Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.5.1.145 - phosphatidylglycerol-prolipoprotein diacylglyceryl transferase and Organism(s) Escherichia coli and UniProt Accession P60955

for references in articles please use BRENDA:EC2.5.1.145
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
This bacterial enzyme, which is associated with the membrane, catalyses the transfer of an sn-1,2-diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the prospective N-terminal cysteine of a prolipoprotein, the first step in the formation of mature triacylated lipoproteins.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P60955
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
L-1-phosphatidyl-sn-glycerol
+
a [prolipoprotein]-L-cysteine
=
sn-glycerol 1-phosphate
+
an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
+
a [prolipoprotein]-L-cysteine
=
+
an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
Synonyms
prolipoprotein diacylglyceryl transferase, lipoprotein diacylglyceryl transferase, phosphatidylglycerol:prolipoprotein diacylglyceryl transferase, phosphatidylglycerol prolipoprotein diacylglyceryl transferase, phosphatidylglycerol-prolipoprotein diacylglyceryl transferase, prolipoprotein glyceryl transferase, phosphatidylglycerol::prolipoprotein diacylglyceryl transferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipoprotein diacylglyceryl transferase
-
phosphatidylglycerol::prolipoprotein diacylglyceryl transferase
-
phosphatidylglycerol:prolipoprotein diacylglyceryl transferase
-
phosphatidylglycerol:prolipoproteindiacylglyceryl transferase
-
prolipoprotein diacylglyceryl transferase
-
GT
-
-
-
-
phosphatidylglycerol-prolipoprotein diacylglyceryl transferase
-
-
phosphatidylglycerol: prolipoprotein diacylglyceryl transferase
-
-
phosphatidylglycerol:prolipoprotein diacylglyceryl transferase
-
-
prolipoprotein diacylglyceryl transferase
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-1-phosphatidyl-sn-glycerol:[prolipoprotein]-L-cysteine diacyl-sn-glyceryltransferase
This bacterial enzyme, which is associated with the membrane, catalyses the transfer of an sn-1,2-diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the prospective N-terminal cysteine of a prolipoprotein, the first step in the formation of mature triacylated lipoproteins.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dipalmitoyl phosphatidic acid + MKATKLVLGAVILGSTLLAGCSSN
?
show the reaction diagram
weak activity
-
-
?
dipalmitoyl phosphatidyl-L-serine + MKATKLVLGAVILGSTLLAGCSSN
?
show the reaction diagram
weak activity
-
-
?
dipalmitoyl-L-1-phosphatidyl-sn-glycerol + MKATKLVLGAVILGSTLLAGCSSN
dipalmitoyl-sn-glycerol 1-phosphate + MKATKLVLGAVILGSTLLAGC-S-1,2-diacyl-sn-glyceryl-L-cysteine-SSN
show the reaction diagram
-
-
-
?
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
show the reaction diagram
L-1-phosphatidyl-sn-glycerol + MKATKLVLGAVILGSTLLAGCSSN
sn-glycerol 1-phosphate + MKATKLVLGAVILGSTLLAGC-S-1,2-diacyl-sn-glyceryl-L-cysteine-SSN
show the reaction diagram
-
-
-
?
L-1-phosphatidyl-sn-glycerol + MKATKSAVGSTLAGCSSHHHHHH
sn-glycerol 1-phosphate + MKATKSAVGSTLAG-(S-1,2-diacyl-sn-glyceryl-L-cysteine)-SHHHHHH
show the reaction diagram
-
-
-
?
L-1-phosphatidyl-sn-glycerol + MKATKLVLGAVILGSTLLAGCSS
sn-glycerol 1-phosphate + MKATKLVLGAVILGSTLLAG-(S-1,2-diacyl-sn-glyceryl-L-cysteine) -SSN
show the reaction diagram
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + MKATKLVLGAVILGSTLLAGCSSN
sn-glycerol 1-phosphate + MKATKLVLGAVILGSTLLAG-S-1,2-diacyl-sn-glyceryl-L-cysteine -SSN
show the reaction diagram
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + [MKATKSAVGSTLAGCSSHHHHHH]-L-cysteine
sn-glycerol 1-phosphate + [MKATKSAVGSTLAGCSSHHHHHH]-S-1,2-diacyl-sn-glyceryl-L-cysteine
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
n-octyl-beta-D-glucoside
-
palmitic acid
-
diethylpyrocarbonate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007 - 0.03
L-1-phosphatidyl-sn-glycerol
0.028 - 0.067
MKATKLVLGAVILGSTLLAGCSSN
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is essential for the viability
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with phosphatidylglycerol and palmitic acid, hanging drop vapor diffusion method, using 0.1 M Tris (pH 6.5), 0.1 M CaCl2 and 13% (w/v) PEG2000 MME
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D129A
the mutation is not essential for enzyme activity
D88N
the mutation has no effect on enzyme activity
D97N
the mutation has no effect on enzyme activity
E151A
E151Q
inactive
E243A
the mutation is essential for enzyme activity
G104A
the mutation is not essential for enzyme activity
G138I
inactive
G138V
inactive
G142A
inactive
G142I
inactive
G142V
inactive
G145A
inactive
G145I
inactive
G145V
inactive
G98A
the mutation is not essential for enzyme activity
H103Q
the mutation is not essential for enzyme activity
R143A
R239A
the mutation is essential for enzyme activity
H103N
-
inactive
H196N
-
the mutations result in an increase of in vitro activity (110% of wild type activity)
H196Q
-
the mutation results in a significant reduction of in vitro activity (50% of wild type activity)
H196R
-
the mutation results in a significant reduction of in vitro activity (50% of wild type activity)
H2103Q
-
inactive
H289Q
-
the mutation results in a reduction of in vitro activity (90% of wild type activity)
H7Q
-
the mutant shows wild type activity
H7Q/H24Q/H103Q/H289Q
-
inactive
H7Q/H24Q/H196Q/H289Q
-
the mutations result in a reduction of in vitro activity (40% of wild type activity)
H7Q/H24Q/H289Q
-
the mutations result in a reduction of in vitro activity (90% of wild type activity)
H7Q/H289Q H7Q/H24Q/H289Q
-
the mutations result in an increase of in vitro activity (110% of wild type activity)
Y190F
-
the mutant shows 110% activity compared to the wild type enzyme
Y201F
-
the mutant shows wild type activity
Y235F
-
inactive
Y235S
-
the mutant shows 60% activity compared to the wild type enzyme
Y235T
-
inactive
Y26F
-
the mutant shows 120% activity compared to the wild type enzyme
Y282F
-
the mutant shows 90% activity compared to the wild type enzyme
Y62F
-
the mutant shows 120% activity compared to the wild type enzyme
Y76F
-
the mutant shows 110% activity compared to the wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiTrap nickel column chromatography and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli CE43 (DE3) cells
expressed in Salmonella typhimurium strain SE5221
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli SK634 cells
-
expressed in Escherichia coli strains SK634 and SK635
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sundaram, S.; Banerjee, S.; Sankaran, K.
The first nonradioactive fluorescence assay for phosphatidylglycerol prolipoprotein diacylglyceryl transferase that initiates bacterial lipoprotein biosynthesis
Anal. Biochem.
423
163-170
2012
Escherichia coli
Manually annotated by BRENDA team
Selvan, A.; Sankaran, K.
Localization and characterization of prolipoprotein diacylglyceryl transferase (Lgt) critical in bacterial lipoprotein biosynthesis
Biochimie
90
1647-1655
2008
Escherichia coli
Manually annotated by BRENDA team
Tamil Selvan, A.; Sankaran, K.
Bacterial lipid modification in vitro synthetic peptide substrate for phosphatidylglycerol-prolipoprotein diacylglyceryl transferase
Indian J. Biotechnol.
5
327-331
2006
Escherichia coli
-
Manually annotated by BRENDA team
Gan, K.; Sankaran, K.; Williams, M.G.; Aldea, M.; Rudd, K.E.; Kushner, S.R.; Wu, H.C.
The umpA gene of Escherichia coli encodes phosphatidylglycerol prolipoprotein diacylglyceryl transferase (lgt) and regulates thymidylate synthase levels through translational coupling
J. Bacteriol.
177
1879-1882
1995
Escherichia coli (P60955), Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team
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
J. Bacteriol.
179
2944-2948
1997
Escherichia coli
Manually annotated by BRENDA team
Pailler, J.; Aucher, W.; Pires, M.; Buddelmeijer, N.
Phosphatidylglycerol prolipoprotein diacylglyceryl transferase (Lgt) of Escherichia coli has seven transmembrane segments, and its essential residues are embedded in the membrane
J. Bacteriol.
194
2142-2151
2012
Escherichia coli (P60955), Escherichia coli
Manually annotated by BRENDA team
Sankaran, K.; Wu, H.C.
Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol
J. Biol. Chem.
269
19701-19706
1994
Escherichia coli
Manually annotated by BRENDA team
Mao, G.; Zhao, Y.; Kang, X.; Li, Z.; Zhang, Y.; Wang, X.; Sun, F.; Sankaran, K.; Zhang, X.C.
Crystal structure of E. coli lipoprotein diacylglyceryl transferase
Nat. Commun.
7
10198
2016
Escherichia coli (P60955), Escherichia coli
Manually annotated by BRENDA team
Sangith, N.; Kumar, S.; Sankaran, K.
Evidence to suggest bacterial lipoprotein diacylglyceryl transferase (Lgt) is a weakly associated inner membrane protein
J. Membr. Biol.
252
563-575
2019
Escherichia coli (P60955)
Manually annotated by BRENDA team
Singh, W.; Bilal, M.; McClory, J.; Dourado, D.; Quinn, D.; Moody, T.S.; Sutcliffe, I.; Huang, M.
Mechanism of phosphatidylglycerol activation catalyzed by prolipoprotein diacylglyceryl transferase
J. Phys. Chem. B
123
7092-7102
2019
Escherichia coli (P60955)
Manually annotated by BRENDA team