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Literature summary for 2.5.1.145 extracted from

  • Sankaran, K.; Gan, K.; Rash, B.; Qi, H.Y.; Wu, H.C.; Rick, P.D.
    Roles of histidine-103 and tyrosine-235 in the function of the prolipoprotein diacylglyceryl transferase of Escherichia coli (1997), J. Bacteriol., 179, 2944-2948 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.5.1.145

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli SK634 cells Escherichia coli

Protein Variants

Protein Variants Comment Organism
H103N inactive Escherichia coli
H196N the mutations result in an increase of in vitro activity (110% of wild type activity) Escherichia coli
H196Q the mutation results in a significant reduction of in vitro activity (50% of wild type activity) Escherichia coli
H196R the mutation results in a significant reduction of in vitro activity (50% of wild type activity) Escherichia coli
H2103Q inactive Escherichia coli
H289Q the mutation results in a reduction of in vitro activity (90% of wild type activity) Escherichia coli
H7Q the mutant shows wild type activity Escherichia coli
H7Q/H24Q/H103Q/H289Q inactive Escherichia coli
H7Q/H24Q/H196Q/H289Q the mutations result in a reduction of in vitro activity (40% of wild type activity) Escherichia coli
H7Q/H24Q/H289Q the mutations result in a reduction of in vitro activity (90% of wild type activity) Escherichia coli
H7Q/H289Q H7Q/H24Q/H289Q the mutations result in an increase of in vitro activity (110% of wild type activity) Escherichia coli
Y190F the mutant shows 110% activity compared to the wild type enzyme Escherichia coli
Y201F the mutant shows wild type activity Escherichia coli
Y235F inactive Escherichia coli
Y235S the mutant shows 60% activity compared to the wild type enzyme Escherichia coli
Y235T inactive Escherichia coli
Y26F the mutant shows 120% activity compared to the wild type enzyme Escherichia coli
Y282F the mutant shows 90% activity compared to the wild type enzyme Escherichia coli
Y62F the mutant shows 120% activity compared to the wild type enzyme Escherichia coli
Y76F the mutant shows 110% activity compared to the wild type enzyme Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
diethylpyrocarbonate
-
 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.007
-
 L-1-phosphatidyl-sn-glycerol mutant enzyme H196Q, at pH 8.0 and 37°C Escherichia coli
0.01
-
 L-1-phosphatidyl-sn-glycerol wild type enzyme, at pH 8.0 and 37°C Escherichia coli
0.028
-
 MKATKLVLGAVILGSTLLAGCSSN mutant enzyme H196Q, at pH 8.0 and 37°C Escherichia coli
0.03
-
 MKATKLVLGAVILGSTLLAGCSSN wild type enzyme, at pH 8.0 and 37°C Escherichia coli
0.03
-
 L-1-phosphatidyl-sn-glycerol mutant enzyme Y235S, at pH 8.0 and 37°C Escherichia coli
0.067
-
 MKATKLVLGAVILGSTLLAGCSSN mutant enzyme Y235S, at pH 8.0 and 37°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-1-phosphatidyl-sn-glycerol + MKATKLVLGAVILGSTLLAGCSSN
-
 Escherichia coli sn-glycerol 1-phosphate + MKATKLVLGAVILGSTLLAG-S-1,2-diacyl-sn-glyceryl-L-cysteine -SSN
-
 ?

Synonyms

Synonyms Comment Organism
LGT
-
 Escherichia coli
phosphatidylglycerol:prolipoprotein diacylglyceryl transferase
-
 Escherichia coli
prolipoprotein diacylglyceryl transferase
-
 Escherichia coli