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Literature summary 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.
    View publication on PubMedView publication on EuropePMC

Activating Compound

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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.8.43 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

EC Number Protein Variants Comment Organism
2.7.8.43 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

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

Inhibitors

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

Localization

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.8.43 60000
-
-
 Neisseria meningitidis

Organism

EC Number Organism UniProt Comment Textmining
2.7.8.43 Neisseria meningitidis Q7DDQ9
-
-
2.7.8.43 Neisseria meningitidis NMB Q7DDQ9
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
2.4.2.53 LptA
-
-
2.7.8.43 lipid A phosphoethanolamine transferase
-
 Neisseria meningitidis
2.7.8.43 LptA
-
 Neisseria meningitidis