calpain inhibitor iii | calpain inhibitor III: potential anticataract drug | ||
gallinamide a | gallinamide A: antimalarial peptide from marine cyanobacteria | ||
6-(3,5-difluoroanilino)-9-ethyl-2-purinecarbonitrile | 6-aminopurines | ||
9-(3,5-difluorophenyl)-6-(ethylamino)-2-purinecarbonitrile | imidazoles | ||
grassystatin a | grassystatin A: isolated from a cyanobacterium, identified as Lyngbya cf.; structure in first source |