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Literature summary for 3.4.25.1 extracted from

  • Kupperman, E.; Lee, E.C.; Cao, Y.; Bannerman, B.; Fitzgerald, M.; Berger, A.; Yu, J.; Yang, Y.; Hales, P.; Bruzzese, F.; Liu, J.; Blank, J.; Garcia, K.; Tsu, C.; Dick, L.; Fleming, P.; Yu, L.; Manfredi, M.; Rolfe, M.; Bolen, J.
    Evaluation of the proteasome inhibitor MLN9708 in preclinical models of human cancer (2010), Cancer Res., 70, 1970-1980.
    View publication on PubMed
Search for more literature for 3.4.25.1

Application

Application Comment Organism
medicine proteasome inhibitors are used for the treatment of multiple myeloma and recurring mantle cell lymphoma, e.g. inhibitors MLN9708 and bortezomib, overview Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
bortezomib
-
 Homo sapiens
bortezomib
-
 Mus musculus
carfilzomib irreversible Homo sapiens
carfilzomib irreversible Mus musculus
CEP-18770 reversible Homo sapiens
CEP-18770 reversible Mus musculus
MLN9708 an N-capped dipeptidyl leucine boronic acid, a potent inhibitor of the proteasome in tumor cells Homo sapiens
MLN9708 an N-capped dipeptidyl leucine boronic acid, a potent inhibitor of the proteasome in tumor cells Mus musculus
additional information MLN9708 has a shorter proteasome dissociation half-life and improved pharmacokinetics, pharmacodynamics, and antitumor activity compared with bortezomib in clinical trials Homo sapiens
additional information MLN9708 has a shorter proteasome dissociation half-life and improved pharmacokinetics, pharmacodynamics, and antitumor activity compared with bortezomib in clinical trials Mus musculus
NPI-0052 irreversible Homo sapiens
NPI-0052 irreversible Mus musculus

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Mus musculus
-
 female CB17-SCID mice
-

Source Tissue

Source Tissue Comment Organism Textmining
carcinoma cell
-
 Mus musculus
-
carcinoma cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
succinyl-LLVY-aminoluciferin + H2O chymotrypsin-like proteasome activity Mus musculus succinyl-LLVY + aminoluciferin
-
 ?
succinyl-LLVY-aminoluciferin + H2O chymotrypsin-like proteasome activity Homo sapiens succinyl-LLVY + aminoluciferin
-
 ?

Synonyms

Synonyms Comment Organism
20S proteasome
-
 Mus musculus
20S proteasome
-
 Homo sapiens
26S proteasome
-
 Mus musculus
26S proteasome
-
 Homo sapiens
proteasome
-
 Mus musculus
proteasome
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Mus musculus
37
-
 assay at Homo sapiens

General Information

General Information Comment Organism
additional information the 26S proteasome consists of a 20S multicatalytic core capped on either end with 19S regulatory subunits. The 20S proteasome is a chambered, barrel-like structure containing two heptameric rings made from alpha subunits and two heptameric rings made from beta subunits. The alpha rings perform capping and gating functions, whereas three of the beta subunits, beta1, beta2, and beta5, contain the NH2-terminal threonines responsible for the different proteasome proteolytic activities. The beta1, beta2, and beta5 subunits are referred to as caspase-like, trypsin-like, and chymotrypsin-like, respectively Mus musculus
additional information the 26S proteasome consists of a 20S multicatalytic core capped on either end with 19S regulatory subunits. The 20S proteasome is a chambered, barrel-like structure containing two heptameric rings made from alpha subunits and two heptameric rings made from beta subunits. The alpha rings perform capping and gating functions, whereas three of the beta subunits, beta1, beta2, and beta5, contain the NH2-terminal threonines responsible for the different proteasome proteolytic activities. The beta1, beta2, and beta5 subunits are referred to as caspase-like, trypsin-like, and chymotrypsin-like, respectively Homo sapiens