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a dodecanoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-dodecanoyloxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
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a tetradecanoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-dodecanoyloxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
a tetradecanoyl-[acyl-carrier protein] + dodecanoyl-Kdo2-lipid IVA
dodecanoyl-(tetradecanoyl)-Kdo2-lipid IVA + an [acyl-carrier protein]
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dodecanoyl-[acyl-carrier protein] + dodecanoyl-Kdo2-lipid IVA
dodecanoyl-(dodecanoyl)-Kdo2-lipid IVA + an [acyl-carrier protein]
the enzyme possesses acyltransferase and acylprotein thioesterase activities. The enzyme displays a strong preference for dodecanoyl-[acyl-carrier protein] over the other acyl chain lengths tested
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hexadecanoyl-[acyl-carrier protein] + dodecanoyl-Kdo2-lipid IVA
dodecanoyl-(hexadecanoyl)-Kdo2-lipid IVA + an [acyl-carrier protein]
the enzyme possesses acyltransferase and acylprotein thioesterase activities. The enzyme displays a strong preference for dodecanoyl-[acyl-carrier protein] over the other acyl chain lengths tested
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octanoyl-[acyl-carrier protein] + dodecanoyl-Kdo2-lipid IVA
dodecanoyl-(octanoyl)-Kdo2-lipid IVA + an [acyl-carrier protein]
the enzyme possesses acyltransferase and acylprotein thioesterase activities. The enzyme displays a strong preference for dodecanoyl-[acyl-carrier protein] over the other acyl chain lengths tested
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tetradecanoyl-[acyl-carrier protein] + dodecanoyl-Kdo2-lipid IVA
dodecanoyl-(tetradecanoyl)-Kdo2-lipid IVA + an [acyl-carrier protein]
the enzyme possesses acyltransferase and acylprotein thioesterase activities. The enzyme displays a strong preference for dodecanoyl-[acyl-carrier protein] over the other acyl chain lengths tested
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additional information
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a tetradecanoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-dodecanoyloxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
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LpxM transfers a C14:0 secondary acyl chain to the 3'-position of lipid A
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a tetradecanoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-dodecanoyloxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
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LpxM transfers a C14:0 secondary acyl chain to the 3'-position of lipid A
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a tetradecanoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-dodecanoyloxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
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a tetradecanoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-dodecanoyloxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
decanoyl, palmitoyl, palmitoleoyl, and (R)-3-hydroxymyristoyl-[acyl-carrier protein] are poor acyl donors. The enzyme acylates (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-dodecanoyloxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose about 100times faster than (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
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a tetradecanoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-dodecanoyloxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
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additional information
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the enzyme transfers a myristoyl chain to the (3R)-hydroxytetradecanoyl chain at the 3-O of the 2'-glucosaminyl moiety of Kdo2-lipid IV A
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additional information
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the enzyme transfers a myristoyl chain to the (3R)-hydroxytetradecanoyl chain at the 3-O of the 2'-glucosaminyl moiety of Kdo2-lipid IV A
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additional information
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enzyme LpxJ catalyzes the addition of a C12:0 or C14:0 acyl chain to the 3'-linked primary acyl chain of lipid IVA. LpxJ can act before the 2' secondary acyltransferase, LpxL, as well as the 3-deoxy-D-manno-octulosonic acid transferase, KdtA. LpxJ can only utilize acyl-ACPs rather than acyl coenzyme A, preferring C12:0-ACP and C14:0-ACP. No substrate: hexa-acylated substrate Kdo2-lipid A
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additional information
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enzyme LpxJ catalyzes the addition of a C12:0 or C14:0 acyl chain to the 3'-linked primary acyl chain of lipid IVA. LpxJ can act before the 2' secondary acyltransferase, LpxL, as well as the 3-deoxy-D-manno-octulosonic acid transferase, KdtA. LpxJ can only utilize acyl-ACPs rather than acyl coenzyme A, preferring C12:0-ACP and C14:0-ACP. No substrate: hexa-acylated substrate Kdo2-lipid A
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additional information
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lipid A in lipopolysaccharide of Escherichia coli mutant strains is modified by the introduction of myristoyltransferase gene cloned from Klebsiella pneumoniae. When the lpxL2 gene is introduced into the mutant having lipid A containing only 3-hydroxymyristic acids, it produces lipid A with two additional myristic acids (C14:0). When the same gene is introduced into the mutant with pentaacylated lipid A containing one lauric acid (C12:0), C12:0 is replaced by C14:0
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additional information
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lipid A in lipopolysaccharide of Escherichia coli mutant strains is modified by the introduction of myristoyltransferase gene cloned from Klebsiella pneumoniae. When the lpxL2 gene is introduced into the mutant having lipid A containing only 3-hydroxymyristic acids, it produces lipid A with two additional myristic acids (C14:0). When the same gene is introduced into the mutant with pentaacylated lipid A containing one lauric acid (C12:0), C12:0 is replaced by C14:0
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metabolism
the enzyme is necessary for the biosynthesis of lipid A, which comprises the outer leaflet of the outer membrane in Gram-negative bacteria. The enzyme has important effects on virulence in many human and animal pathogen
malfunction
LpxL depletion caused reduced cell growth and defects in cell morphology
malfunction
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LpxL depletion caused reduced cell growth and defects in cell morphology
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physiological function
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a strain E058 lpxM mutant lacks one myristoyl (C14:0) on its lipid A molecules. No differences are observed between the mutant and wild-type in growth rate in different broths and ability to survive in specific-pathogen-free chicken serum. The mutant strain shows significantly reduced invasion and intracellular survival in the avian macrophage HD11 cell line. HD11 cells treated with E058 lpxM-mutant derived lipopolysaccharide also show reduction of nitric oxide production and downregulation of cytokine gene expression. Compared to the parental strain, the mutant leads to a significant reduction in bacterial load in heart, liver, spleen, lung, and kidney tissues. The histopathological lesions in visceral organs of birds challenged with the wild-type strain are more severe than in birds infected with the mutant. The mutant shows a sensitivity pattern similar to the parental strain following exposure to several hydrophobic reagents
physiological function
expression of LpxJ complements the defects of an Escherichia coli LpxM mutant
physiological function
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lipid A structures of lpxM and lpxP mutants lack the secondary lauroyl 12:0 group (R3'') or palmitoleoyl 16:1 group (R2''), respectively, and thus both represent a pentaacyl lipid A. Lipid A of Yersinia pestis lpxM/lpxP double mutant lacks both secondary acyl groups, 12:0 and 16:1, and is thus represented by the tetraacyl form. The absence of at least one acyl group is crucial for binding of lipopolysaccharide to toll-like receptor TLR4. Lipopolysaccharide from lpxM and and lpxP mutants induces TNF production at approximately the same level, the former being a slightly stronger activator than the latter
physiological function
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a strain E058 lpxM mutant lacks one myristoyl (C14:0) on its lipid A molecules. No differences are observed between the mutant and wild-type in growth rate in different broths and ability to survive in specific-pathogen-free chicken serum. The mutant strain shows significantly reduced invasion and intracellular survival in the avian macrophage HD11 cell line. HD11 cells treated with E058 lpxM-mutant derived lipopolysaccharide also show reduction of nitric oxide production and downregulation of cytokine gene expression. Compared to the parental strain, the mutant leads to a significant reduction in bacterial load in heart, liver, spleen, lung, and kidney tissues. The histopathological lesions in visceral organs of birds challenged with the wild-type strain are more severe than in birds infected with the mutant. The mutant shows a sensitivity pattern similar to the parental strain following exposure to several hydrophobic reagents
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physiological function
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lipid A structures of lpxM and lpxP mutants lack the secondary lauroyl 12:0 group (R3'') or palmitoleoyl 16:1 group (R2''), respectively, and thus both represent a pentaacyl lipid A. Lipid A of Yersinia pestis lpxM/lpxP double mutant lacks both secondary acyl groups, 12:0 and 16:1, and is thus represented by the tetraacyl form. The absence of at least one acyl group is crucial for binding of lipopolysaccharide to toll-like receptor TLR4. Lipopolysaccharide from lpxM and and lpxP mutants induces TNF production at approximately the same level, the former being a slightly stronger activator than the latter
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Clementz, T.; Zhou, Z.; Raetz, C.R.
Function of the Escherichia coli msbB gene, a multicopy suppressor of htrB knockouts, in the acylation of lipid A. Acylation by MsbB follows laurate incorporation by HtrB
J. Biol. Chem.
272
10353-10360
1997
Escherichia coli (P24205)
brenda
Cai, L.; Li, Y.; Tao, G.; Guo, W.; Zhang, C.; Wang, X.
Identification of three genes encoding for the late acyltransferases of lipid A in Cronobacter sakazakii
Mar. Drugs
11
377-386
2013
Cronobacter sakazakii (A7MEA8), Cronobacter sakazakii, Cronobacter sakazakii ATCC BAA-894 (A7MEA8)
brenda
Korneev, K.V.; Kondakova, A.N.; Arbatsky, N.P.; Novototskaya-Vlasova, K.A.; Rivkina, E.M.; Anisimov, A.P.; Kruglov, A.A.; Kuprash, D.V.; Nedospasov, S.A.; Knirel, Y.A.; Drutskaya, M.S.
Distinct biological activity of lipopolysaccharides with different lipid A acylation status from mutant strains of Yersinia pestis and some members of genus Psychrobacter
Biochemistry (Moscow)
79
1333-1338
2014
Yersinia pestis, Yersinia pestis KM260
brenda
Rubin, E.J.; OBrien, J.P.; Ivanov, P.L.; Brodbelt, J.S.; Trent, M.S.
Identification of a broad family of lipid A late acyltransferases with non-canonical substrate specificity
Mol. Microbiol.
91
887-899
2014
Helicobacter pylori (Q9ZMG5), Helicobacter pylori
brenda
Xu, H.; Ling, J.; Gao, Q.; He, H.; Mu, X.; Yan, Z.; Gao, S.; Liu, X.
Role of the lpxM lipid A biosynthesis pathway gene in pathogenicity of avian pathogenic Escherichia coli strain E058 in a chicken infection model
Vet. Microbiol.
166
516-526
2013
Escherichia coli, Escherichia coli E058
brenda
Erova, T.; Kirtley, M.; Fitts, E.; Ponnusamy, D.; Baze, W.; Andersson, J.; Cong, Y.; Tiner, B.; Sha, J.; Chopra, A.
Protective immunity elicited by oral immunization of mice with Salmonella enterica serovar typhimurium braun lipoprotein (Lpp) and acetyltransferase (MsbB) mutants
Front. Cell. Infect. Microbiol.
6
148
2016
Salmonella enterica subsp. enterica serovar Typhimurium (A0A0F6B2L6), Salmonella enterica subsp. enterica serovar Typhimurium 14028s (A0A0F6B2L6)
brenda
Taniguchi, C.; Sugawara, T.; Onoue, S.; Kawahara, K.
Structural modification of Escherichia coli lipid A by myristoyltransferase gene from Klebsiella pneumoniae
Microbiol. Immunol.
63
334-337
2019
Klebsiella pneumoniae, Klebsiella pneumoniae NBRC 14940T
brenda
Fathy Mohamed, Y.; Hamad, M.; Ortega, X.; Valvano, M.
The LpxL acyltransferase is required for normal growth and penta-acylation of lipid A in Burkholderia cenocepacia
Mol. Microbiol.
104
144-162
2017
Burkholderia cenocepacia (B4E7Z9), Burkholderia cenocepacia ATCC BAA-245 (B4E7Z9)
brenda
Dovala, D.; Rath, C.; Hu, Q.; Sawyer, W.; Shia, S.; Elling, R.; Knapp, M.; Metzger, L.I.
Structure-guided enzymology of the lipid a acyltransferase LpxM reveals a dual activity mechanism
Proc. Natl. Acad. Sci. USA
113
E6064-E6071
2016
Acinetobacter baumannii (A0A1Y1P7X1)
brenda