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Information on EC 2.3.1.251 - lipid IVA palmitoyltransferase and Organism(s) Bordetella bronchiseptica and UniProt Accession Q7WFT9

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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 bronchiseptica
UNIPROT: Q7WFT9
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Word Map
The taxonomic range for the selected organisms is: Bordetella bronchiseptica
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 bronchiseptica transfers palmitates to the lipid A 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 bronchiseptica transfers palmitates to the lipid A C-3' positions
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
lipid A of a PagP mutant differs from wild-type lipid A by the absence of a palmitate group in secondary acylation at the C3' position. PagP mediates modification of the lipid A as part of the overall Bvg-mediated adaptation of this organism to changing environmental conditions. PagP is not required for the initial colonization of the mouse respiratory tract by Bordetella bronchiseptica, but is required for persistence of the organism within this organ
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
PagP is not required for the initial colonization of the mouse respiratory tract by Bordetella bronchiseptica, but is required for persistence of the organism within this organ
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Preston, A.; Maxim, E.; Toland, E.; Pishko, E.J.; Harvill, E.T.; Caroff, M.; Maskell, D.J.
Bordetella bronchiseptica PagP is a Bvg-regulated lipid A palmitoyl transferase that is required for persistent colonization of the mouse respiratory tract
Mol. Microbiol.
48
725-736
2003
Bordetella bronchiseptica (Q7WFT9), Bordetella bronchiseptica ATCC BAA-588 (Q7WFT9)
Manually annotated by BRENDA team