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Information on EC 2.3.1.251 - lipid IVA palmitoyltransferase and Organism(s) Bordetella parapertussis and UniProt Accession Q7W4D1

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IUBMB Comments
Isolated from the bacteria Escherichia coli and Salmonella typhimurium. The enzyme prefers phosphatidylcholine with a palmitoyl group at the sn-1 position and palmitoyl or stearoyl groups at the sn-2 position. There is some activity with corresponding phosphatidylserines but only weak activity with other diacylphosphatidyl compounds. The enzyme also acts on Kdo-(2->4)-Kdo-(2->6)-lipid IVA.
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Bordetella parapertussis
UNIPROT: Q7W4D1
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Word Map
The taxonomic range for the selected organisms is: Bordetella parapertussis
The enzyme appears in selected viruses and cellular organisms
Synonyms
lipid a palmitoyltransferase, pa1343, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
crcA
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PagP
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine:lipid-IVA palmitoyltransferase
Isolated from the bacteria Escherichia coli and Salmonella typhimurium. The enzyme prefers phosphatidylcholine with a palmitoyl group at the sn-1 position and palmitoyl or stearoyl groups at the sn-2 position. There is some activity with corresponding phosphatidylserines but only weak activity with other diacylphosphatidyl compounds. The enzyme also acts on Kdo-(2->4)-Kdo-(2->6)-lipid IVA.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + hexa-acyl lipid A
2-acyl-sn-glycero-3-phosphocholine + hepta-acyl lipid A
show the reaction diagram
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-
?
additional information
?
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enzyme from Bordetella parapertussis transfers palmitates to the lipid A C-2 and C-3' positions
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + hexa-acyl lipid A
2-acyl-sn-glycero-3-phosphocholine + hepta-acyl lipid A
show the reaction diagram
-
-
-
?
additional information
?
-
enzyme from Bordetella parapertussis transfers palmitates to the lipid A C-2 and C-3' positions
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
mutation of PagP results in a mutant strain with increased sensitivity to antimicrobial peptide killing and decreased endotoxicity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
J. Bacteriol.
197
572-580
2015
Bordetella parapertussis (Q7W4D1)
Manually annotated by BRENDA team