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Literature summary for 3.4.21.105 extracted from

  • Arutyunova, E.; Panwar, P.; Skiba, P.M.; Gale, N.; Mak, M.W.; Lemieux, M.J.
    Allosteric regulation of rhomboid intramembrane proteolysis (2014), EMBO J., 33, 1869-1881.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Escherichia coli
expression in Escherichia coli Haemophilus influenzae

Protein Variants

Protein Variants Comment Organism
S150A inactive Escherichia coli
S150A inactive Providencia stuartii
S150A inactive Haemophilus influenzae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0018
-
FL-casein pH 6.0, 3°C Providencia stuartii
0.0025
-
FL-casein pH 6.0, 3°C Escherichia coli
0.0039
-
CyPet-TatA-YPet K0.5 value, Hill coefficient 1.8, pH 6.0, 3°C Providencia stuartii
0.0065
-
FL-casein pH 6.0, 3°C Haemophilus influenzae
0.0076
-
TatA K0.5 value, Hill coefficient 1.7, pH 6.0, 3°C Providencia stuartii
0.022
-
TatA K0.5 value, Hill coefficient 1.2, pH 6.0, 3°C Escherichia coli
0.119
-
TatA K0.5 value, Hill coefficient 1.2, pH 6.0, 3°C Haemophilus influenzae

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Haemophilus influenzae P44783
-
-
Haemophilus influenzae ATCC 51907 P44783
-
-
Providencia stuartii P46116
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CyPet-TatA-YPet + H2O engineered substrate based on transmembrane substrate TatA from Providencia stuartii, suitable for FRET assay Providencia stuartii ?
-
?
FL-casein + H2O
-
Escherichia coli ?
-
?
FL-casein + H2O
-
Providencia stuartii ?
-
?
FL-casein + H2O
-
Haemophilus influenzae ?
-
?
FL-casein + H2O
-
Haemophilus influenzae ATCC 51907 ?
-
?
additional information rhomboids may have two different mechanisms for substrate recognition. The transmembrane substrate is recognized on the hydrophobic belt of the enzyme by the exosite, which facilitates the substrate entry laterally into the active site. Soluble substrates, such as FL-casein, do not require initial exosite binding and approach the active site from the soluble face of the enzyme via the opening of loop 5 Escherichia coli ?
-
?
additional information rhomboids may have two different mechanisms for substrate recognition. The transmembrane substrate is recognized on the hydrophobic belt of the enzyme by the exosite, which facilitates the substrate entry laterally into the active site. Soluble substrates, such as FL-casein, do not require initial exosite binding and approach the active site from the soluble face of the enzyme via the opening of loop 5 Providencia stuartii ?
-
?
additional information rhomboids may have two different mechanisms for substrate recognition. The transmembrane substrate is recognized on the hydrophobic belt of the enzyme by the exosite, which facilitates the substrate entry laterally into the active site. Soluble substrates, such as FL-casein, do not require initial exosite binding and approach the active site from the soluble face of the enzyme via the opening of loop 5 Haemophilus influenzae ?
-
?
additional information rhomboids may have two different mechanisms for substrate recognition. The transmembrane substrate is recognized on the hydrophobic belt of the enzyme by the exosite, which facilitates the substrate entry laterally into the active site. Soluble substrates, such as FL-casein, do not require initial exosite binding and approach the active site from the soluble face of the enzyme via the opening of loop 5 Haemophilus influenzae ATCC 51907 ?
-
?
TatA + H2O transmembrane substrate from Providencia stuartii. Binding of TatA occurs with positive cooperativity in an exosite-mediated mode of substrate binding. Exosite formation is dependent on the oligomeric state of rhomboids, and when dimers are dissociated, allosteric substrate activation is not observed Escherichia coli ?
-
?
TatA + H2O transmembrane substrate from Providencia stuartii. Binding of TatA occurs with positive cooperativity in an exosite-mediated mode of substrate binding. Exosite formation is dependent on the oligomeric state of rhomboids, and when dimers are dissociated, allosteric substrate activation is not observed Providencia stuartii ?
-
?
TatA + H2O transmembrane substrate from Providencia stuartii. Binding of TatA occurs with positive cooperativity in an exosite-mediated mode of substrate binding. Exosite formation is dependent on the oligomeric state of rhomboids, and when dimers are dissociated, allosteric substrate activation is not observed Haemophilus influenzae ?
-
?
TatA + H2O transmembrane substrate from Providencia stuartii. Binding of TatA occurs with positive cooperativity in an exosite-mediated mode of substrate binding. Exosite formation is dependent on the oligomeric state of rhomboids, and when dimers are dissociated, allosteric substrate activation is not observed Haemophilus influenzae ATCC 51907 ?
-
?

Synonyms

Synonyms Comment Organism
AarA
-
Providencia stuartii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0017
-
TatA pH 6.0, 3°C Escherichia coli
0.0028
-
CyPet-TatA-YPet pH 6.0, 3°C Providencia stuartii
0.018
-
TatA pH 6.0, 3°C Providencia stuartii
0.06
-
FL-casein pH 6.0, 3°C Providencia stuartii
0.062
-
FL-casein pH 6.0, 3°C Escherichia coli
0.063
-
FL-casein pH 6.0, 3°C Haemophilus influenzae
0.07
-
TatA pH 6.0, 3°C Haemophilus influenzae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.7 6.5
-
Escherichia coli
5.7 6.5
-
Providencia stuartii
5.7 6.5
-
Haemophilus influenzae

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.08
-
TatA pH 6.0, 3°C Escherichia coli
0.59
-
TatA pH 6.0, 3°C Haemophilus influenzae
0.7
-
CyPet-TatA-YPet pH 6.0, 3°C Providencia stuartii
2.37
-
TatA pH 6.0, 3°C Providencia stuartii
2.48
-
FL-casein pH 6.0, 3°C Escherichia coli
9.7
-
FL-casein pH 6.0, 3°C Haemophilus influenzae
33
-
FL-casein pH 6.0, 3°C Providencia stuartii