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

BRENDA support

Literature summary for 2.7.8.43 extracted from

  • Cox, A.D.; Wright, J.C.; Li, J.; Hood, D.W.; Moxon, E.R.; Richards, J.C.
    Phosphorylation of the lipid A region of meningococcal lipopolysaccharide: identification of a family of transferases that add phosphoethanolamine to lipopolysaccharide (2003), J. Bacteriol., 185, 3270-3277.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.8.43

Cloned(Commentary)

Cloned (Comment) Organism
gene lptA Neisseria meningitidis

Protein Variants

Protein Variants Comment Organism
additional information construction of insertional lptA mutants from 35E (L2), H44/76 (L3), and 89I (L4) backgrounds Neisseria meningitidis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Neisseria meningitidis in all meningococcal strains examined, each lipid A species contains the basal diphosphorylated species, wherein a phosphate group is attached to each glucosamine residue. Also elaborated within the population of lipopolysacchride molecules are a variety of phosphoforms that contain either an additional phosphate residue, an additional phosphoethanolamine residue, additional phosphate and phosphoethanolamine residues, or an additional phosphate and two phosphoethanolamine residues in the lipid A, mass spectroscopic analyses, overview ?
-
 ?

Organism

Organism UniProt Comment Textmining
Neisseria meningitidis X5ELY0 serogroups A and B, diverse strains, overview, gene lptA
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information in all meningococcal strains examined, each lipid A species contains the basal diphosphorylated species, wherein a phosphate group is attached to each glucosamine residue. Also elaborated within the population of lipopolysacchride molecules are a variety of phosphoforms that contain either an additional phosphate residue, an additional phosphoethanolamine residue, additional phosphate and phosphoethanolamine residues, or an additional phosphate and two phosphoethanolamine residues in the lipid A, mass spectroscopic analyses, overview Neisseria meningitidis ?
-
 ?

Synonyms

Synonyms Comment Organism
LPS phosphoethenolamine transferase for lipid A
-
 Neisseria meningitidis
LptA
-
 Neisseria meningitidis

General Information

General Information Comment Organism
malfunction in three enzyme mutant strains, no phosphoethanolamine residues are included in the lipid A region of the lipopolysacchride and there is no further phosphorylation of lipid A beyond one additional phosphate species Neisseria meningitidis
physiological function the enzyme is responsible for the transfer of phosphoethanolamine residues to the lipid A in several Neisseria meningitidis strains. In all meningococcal strains examined, each lipid A species contains the basal diphosphorylated species, wherein a phosphate group is attached to each glucosamine residue. Also elaborated within the population of lipopolysacchride molecules are a variety of phosphoforms that contain either an additional phosphate residue, an additional phosphoethanolamine residue, additional phosphate and phosphoethanolamine residues, or an additional phosphate and two phosphoethanolamine residues in the lipid A, mass spectroscopic analyses, overview Neisseria meningitidis