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Literature summary for 3.4.22.68 extracted from

  • Alegre, K.; Reverter, D.
    Swapping small ubiquitin-like modifier (SUMO) isoform specificity of SUMO proteases SENP6 and SENP7 (2011), J. Biol. Chem., 286, 36142-36151.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.68

Cloned(Commentary)

Cloned (Comment) Organism
expression of catalytic domains of human SENP2-(364-589), SENP6-(637-1112), and SENP7-(662-984) and of mutant SENP-7s in Escherichia coli Homo sapiens

Protein Variants

Protein Variants Comment Organism
K691A site-directed mutagenesis of SENP7 Homo sapiens
K691E site-directed mutagenesis of SENP7 Homo sapiens
P686G/P687G/P688G/P689G site-directed mutagenesis of SENP7 Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten steady-state kinetics are performed for SENP6 by introduction of S9C and C52A point mutants into SUMO1 and SUMO1 mutant A68N/H71D to allow for fluorophore addition Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
nucleoplasm SENP6 and SENP7 Homo sapiens 5654
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
small ubiquitin-related modifier-protein + H2O Homo sapiens SUMO-specific proteases, SENPs, reversibly remove small ubiquitin-related modifier-protein, SUMO, from the SUMOylated proteins small ubiquitin-related modifier-protein + protein
-
 r

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant catalytic domains of human SENP2-(364-589), SENP6-(637-1112), and SENP7-(662-984) and of mutant SENP-7s from Escherichia coli by metal affinity chromatography and gel filtration Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information substrate specificities of different SENPS with different SUMOs, wild-types and mutants, very detailed overview. the SENP6 and SENP7 subclass displays a clear proteolytic cleavage preference for SUMO2/3 isoformsm structural determinants, overview. Identification of a unique sequence insertion in the SENP6 and SENP7 subclass that is essential for their proteolytic activity and that forms a more extensive interface with SUMO during the proteolytic reaction. Structure-based comparisons combined with biochemical and mutagenesis analysis reveal Loop 1 insertion in SENP6 and SENP7 as a platform to discriminate between SUMO1 and SUMO2/3 isoforms in this subclass of the SUMO protease family. Loop 1 SENP7 interacts with SUMO2. Deconjugation of diSUMO2(D71K) with SENP7 loop 1 mutant constructs, although proteolytic cleavage of diSUMO2(D71K) substrate shows a decrease in the proteolytic activity for all SENP7 constructs tested, including the wild type form. Mutation D71K, on the surface of SUMO2 distant from the cleavage site, can produce marked defects in the proteolytic activity of SENP7, with an approximately loss of 20fold with respect to the diSUMO2 wild type reaction Homo sapiens ?
-
 ?
small ubiquitin-related modifier-protein + H2O SUMO-specific proteases, SENPs, reversibly remove small ubiquitin-related modifier-protein, SUMO, from the SUMOylated proteins Homo sapiens small ubiquitin-related modifier-protein + protein
-
 r

Synonyms

Synonyms Comment Organism
SENP6
-
 Homo sapiens
SENP7
-
 Homo sapiens
SUMO protease
-
 Homo sapiens

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Homo sapiens

General Information

General Information Comment Organism
evolution in humans, the SENP/ULP protease family is comprised of seven members, six are SUMO-specific proteases, SENP1, SENP2, SENP3, SENP5, SENP6, and SENP7, whereas one is specific for another ubiquitin-like protein, Nedd8, or SENP8, also named DEN1 or NEDP1. SENP6 and SENP7 are the most divergent members in their conserved catalytic domain Homo sapiens
physiological function SUMO proteases can regulate the amounts of SUMO-conjugated proteins in the cell by cleaving off the isopeptidic bond between SUMO and the target protein Homo sapiens