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Literature summary for 3.4.25.1 extracted from

  • Wojcikiewicz, R.J.H.; Xu, Q.; Webster, J.M.; Alzayady, K.; Gao, C.
    Ubiquitination and proteasomal degrdn. of endogenous and exogenous inositol 1,4,5-trisphosphate receptors in aT3-1 anterior pituitary cells (2003), J. Biol. Chem., 278, 940-947.
    View publication on PubMed
Search for more literature for 3.4.25.1

Activating Compound

Activating Compound Comment Organism Structure
additional information occupancy of the caspase-like sites stimulates the trypsin-like activity of the proteasomes Saccharomyces cerevisiae
additional information occupancy of the caspase-like sites stimulates the trypsin-like activity of the proteasomes Oryctolagus cuniculus

Inhibitors

Inhibitors Comment Organism Structure
acetyl-Ala-Pro-norleucine-Leu-Asp-aldehyde 99% inhibition of hydrolysis of acetyl-norleucine-Leu-Pro-norleucine-Leu-Asp-7-amido-4-methylcoumarin, complete inhibition of hydrolysis of acetyl-norleucine-GPLD-7-amido-4-methylcoumarin, 95% inhibition of hydrolysis of acetyl-GPLL-7-amido-4-methylcoumarin, 89% inhibition of hydrolysis of acetyl-Ala-Pro-norleucine-Leu-Leu-7-amido-4-methylcoumarin, 24% inhibition of hydrolysis of succinyl-LLVY-7-amido-4-methylcoumarin, no inhibition of hydrolysis of tert-butyloxycarbonyl-LRR-7-amino-4-methylcoumarin Oryctolagus cuniculus
acetyl-Ala-Pro-norleucine-Leu-Asp-aldehyde
-
 Saccharomyces cerevisiae
AEBSF 25% inhibition of hydrolysis of acetyl-norleucine-Leu-Pro-norleucine-Leu-Asp-7-amino-4-methylcoumarin, 22% inhibition of hydrolysis of acetyl-norleucine-GPLD-7-amido-4-methylcoumarin, 19% inhibition of hydrolysis of acetyl-GPLL-7-amido-4-methylcoumarin, 21% inhibition of hydrolysis of acetyl-Ala-Pro-norleucine-Leu-Leu-7-amido-4-methylcoumarin, 26% inhibition of hydrolysis of succinyl-LLVY-7-amido-4-methylcoumarin, 98% inhibition of hydrolysis of tert-butyloxycarbonyl-LRR-7-amino-4-methylcoumarin Oryctolagus cuniculus
benzyloxycarbonyl-Pro-norleucine-Leu-Asp-aldehyde 99% inhibition of hydrolysis of acetyl-norleucine-Leu-Pro-norleucine-Leu-Asp-7-amino-4-methylcoumarin, complete inhibition of hydrolysis of acetyl-norleucine-GPLD-7-amido-4-methylcoumarin, 95% inhibition of hydrolysis of acetyl-GPLL-7-amido-4-methylcoumarin, 91% inhibition of hydrolysis of acetyl-Ala-Pro-norleucine-Leu-Leu-7-amido-4-methylcoumarin, 12% inhibition of hydrolysis of succinyl-LLVY-7-amido-4-methylcoumarin, no inhibition of hydrolysis of tert-butyloxycarbonyl-LRR-7-amido-4-methylcoumarin Oryctolagus cuniculus
benzyloxycarbonyl-Pro-norleucine-Leu-Asp-aldehyde
-
 Saccharomyces cerevisiae
additional information although inhibitors of the caspase-like sites allosterically inhibit the chymotrypsin-like activity, inhibitors of the caspase-like sites allosterically inhibit the chymotrypsin-like activity. When caspase-like sites are occupied by the uncleaved propeptide or inhibitor, their substrates still inhibit the chymotrypsin like activity Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Oryctolagus cuniculus proteasomes are the primary sites for protein degradation in mammalian cells. Each proteasome particle contains two chymotrypsin-like, two trypsin-like, and two caspase-like proteolytic sites ?
-
 ?

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-
Saccharomyces cerevisiae
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-Ala-Pro-norleucine-Leu-Leu-7-amido-4-methylcoumarin + H2O
-
 Saccharomyces cerevisiae acetyl-Ala-Pro-norleucine-Leu-Leu + 7-amino-4-methylcoumarin
-
 ?
acetyl-Ala-Pro-norleucine-Leu-Leu-7-amido-4-methylcoumarin + H2O
-
 Oryctolagus cuniculus acetyl-Ala-Pro-norleucine-Leu-Leu + 7-amino-4-methylcoumarin
-
 ?
acetyl-GPLD-7-amido-4-methylcoumarin + H2O
-
 Saccharomyces cerevisiae acetyl-GPLD + 7-amino-4-methylcoumarin
-
 ?
acetyl-GPLD-7-amido-4-methylcoumarin + H2O
-
 Oryctolagus cuniculus acetyl-GPLD + 7-amino-4-methylcoumarin
-
 ?
acetyl-GPLE-7-amido-4-methylcoumarin + H2O
-
 Saccharomyces cerevisiae acetyl-GPLE + 7-amino-4-methylcoumarin
-
 ?
acetyl-GPLE-7-amido-4-methylcoumarin + H2O
-
 Oryctolagus cuniculus acetyl-GPLE + 7-amino-4-methylcoumarin
-
 ?
acetyl-GPLL-7-amido-4-methylcoumarin + H2O
-
 Saccharomyces cerevisiae acetyl-GPLL + 7-amino-4-methylcoumarin
-
 ?
acetyl-GPLL-7-amido-4-methylcoumarin + H2O
-
 Oryctolagus cuniculus acetyl-GPLL + 7-amino-4-methylcoumarin
-
 ?
acetyl-norleucine-Leu-Pro-norleucine-Leu-YVAD-7-amido-4-methylcoumarin + H2O
-
 Saccharomyces cerevisiae acetyl-norleucine-Leu-Pro-norleucine-Leu-YVAD + 7-amino-4-methylcoumarin
-
 ?
acetyl-norleucine-Leu-Pro-norleucine-Leu-YVAD-7-amido-4-methylcoumarin + H2O
-
 Oryctolagus cuniculus acetyl-norleucine-Leu-Pro-norleucine-Leu-YVAD + 7-amino-4-methylcoumarin
-
 ?
acetyl-YVAD-7-amido-4-methylcoumarin + H2O
-
 Saccharomyces cerevisiae acetyl-YVAD + 7-amino-4-methylcoumarin
-
 ?
acetyl-YVAD-7-amido-4-methylcoumarin + H2O
-
 Oryctolagus cuniculus acetyl-YVAD + 7-amino-4-methylcoumarin
-
 ?
additional information proteasomes are the primary sites for protein degradation in mammalian cells. Each proteasome particle contains two chymotrypsin-like, two trypsin-like, and two caspase-like proteolytic sites. Caspase-like sites cleave after aspartates better than after glutamates Oryctolagus cuniculus ?
-
 ?
additional information proteasomes are the primary sites for protein degradation in mammalian cells. Each proteasome particle contains two chymotrypsin-like, two trypsin-like, and two caspase-like proteolytic sites Oryctolagus cuniculus ?
-
 ?

Synonyms

Synonyms Comment Organism
20S proteasome
-
 Saccharomyces cerevisiae
26S proteasome
-
 Oryctolagus cuniculus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
 additional information
-
 Oryctolagus cuniculus
0.02
-
 acetyl-Ala-Pro-norleucine-Leu-Asp-aldehyde
-
 Saccharomyces cerevisiae
0.021
-
 benzyloxycarbonyl-Pro-norleucine-Leu-Asp-aldehyde
-
 Saccharomyces cerevisiae