Page last updated: 2024-10-24

inhibition of cysteine-type endopeptidase activity

Definition

Target type: biologicalprocess

Any process that prevents the activation of an inactive cysteine-type endopeptidase. [GOC:mtg_apoptosis, PMID:20383739]

Cysteine-type endopeptidase activity inhibition is a complex process that involves the interaction of a variety of molecules, including the enzyme itself, the inhibitor, and other cellular components. Cysteine-type endopeptidases are a class of proteases that use a cysteine residue in their active site to cleave peptide bonds. They are involved in a wide range of cellular processes, including protein degradation, signal transduction, and cell death. Inhibition of cysteine-type endopeptidase activity can occur through a variety of mechanisms, including the following:

1. **Binding to the active site:** Many cysteine-type endopeptidase inhibitors bind directly to the active site of the enzyme, preventing it from binding to its substrate. These inhibitors are often designed to mimic the transition state of the peptide bond cleavage reaction.
2. **Modification of the active site:** Some cysteine-type endopeptidase inhibitors modify the active site of the enzyme, either by reacting with the cysteine residue itself or by modifying nearby residues. These modifications can inactivate the enzyme by preventing it from binding to its substrate or by changing its conformation.
3. **Inhibition of enzyme synthesis:** Some inhibitors prevent the synthesis of cysteine-type endopeptidases, either by blocking the transcription or translation of the enzyme gene or by inhibiting the activity of enzymes involved in the biosynthesis of the enzyme.
4. **Activation of endogenous inhibitors:** Some cysteine-type endopeptidase inhibitors work by activating endogenous inhibitors of the enzyme. These endogenous inhibitors may be proteins, peptides, or small molecules that bind to the enzyme and prevent its activity.

The specific mechanism of inhibition depends on the particular inhibitor and the cysteine-type endopeptidase being targeted. However, all of these mechanisms ultimately lead to the same outcome: the inhibition of cysteine-type endopeptidase activity. This inhibition can have a variety of effects on cellular processes, depending on the role of the enzyme in the cell. For example, inhibition of cysteine-type endopeptidases involved in protein degradation can lead to the accumulation of misfolded proteins, which can contribute to disease. Inhibition of cysteine-type endopeptidases involved in signal transduction can disrupt cell signaling pathways, which can affect cell growth, differentiation, and survival. Inhibition of cysteine-type endopeptidases involved in cell death can prevent apoptosis, which can contribute to cancer development.

The inhibition of cysteine-type endopeptidase activity is a complex process with a wide range of potential consequences. Further research is needed to fully understand the effects of this inhibition on cellular processes and to develop effective strategies for manipulating these enzymes for therapeutic purposes.'
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Proteins (1)

ProteinDefinitionTaxonomy
E3 ubiquitin-protein ligase XIAPA baculoviral IAP repeat-containing protein 4 that is encoded in the genome of human. [PRO:CNA, UniProtKB:P98170]Homo sapiens (human)

Compounds (12)

CompoundDefinitionClassesRoles
embelinembelin : A member of the class of dihydroxy-1,4-benzoquinones that is 2,5-dihydroxy-1,4-benzoquinone which is substituted by an undecyl group at position 3. Isolated from Lysimachia punctata and Embelia ribes, it exhibits antimicrobial, antineoplastic and inhibitory activity towards hepatitis C protease.

embelin: from Embelia fruit (Myrsinaceae)
dihydroxy-1,4-benzoquinonesantimicrobial agent;
antineoplastic agent;
hepatitis C protease inhibitor;
plant metabolite
phenylalanineL-phenylalanine : The L-enantiomer of phenylalanine.

phenylalanine : An aromatic amino acid that is alanine in which one of the methyl hydrogens is substituted by a phenyl group.

Phenylalanine: An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.
amino acid zwitterion;
erythrose 4-phosphate/phosphoenolpyruvate family amino acid;
L-alpha-amino acid;
phenylalanine;
proteinogenic amino acid
algal metabolite;
EC 3.1.3.1 (alkaline phosphatase) inhibitor;
Escherichia coli metabolite;
human xenobiotic metabolite;
micronutrient;
mouse metabolite;
nutraceutical;
plant metabolite;
Saccharomyces cerevisiae metabolite
kaempferol7-hydroxyflavonol;
flavonols;
tetrahydroxyflavone
antibacterial agent;
geroprotector;
human blood serum metabolite;
human urinary metabolite;
human xenobiotic metabolite;
plant metabolite
kaempferol 3-o-rhamnosideafzelin : A glycosyloxyflavone that is kaempferol attached to an alpha-L-rhamnosyl residue at position 3 via a glycosidic linkage.

kaempferol 3-O-rhamnoside: from apple (Malus domestica) leaves; structure in first source
glycosyloxyflavone;
monosaccharide derivative;
trihydroxyflavone
anti-inflammatory agent;
antibacterial agent;
plant metabolite
lbw242LBW242: proapoptotic IAP inhibitor; low MW Smac (Second mitochondria-derived activator of caspases) mimetic; structure in first source
sm 164SM 164: a bivalent Smac mimetic with antineoplastic activity; structure in first sourcebenzenes;
organic heterobicyclic compound;
secondary carboxamide;
triazoles
antineoplastic agent;
apoptosis inducer;
radiosensitizing agent
lcl1611,3-thiazoles;
aromatic ketone;
L-alanine derivative;
monofluorobenzenes;
N-acylpyrrolidine
antineoplastic agent;
apoptosis inducer
at 406
gdc-0152GDC-0152: structure in first source
birinapantbirinapant: a Smac mimetic with antineoplastic activitydipeptide
nvp-cgm097NVP-CGM097: an MDM2 and HDM2 inhibitor; structure in first source
2-carboxyarabinitol 1-phosphate