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Literature summary for 3.4.21.105 extracted from

  • Lazareno-Saez, C.; Arutyunova, E.; Coquelle, N.; Lemieux, M.J.
    Domain swapping in the cytoplasmic domain of the Escherichia coli rhomboid protease (2013), J. Mol. Biol., 425, 1127-1142.
    View publication on PubMed
Search for more literature for 3.4.21.105

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of the soluble cytoplasmic domain, 1.35 Å resolution. The cytoplasmic domain exists as a dimer with extensive domain swapping between the two monomers. Domain-swapped dimers can be isolated from the full-length protein Escherichia coli

Protein Variants

Protein Variants Comment Organism
D18A mutation in residue conserved among 32 sequenced prokaryotic rhomboids. No significant change in activity is observed Escherichia coli
E42A mutation in residue conserved among 32 sequenced prokaryotic rhomboids. No significant change in activity is observed Escherichia coli
M3A mutation in residue conserved among 32 sequenced prokaryotic rhomboids. No significant change in activity is observed Escherichia coli
additional information expression of the isolated membrane domain. Catalytic parameters for the domain are not significantly different in comparison to the full-length protein. Similar to wild-type, membrane domain formsdimers Escherichia coli
N33P mutation promotes domain-swapped dimer formation, due to probably a lower entropic barrier of protein–protein association Escherichia coli
Q14A mutation in residue conserved among 32 sequenced prokaryotic rhomboids. No significant change in activity is observed Escherichia coli
Q30A mutation in residue conserved among 32 sequenced prokaryotic rhomboids. No significant change in activity is observed Escherichia coli
R11A mutation in residue conserved among 32 sequenced prokaryotic rhomboids. No significant change in activity is observed Escherichia coli
R49A mutation in residue conserved among 32 sequenced prokaryotic rhomboids. No significant change in activity is observed Escherichia coli
S68A mutation in residue conserved among 32 sequenced prokaryotic rhomboids. No significant change in activity is observed Escherichia coli
T22A mutation in residue conserved among 32 sequenced prokaryotic rhomboids. No significant change in activity is observed Escherichia coli
W38A mutation in residue conserved among 32 sequenced prokaryotic rhomboids. No significant change in activity is observed Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00074
-
 BODIPY FL casein mutant S68A, pH 8.0, 37°C Escherichia coli
0.00087
-
 BODIPY FL casein wild-type, pH 8.0, 37°C Escherichia coli
0.00093
-
 BODIPY FL casein mutant R11A, pH 8.0, 37°C Escherichia coli
0.00095
-
 BODIPY FL casein mutant D18A, pH 8.0, 37°C Escherichia coli
0.00104
-
 BODIPY FL casein mutant Q30A, pH 8.0, 37°C Escherichia coli
0.00104
-
 BODIPY FL casein mutant R49A, pH 8.0, 37°C Escherichia coli
0.0012
-
 BODIPY FL casein mutant M3A, pH 8.0, 37°C Escherichia coli
0.00126
-
 BODIPY FL casein mutant Q14A, pH 8.0, 37°C Escherichia coli
0.00126
-
 BODIPY FL casein mutant T22A, pH 8.0, 37°C Escherichia coli
0.00127
-
 BODIPY FL casein mutant E42A, pH 8.0, 37°C Escherichia coli
0.00168
-
 BODIPY FL casein mutant W38A, pH 8.0, 37°C Escherichia coli
0.0029
-
 BODIPY FL casein isolated membrane domain, pH 8.0, 37°C Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Escherichia coli P09391
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
BODIPY FL casein + H2O commercially available fluorescent substrate Escherichia coli ?
-
 ?
additional information removal of the cytoplasmic domain does not alter the catalytic parameters for detergent-solubilized rhomboid for both substrates BODIPY FL casein and protein TatA Escherichia coli ?
-
 ?
TatA + H2O
-
 Escherichia coli ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.003
-
 BODIPY FL casein mutant R49A, pH 8.0, 37°C Escherichia coli
0.0038
-
 BODIPY FL casein mutant Q30A, pH 8.0, 37°C Escherichia coli
0.0042
-
 BODIPY FL casein mutant M3A, pH 8.0, 37°C Escherichia coli
0.0042
-
 BODIPY FL casein mutant R11A, pH 8.0, 37°C Escherichia coli
0.0051
-
 BODIPY FL casein wild-type, pH 8.0, 37°C Escherichia coli
0.0053
-
 BODIPY FL casein mutant Q14A, pH 8.0, 37°C Escherichia coli
0.0058
-
 BODIPY FL casein mutant S68A, pH 8.0, 37°C Escherichia coli
0.0059
-
 BODIPY FL casein mutant T22A, pH 8.0, 37°C Escherichia coli
0.0069
-
 BODIPY FL casein mutant W38A, pH 8.0, 37°C Escherichia coli
0.007
-
 BODIPY FL casein isolated membrane domain, pH 8.0, 37°C Escherichia coli
0.0073
-
 BODIPY FL casein mutant D18A, pH 8.0, 37°C Escherichia coli
0.0073
-
 BODIPY FL casein mutant E42A, pH 8.0, 37°C Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.4
-
 BODIPY FL casein isolated membrane domain, pH 8.0, 37°C Escherichia coli
3.5
-
 BODIPY FL casein mutant M3A, pH 8.0, 37°C Escherichia coli
3.67
-
 BODIPY FL casein mutant Q30A, pH 8.0, 37°C Escherichia coli
3.67
-
 BODIPY FL casein mutant R49A, pH 8.0, 37°C Escherichia coli
4.12
-
 BODIPY FL casein mutant W38A, pH 8.0, 37°C Escherichia coli
4.17
-
 BODIPY FL casein mutant Q14A, pH 8.0, 37°C Escherichia coli
4.46
-
 BODIPY FL casein mutant R11A, pH 8.0, 37°C Escherichia coli
4.63
-
 BODIPY FL casein mutant T22A, pH 8.0, 37°C Escherichia coli
5.7
-
 BODIPY FL casein mutant E42A, pH 8.0, 37°C Escherichia coli
5.73
-
 BODIPY FL casein wild-type, pH 8.0, 37°C Escherichia coli
7.68
-
 BODIPY FL casein mutant D18A, pH 8.0, 37°C Escherichia coli
7.78
-
 BODIPY FL casein mutant S68A, pH 8.0, 37°C Escherichia coli