Literature summary for 2.7.8.43 extracted from

Piek, S.; Wang, Z.; Ganguly, J.; Lakey, A.M.; Bartley, S.N.; Mowlaboccus, S.; Anandan, A.; Stubbs, K.A.; Scanlon, M.J.; Vrielink, A.; Azadi, P.; Carlson, R.W.; Kahler, C.M.
The role of oxidoreductases in determining the function of the neisserial lipid A phosphoethanolamine transferase required for resistance to polymyxin (2014), PLoS ONE, 9, e106513.

Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	the neisserial oxidoreductase, DsbA3, contributes to the activity of LptA	Neisseria meningitidis

Cloned(Commentary)

Cloned (Comment)	Organism
gene lptA, DNA and amino acid sequence determination and analysis, genotyping in Neisseria, recombinant expression of His6-tagged enzyme in Escherichi coli strain JCB570 and in Neisseria meningitidis from low copy expression vector pCMK1001. In Escherichia coli, the stability and activity of neisserial LptA::Hisx6 is entirely dependent upon the coexpression of the EcDsbA oxidoreductase. Although expression of LptA::Hisx6 and EcDsbA in Escherichia coli results in a 32fold increase in polymyxin resistance, the proportion of lipid A headgroups substituted with PEA rises to 26%	Neisseria meningitidis

Cloned (Comment)

Organism

gene lptA, DNA and amino acid sequence determination and analysis, genotyping in Neisseria, recombinant expression of His6-tagged enzyme in Escherichi coli strain JCB570 and in Neisseria meningitidis from low copy expression vector pCMK1001. In Escherichia coli, the stability and activity of neisserial LptA::Hisx6 is entirely dependent upon the coexpression of the EcDsbA oxidoreductase. Although expression of LptA::Hisx6 and EcDsbA in Escherichia coli results in a 32fold increase in polymyxin resistance, the proportion of lipid A headgroups substituted with PEA rises to 26%

Neisseria meningitidis

Protein Variants

Protein Variants	Comment	Organism
additional information	neisserial LptA stability is dependent on the presence of an oxidoreductase DsbA, LptA::Hisx6 expressed in JCB571 (CKEC543), in which the chromosomal copy of dsbA has been insertionally inactivated, is not stable and is rapidly removed via proteolytic degradation	Neisseria meningitidis

General Stability

General Stability	Organism
all three neisserial oxidoreductases, including DsbA1, DsbA2 and DsbA3, contribute to resistance to polymyxin	Neisseria meningitidis

Inhibitors

Inhibitors	Comment	Organism	Structure
polymyxin	resistance to polymyxin for the enzyme is realized by oxidoreductase DsbA	Neisseria meningitidis

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	LptA is an integral membrane protein	Neisseria meningitidis	16020	-

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
60000	-	-	Neisseria meningitidis

Organism

Organism	UniProt	Comment	Textmining
Neisseria meningitidis	Q7DDQ9	-	-
Neisseria meningitidis NMB	Q7DDQ9	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His6-tagged enzyme from Escherichi coli strain JCB570 and Neisseria meningitidis by nickel affinity chromatography and ultrafiltration	Neisseria meningitidis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
diacylphosphatidylethanolamine + lipid A	-	Neisseria meningitidis	diacylglycerol + lipid A (2-aminoethyl diphosphate)	-	?
diacylphosphatidylethanolamine + lipid A	-	Neisseria meningitidis NMB	diacylglycerol + lipid A (2-aminoethyl diphosphate)	-	?

Subunits

Subunits	Comment	Organism
?	x * 60000, about, sequence calculation	Neisseria meningitidis

Synonyms

Synonyms	Comment	Organism
lipid A phosphoethanolamine transferase	-	Neisseria meningitidis
LptA	-	Neisseria meningitidis