3.4.22.B70: SENP1 peptidase
This is an abbreviated version!
For detailed information about SENP1 peptidase, go to the full flat file.
Word Map on EC 3.4.22.B70
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3.4.22.B70
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desumoylation
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deconjugating
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senp-1
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medicine
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sumo-modified
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senp1-mediated
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drug development
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ranbp2
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sumo-2
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diagnostics
- 3.4.22.B70
-
desumoylation
-
deconjugating
-
senp-1
- medicine
-
sumo-modified
-
senp1-mediated
- drug development
- ranbp2
- sumo-2
- diagnostics
Reaction
The enzyme catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO-1, SUMO-2 and SUMO-3 to their mature forms and deconjugation of SUMO-1, SUMO-2 and SUMO-3 from targeted proteins. Deconjugates SUMO-1 from homeodomain-interacting protein kinase 2. Deconjugates SUMO-1 from histone deacetylase 1, which decreases its transcriptional repression activity. Cleavage of Gly97-/-His98 bond in the SUMO-1 precursor with release of the propeptide His-Ser-Thr-Val. Cleavage of Gly93-/-Val94 bond in the SUMO-2 precursor with release of the propeptide Val94-Thyr. Cleavage of the Gly92-/-Val93 in the SUMO-3 precursor with release of the propeptide Pro-Glu-Ser-Ser-Leu-Ala-Gly-His-Ser-Phe. =
Synonyms
C13orf22l, SENP, SENP1, sentrin-specific protease 1, sentrin/SUMO-specific protease 1, small ubiquitin-like modifier protein-specific protease 1, small ubiquitin-related modifier-specific isopeptidase, SUMO isopeptidase, SUMO protease, SUMO protein-specific protease 1, SUMO-specific isopeptidase, SUMO-specific protease, SUMO-specific protease 1, ubiquitin-specific protease-like 1, USPL1
ECTree
3.4.22.B70 SENP1 peptidaseAdvanced search results
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results (Crystallization
Crystallization on EC 3.4.22.B70 - SENP1 peptidase
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
crystals of the human SENP1 catalytic domain are obtained at room temperature by hanging-drop vapour diffusion. When interpreting a medium-resolution electron-density map of the catalytic domain of human sentrin-specific protease 1 (SENP1), a strong feature indicative of an ordered divalent cation is noted. This is assigned as Co2+, an essential component of the crystallization mixture. The ion displays tetrahedral coordination by Glu430 and His640 from one molecule and the corresponding residues from a symmetry-related molecule. Analysis of the data derived from a previous structure of SENP1 suggest that Co2+ has been overlooked and rerefinement support this conclusion. Highthroughput automated re-refinement protocols also failed to mark the Co2+ position
SENP1 crystallization is performed at 20°C using a sitting drop vapour-diffusion method. Single diamond-shaped crystals are grown after 2 days from equal volumes of protein solution (20 mg/ml in 20 mM Tris/HCl, pH 8.0, and 50 mM NaCl) and reservoir solution containing 100 mM CoCl2, 0.1 M Mes, pH 6.5, and 1.8 M (NH4)2SO4. The structure of SENP1 is determined to 2.45 A. NaBH4 is used to trap a stable thiohemiacetal transition-state analogue between Cys602 of SENP1 and Gly92 of SUMO-2, determination of the structure of this complex to 3.2 A. Crystallization and structure determination of the SENP1-SUMO-2 complex
