Literature summary extracted from
Sherratt, A.R.; Braganza, M.V.; Nguyen, E.; Ducat, T.; Goto, N.K.
Insights into the effect of detergents on the full-length rhomboid protease from Pseudomonas aeruginosa and its cytosolic domain (2009), Biochim. Biophys. Acta, 1788, 2444-2453.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
3.4.21.105 |
expressed as a C-terminal His-tagged fusion protein in Escherichia coli BL21 |
Pseudomonas aeruginosa |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
3.4.21.105 |
1,2-dihexanoyl-sn-glycero-3-phosphocholine |
1,2-dimyristoyl-sn-glycero-3-phosphocholine additionally added, paGlpG purified in detergent causes 37% reduction in activity |
Pseudomonas aeruginosa |
|
3.4.21.105 |
1,2-dimyristoyl-sn-glycero-3-phosphocholine |
paGlpG purified in detergent causes 5% reduction in activity |
Pseudomonas aeruginosa |
|
3.4.21.105 |
1-myristoyl-sn-glycero-3-phosphocholine |
paGlpG purified in detergent causes 10% reduction in activity |
Pseudomonas aeruginosa |
|
3.4.21.105 |
1-palmitoyl-sn-glycero-3-phospho-rac-(1-glycerol) |
paGlpG purified in detergent causes 20% reduction in activity |
Pseudomonas aeruginosa |
|
3.4.21.105 |
3-[(3-cholamidopropyl)-dimethylammonio]-1-propansulfonate |
1,2-dimyristoyl-sn-glycero-3-phosphocholine additionally added, paGlpG purified in detergent causes 37% reduction in activity |
Pseudomonas aeruginosa |
|
3.4.21.105 |
dodecyl maltoside |
paGlpG purified in detergent causes 77% reduction in activity |
Pseudomonas aeruginosa |
|
3.4.21.105 |
n-nonyl-beta-D-glucoside |
paGlpG purified in detergent causes 45% reduction in activity |
Pseudomonas aeruginosa |
|
Localization
EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
---|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.4.21.105 |
Pseudomonas aeruginosa |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
3.4.21.105 |
rhomboid from Pseudomonas aeruginosa is purified in a range of membrane-mimetic media, its functional status in vitro and the NMR spectroscopic properties of these samples are investigated. NMR signals can only be observed from the cytosolic domain, and only in detergents that do not support rhomboid activity. In contrast, media that support rhomboid function do not show these resonances, suggesting an association between the cytosolic domain and the protein-detergent complex |
Pseudomonas aeruginosa |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
3.4.21.105 |
beta-lactamase-Spitz transmembrane segment-maltose binding protein + H2O |
a fusion protein containing the Spitz TM segment fused to globular proteins at the N- and C-termini (beta-lactamase and maltose binding protein, respectively) |
Pseudomonas aeruginosa |
? |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.4.21.105 |
paGlpG |
- |
Pseudomonas aeruginosa |
3.4.21.105 |
Rhomboid |
- |
Pseudomonas aeruginosa |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
3.4.21.105 |
physiological function |
the cytosolic domain does not interact with the lipid membrane, but instead enhances rhomboid activity through interactions with some other part of the rhomboid, such as the catalytic core domain |
Pseudomonas aeruginosa |