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Information on EC 2.5.1.145 - phosphatidylglycerol-prolipoprotein diacylglyceryl transferase
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2.5.1.145 phosphatidylglycerol-prolipoprotein diacylglyceryl transferaseIUBMB 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.
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Word Map
- 2.5.1.145
- prolipoproteins
- peptidase
- streptococcus
-
lipobox
-
n-acylation
-
tlr2-dependent
-
lipoprotein-specific
-
braun
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
=
+
+
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GT
-
-
-
-
LGT
lipoprotein diacylglyceryl transferase
phosphatidylglycerol: prolipoproteindiacylglyceryl transferase
phosphatidylglycerol::prolipoprotein diacylglyceryl transferase
phosphatidylglycerol:prolipoprotein diacylglyceryl transferase
prolipoprotein diacylglyceryl transferase
prolipoprotein glyceryl transferase
-
-
phosphatidylglycerol::prolipoprotein diacylglyceryl transferase
-
-
phosphatidylglycerol::prolipoprotein diacylglyceryl transferase
-
-
-
phosphatidylglycerol:prolipoprotein diacylglyceryl transferase
-
-
phosphatidylglycerol:prolipoprotein diacylglyceryl transferase
-
phosphatidylglycerol:prolipoprotein diacylglyceryl transferase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine = sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dipalmitoyl phosphatidic acid + MKATKLVLGAVILGSTLLAGCSSN
?
weak activity
-
-
?
dipalmitoyl phosphatidyl-L-serine + MKATKLVLGAVILGSTLLAGCSSN
?
weak activity
-
-
?
dipalmitoyl-L-1-phosphatidyl-sn-glycerol + MKATKLVLGAVILGSTLLAGCSSN
dipalmitoyl-sn-glycerol 1-phosphate + MKATKLVLGAVILGSTLLAGC-S-1,2-diacyl-sn-glyceryl-L-cysteine-SSN
-
-
-
?
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
L-1-phosphatidyl-sn-glycerol + MKATKLVLGAVILGSTLLAGCSS
sn-glycerol 1-phosphate + MKATKLVLGAVILGSTLLAG-(S-1,2-diacyl-sn-glyceryl-L-cysteine) -SSN
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + MKATKLVLGAVILGSTLLAGCSSN
sn-glycerol 1-phosphate + MKATKLVLGAVILGSTLLAG-S-1,2-diacyl-sn-glyceryl-L-cysteine -SSN
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + MKATKLVLGAVILGSTLLAGCSSN
sn-glycerol 1-phosphate + MKATKLVLGAVILGSTLLAGC-S-1,2-diacyl-sn-glyceryl-L-cysteine-SSN
-
-
-
?
L-1-phosphatidyl-sn-glycerol + MKATKSAVGSTLAGCSSHHHHHH
sn-glycerol 1-phosphate + MKATKSAVGSTLAG-(S-1,2-diacyl-sn-glyceryl-L-cysteine)-SHHHHHH
-
-
-
?
L-1-phosphatidyl-sn-glycerol + MKATKSAVGSTLAGCSSHHHHHH
sn-glycerol 1-phosphate + MKATKSAVGSTLAG-S-1,2-diacyl-sn-glyceryl-L-cysteine-SSHHHHHH
L-1-phosphatidyl-sn-glycerol + [MKATKSAVGSTLAGCSSHHHHHH]-L-cysteine
sn-glycerol 1-phosphate + [MKATKSAVGSTLAGCSSHHHHHH]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + [prolipoprotein MsmE]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein MsmE]-S-1,2-diacyl-sn-glyceryl-L-cysteine
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
?
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
?
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + MKATKSAVGSTLAGCSSHHHHHH
sn-glycerol 1-phosphate + MKATKSAVGSTLAG-S-1,2-diacyl-sn-glyceryl-L-cysteine-SSHHHHHH
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + MKATKSAVGSTLAGCSSHHHHHH
sn-glycerol 1-phosphate + MKATKSAVGSTLAG-S-1,2-diacyl-sn-glyceryl-L-cysteine-SSHHHHHH
Lactococcus lactis ATCC 11454
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + [prolipoprotein MsmE]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein MsmE]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
?
L-1-phosphatidyl-sn-glycerol + [prolipoprotein MsmE]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein MsmE]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
?
additional information
?
-
neutral phospholipid, dipalmitoyl phosphatidyl-ethanolamine, dipalmitoyl phosphatidyl-choline and diacylglycerol are no substrates
-
-
?
additional information
?
-
-
neutral phospholipid, dipalmitoyl phosphatidyl-ethanolamine, dipalmitoyl phosphatidyl-choline and diacylglycerol are no substrates
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
?
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
?
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
-
?
L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine
sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
-
-
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Mastitis
In the absence of Lgt, lipoproteins are shed from Streptococcus uberis independently of Lsp.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.007
L-1-phosphatidyl-sn-glycerol
-
mutant enzyme H196Q, at pH 8.0 and 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
an integral inner membrane protein, the enzyme's signature motif faces the periplasm
brenda
-
peripheral membrane protein on the cytoplasmic side of the inner-membrane
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
inactivation of the enzyme enhances growth in a high concentration of Mn2+ or under oxidative stress in vitro, and significantly decreases virulence of Enterococcus faecalis
malfunction
-
the enzyme deletion mutant has reduced growth in cation depleted medium, increased sensitivity to oxidative stress, reduced zinc uptake, and reduced intracellular levels of several cations. The deletion mutant has significantly reduced growth in blood or bronchoalveolar lavage fluid and a marked impairment in virulence in mouse models of nasopharyngeal colonisation, sepsis and pneumonia
malfunction
-
inactivation of the enzyme enhances growth in a high concentration of Mn2+ or under oxidative stress in vitro, and significantly decreases virulence of Enterococcus faecalis
-
metabolism
-
the enzyme is necessary for the acylation and membrane anchoring of two model lipoproteins expressed in Corynebacterium glutamicum: MusE, a C. glutamicum maltose-binding lipoprotein, and LppX, a Mycobacterium tuberculosis lipoprotein. However, the enzyme is not required for these proteins' signal peptide cleavage, or for LppX glycosylation. The enzyme is not necessary for growth on maltose
metabolism
-
the enzyme is necessary for the acylation and membrane anchoring of two model lipoproteins expressed in Corynebacterium glutamicum: MusE, a C. glutamicum maltose-binding lipoprotein, and LppX, a Mycobacterium tuberculosis lipoprotein. However, the enzyme is not required for these proteins' signal peptide cleavage, or for LppX glycosylation. The enzyme is not necessary for growth on maltose
-
physiological function
-
the enzyme is essential for the growth and viability
physiological function
-
the enzyme is essential for the viability
physiological function
-
the enzyme is required for efficient spore germination and full virulence of Bacillus anthracis
physiological function
-
the enzyme plays an important role in the susceptibility of Vibrio cholerae phage VP3 infection
physiological function
-
the enzyme is required for efficient spore germination and full virulence of Bacillus anthracis
-
Show AA Sequence and Transmembrane Helices (39222 entries)
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E151A
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)
H289Q
-
the mutation results in a reduction of in vitro activity (90% of wild type activity)
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)
R143A
Y26F
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli strains SK634, SK635, and SK636
-
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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
brenda
Selvan, A.; Sankaran, K.
Localization and characterization of prolipoprotein diacylglyceryl transferase (Lgt) critical in bacterial lipoprotein biosynthesis
Biochimie
90
1647-1655
2008
Escherichia coli
brenda
Wang, D.; Guo, X.; Diao, B.; Liang, W.; Qiu, H.; Gao, S.; Kan, B.
Prolipoprotein diacylglyceryl transferase (Igt) is a gene associated with receptor of V. cholerae phage VP3
Chin. J. Microbiol. Immunol.
24
564-567
2004
Vibrio phage VP3
-
brenda
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
-
brenda
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
Salmonella enterica subsp. enterica serovar Typhimurium, Escherichia coli (P60955), Escherichia coli
brenda
Qi, H.; Sankaran, K.; Gan, K.; Wu, H.
Structure-function relationship of bacterial prolipoprotein diacylglyceryl transferase Functionally significant conserved regions
J. Bacteriol.
177
6820-6824
1995
Staphylococcus aureus
brenda
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
brenda
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
brenda
Gan, K.; Gupta, S.; Sankaran, K.; Schmid, M.; Wu, H.
Isolation and characterization of a temperature-sensitive mutant of Salmonella typhimurium defective in prolipoprotein modification
J. Biol. Chem.
268
16544-16550
1993
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
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
brenda
Reffuveille, F.; Serror, P.; Chevalier, S.; Budin-Verneuil, A.; Ladjouzi, R.; Bernay, B.; Auffray, Y.; Rince, A.
The prolipoprotein diacylglyceryl transferase (Lgt) of Enterococcus faecalis contributes to virulence
Microbiology
158
816-825
2012
Enterococcus faecalis, Enterococcus faecalis V19
brenda
Okugawa, S.; Moayeri, M.; Pomerantsev, A.; Sastalla, I.; Crown, D.; Gupta, P.; Leppla, S.
Lipoprotein biosynthesis by prolipoprotein diacylglyceryl transferase is required for efficient spore germination and full virulence of Bacillus anthracis
Mol. Microbiol.
83
96-109
2012
Bacillus anthracis, Bacillus anthracis Ames 35
brenda
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
brenda
Arimoto, T.; Igarashi, T.
Role of prolipoprotein diacylglyceryl transferase (Lgt) and lipoprotein-specific signal peptidase II (LspA) in localization and physiological function of lipoprotein MsmE in Streptococcus mutans
Oral Microbiol. Immunol.
23
515-519
2008
Streptococcus mutans serotype c (P72482), Streptococcus mutans serotype c ATCC 700610 (P72482)
brenda
Chimalapati, S.; Cohen, J.; Camberlein, E.; MacDonald, N.; Durmort, C.; Vernet, T.; Hermans, P.; Mitchell, T.; Brown, J.
Effects of deletion of the Streptococcus pneumoniae lipoprotein diacylglyceryl transferase gene lgt on ABC transporter function and on growth in vivo
PLoS ONE
7
e41393
2012
Streptococcus pneumoniae
brenda
Banerjee, S.; Sankaran, K.
First ever isolation of bacterial prolipoprotein diacylglyceryl transferase in single step from Lactococcus lactis
Protein Expr. Purif.
87
120-128
2013
Lactococcus lactis, Lactococcus lactis ATCC 11454
brenda
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)
brenda
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)
brenda
Dautin, N.; Argentini, M.; Mohiman, N.; Labarre, C.; Cornu, D.; Sago, L.; Chami, M.; Dietrich, C.; de Sousa d'Auria, C.; Houssin, C.; Masi, M.; Salmeron, C.; Bayan, N.
Role of the unique, non-essential phosphatidylglycerol prolipoprotein diacylglyceryl transferase (Lgt) in Corynebacterium glutamicum
Microbiology
166
759-776
2020
Corynebacterium glutamicum, Corynebacterium glutamicum RES167
brenda
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