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Literature summary for 2.7.1.107 extracted from

  • Jittikoon, J.; East, J.M.; Lee, A.G.
    A fluorescence method to define transmembrane alpha-helices in membrane proteins: studies with bacterial diacylglycerol kinase (2007), Biochemistry, 46, 10950-10959.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C46A/C113A mutant lacking all Cys residues. Activity is slightly higher than wild-type Escherichia coli
C46A/C113A/A29C introduction of Cys residue at transmembrane helix 1 into mutant lacking the native Cys residues. Low activity mutant, 64% trimer formation compared to wild-type Escherichia coli
C46A/C113A/A30C introduction of Cys residue at transmembrane helix 1 into mutant lacking the native Cys residues. Low activity mutant, 79% trimer formation compared to wild-type Escherichia coli
C46A/C113A/E28C introduction of Cys residue at transmembrane helix 1 into mutant lacking the native Cys residues. Low activity mutant, 93% trimer formation compared to wild-type Escherichia coli
C46A/C113A/Q33C introduction of Cys residue at transmembrane helix 1 into mutant lacking the native Cys residues. Low activity mutant, 77% trimer formation compared to wild-type Escherichia coli
C46A/C113A/R32C introduction of Cys residue at transmembrane helix 1 into mutant lacking the native Cys residues. Low activity mutant, 63% trimer formation compared to wild-type Escherichia coli
C46A/C113AE34C introduction of Cys residue at transmembrane helix 1 into mutant lacking the native Cys residues. Low activity mutant, 100% trimer formation compared to wild-type Escherichia coli
C46A/C113AF31C introduction of Cys residue at transmembrane helix 1 into mutant lacking the native Cys residues. Low activity mutant, 72% trimer formation compared to wild-type Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Km-value in mol% for wild-type 9.2, mutant C46A/C113A 4.9, mutant C46A/C113A/E28C 5.7, mutant C46A/C113A/A29C 7.4, mutant C46A/C113AA30C 27.2, mutant C46A/C113A/F31C 17.2, mutant C46A/C113A/R32C 12.9, mutant C46A/C113A/Q33C 12.1, mutant C46A/C113A/E34C 13.7 Escherichia coli
0.13
-
ATP mutant C46A/C113A, pH 6.9, 25°C Escherichia coli
0.34
-
ATP wild-type, pH 6.9, 25°C Escherichia coli
0.4
-
ATP mutant C46A/C113A/Q33C, pH 6.9, 25°C Escherichia coli
0.6
-
ATP mutant C46A/C113A/E34C, pH 6.9, 25°C Escherichia coli
1
-
ATP mutant C46A/C113A/A29C, pH 6.9, 25°C Escherichia coli
1.3
-
ATP mutant C46A/C113A/E28C, pH 6.9, 25°C Escherichia coli
2.1
-
ATP mutant C46A/C113A/F31C, pH 6.9, 25°C Escherichia coli
3.3
-
ATP mutant C46A/C113AA30C, pH 6.9, 25°C Escherichia coli
4.8
-
ATP mutant C46A/C113A/R32C, pH 6.9, 25°C Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane the region of transmembrane helix 1 spanning the hydrophobic core of the bilayer runs from Glu28 on the cytoplasmic side to Asp49 or Val50 on the periplasmic side. This locates the charged/polar cluster 32RQE34 within the hydrophobic core of the bilayer. Hydrophobic matching between the protein and the surrounding lipid bilayer is highly efficient Escherichia coli 16020
-

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 1,2-dihexanoylglycerol
-
Escherichia coli ADP + 1,2-dihexanoylglycerol 3-phosphate
-
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