Literature summary for 3.4.21.105 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.

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Cloned(Commentary)

Cloned (Comment)	Organism
expressed as a C-terminal His-tagged fusion protein in Escherichia coli BL21	Pseudomonas aeruginosa

Inhibitors

Inhibitors	Comment	Organism
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
1,2-dimyristoyl-sn-glycero-3-phosphocholine	paGlpG purified in detergent causes 5% reduction in activity	Pseudomonas aeruginosa
1-myristoyl-sn-glycero-3-phosphocholine	paGlpG purified in detergent causes 10% reduction in activity	Pseudomonas aeruginosa
1-palmitoyl-sn-glycero-3-phospho-rac-(1-glycerol)	paGlpG purified in detergent causes 20% reduction in activity	Pseudomonas aeruginosa
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
dodecyl maltoside	paGlpG purified in detergent causes 77% reduction in activity	Pseudomonas aeruginosa
n-nonyl-beta-D-glucoside	paGlpG purified in detergent causes 45% reduction in activity	Pseudomonas aeruginosa

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
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

Purification (Comment)

Organism

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)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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

Synonyms	Comment	Organism
paGlpG	-	Pseudomonas aeruginosa
Rhomboid	-	Pseudomonas aeruginosa

General Information

General Information	Comment	Organism
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