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Literature summary for 3.4.22.B70 extracted from

  • Chen, C.H.; Namanja, A.T.; Chen, Y.
    Conformational flexibility and changes underlying activation of the SUMO-specific protease SENP1 by remote substrate binding (2014), Nat. Commun., 5, 4968.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
drug development SENP1 is an essential gene and is a potential target for developing therapeutic agents for cancer Homo sapiens

Protein Variants

Protein Variants Comment Organism
C603S a catalytically inactive mutant of the SENP1 catalytic domain Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information enzyme-substrate complex formation kinetics, overview Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
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Source Tissue

Source Tissue Comment Organism Textmining
prostate cancer cell
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Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme SENP1 interacts with SUMO1-FL, SUMO1-GG, SUMO11-92 (containing residues 1-92, with C-terminus truncated) or peptides corresponding to the C-terminus of SUMO1. The exchange rates between free SENP1 and SENP1 in complex with SUMO1-FL or SUMO1-GG are mostly slow to intermediate, relative to the NMR chemical shift timescale, and both SUMO-GG and SUMO-FL produce similar chemical shift perturbation. The beta-grasp domain of SUMO1 interacts with enzyme SENP1 in a manner similar to that in the context of SUMO1-FL, effects of beta-grasp domain on the enzyme, overview Homo sapiens ?
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?

Synonyms

Synonyms Comment Organism
SENP1
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Homo sapiens
SUMO-specific protease
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Homo sapiens

General Information

General Information Comment Organism
evolution the enzyme belongs to the superfamily of Ubl-specific proteases being Cys proteases. In all SENPs, an aromatic side chain, such as that of Trp or Phe, forms the channel lid. The catalytic Cys residues are located within the closed catalytic channels for binding the C-termini of ubiquitin-likes, and the catalytic residues undergo conformational changes when these proteases form complexes with their substrates. SENP1 is a model system for the Ubl-specific proteases in the Cys protease superfamily because it shares the same biochemical mechanism and its catalytic Cys is similarly buried as those of other Ubl-specific proteases. The mode of substrate recognition and binding of SENP1 may be shared by other de-Ubl enzymes Homo sapiens
additional information NMR enzyme-substrate complex analysis, the distally bound beta-grasp domain of SUMO1 induces realignment of the catalytic residues that enhance the enzyme activity, mode of substrate recognition and binding, molecular dynamics, overview Homo sapiens
physiological function enzyme SENP1 plays a key role in tumor angiogenesis, because it regulates the stability of hypoxia-inducible factor 1alpha, which is a key player in the formation of new blood vessels to support tumor growth. It is highly expressed in human prostate cancer specimens and regulates androgen receptor activities The enzyme is responsible for processing small ubiquitin-like modifier, SUMO Homo sapiens