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

BRENDA support

Literature summary for 2.3.1.251 extracted from

  • Hittle, L.E.; Jones, J.W.; Hajjar, A.M.; Ernst, R.K.; Preston, A.
    Bordetella parapertussis PagP mediates the addition of two palmitates to the lipopolysaccharide lipid A (2015), J. Bacteriol., 197, 572-580.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.251

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + hexa-acyl lipid A Bordetella parapertussis
-
 2-acyl-sn-glycero-3-phosphocholine + hepta-acyl lipid A
-
 ?
additional information Bordetella parapertussis enzyme from Bordetella parapertussis transfers palmitates to the lipid A C-2 and C-3' positions ?
-
 ?

Organism

Organism UniProt Comment Textmining
Bordetella parapertussis Q7W4D1
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + hexa-acyl lipid A
-
 Bordetella parapertussis 2-acyl-sn-glycero-3-phosphocholine + hepta-acyl lipid A
-
 ?
additional information enzyme from Bordetella parapertussis transfers palmitates to the lipid A C-2 and C-3' positions Bordetella parapertussis ?
-
 ?

General Information

General Information Comment Organism
physiological function mutation of PagP results in a mutant strain with increased sensitivity to antimicrobial peptide killing and decreased endotoxicity Bordetella parapertussis