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Information on EC 2.3.1.265 - phosphatidylinositol dimannoside acyltransferase
for references in articles please use BRENDA:EC2.3.1.265
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.265 phosphatidylinositol dimannoside acyltransferase
IUBMB Comments
The enzyme, found in Corynebacteriales, is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIMs).
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 2.3.1.265
- mannosides
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mycobacterial
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6-position
- glycolipids
- phosphatidyl-myo-inositol
- phospholipid
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palmitoyl
- mannose
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lipomannan
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host-pathogen
- lipoarabinomannan
- envelope
- smegmatis
- palmitoyl-coa
-
mannosyltransferases
- palmitate
-
transacylase
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lipoglycans
-
fluidity
Reaction Schemes
show+
=
+
+
=
+
Synonyms
membrane acyltransferase, rv2611c, msmeg_2934, acyltransferase pata, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acyltransferase PatA
membrane acyltransferase
MSMEG 2934 protein
MSMEG_2934
PatA
phosphatidyl-myo-inositol dimannoside acyltransferase
phosphatidylinositol mannoside acyltransferase
PIM acyltransferase
PIM2 acyltransferase
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ptfP1
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Rv2611c
phosphatidyl-myo-inositol dimannoside acyltransferase
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phosphatidylinositol mannoside acyltransferase
UniProt
phosphatidylinositol mannoside acyltransferase
SwissProt
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phosphatidylinositol mannoside acyltransferase
UniProt
-
phosphatidylinositol mannoside acyltransferase
UniProt
phosphatidylinositol mannoside acyltransferase
UniProt
-
phosphatidylinositol mannoside acyltransferase
UniProt
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an acyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol = CoA + 2-O-(6-O-acyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
an acyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol = CoA + 2-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
an acyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol = CoA + 2-O-(6-O-acyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
(1)
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-
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an acyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol = CoA + 2-O-(6-O-acyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
an interfacial catalytic mechanism allows PatA to acylate hydrophobic PIMs anchored in the inner membrane of mycobacteria, through the use of water-soluble acyl-CoA donors
an acyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol = CoA + 2-O-(6-O-acyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
an interfacial catalytic mechanism allows PatA to acylate hydrophobic PIMs anchored in the inner membrane of mycobacteria, through the use of water-soluble acyl-CoA donors
-
-
an acyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol = CoA + 2-O-(6-O-acyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
an interfacial catalytic mechanism allows PatA to acylate hydrophobic PIMs anchored in the inner membrane of mycobacteria, through the use of water-soluble acyl-CoA donors
-
-
an acyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol = CoA + 2-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
(2)
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-
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an acyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol = CoA + 2-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
an interfacial catalytic mechanism allows PatA to acylate hydrophobic PIMs anchored in the inner membrane of mycobacteria, through the use of water-soluble acyl-CoA donors
an acyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol = CoA + 2-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
an interfacial catalytic mechanism allows PatA to acylate hydrophobic PIMs anchored in the inner membrane of mycobacteria, through the use of water-soluble acyl-CoA donors
-
-
an acyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol = CoA + 2-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
an interfacial catalytic mechanism allows PatA to acylate hydrophobic PIMs anchored in the inner membrane of mycobacteria, through the use of water-soluble acyl-CoA donors
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-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
phosphatidylinositol mannoside biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol acyltransferase
The enzyme, found in Corynebacteriales, is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIMs).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + acyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + lauroyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-lauroyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + myristoyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-myristoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
Substrates: preferred substrate
Products: -
Products: -
?
2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + octanoyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-octanoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + palmitoyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + stearoyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-stearoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
Substrates: low activity
Products: -
Products: -
?
acyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-acyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
lauroyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-lauroyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
myristoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-myristoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: preferred substrate
Products: -
Products: -
?
octanoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-octanoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
stearoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-stearoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: low activity
Products: -
Products: -
?
2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + acyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
Substrates: -
Products: -
Products: -
?
2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + acyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
Substrates: -
Products: -
Products: -
?
2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + acyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
Substrates: -
Products: -
Products: -
?
2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + lauroyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-lauroyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
Substrates: -
Products: -
Products: -
?
2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + lauroyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-lauroyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
Substrates: -
Products: -
Products: -
?
2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + lauroyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-lauroyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
Substrates: -
Products: -
Products: -
?
2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + octanoyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-octanoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
Substrates: low activity
Products: -
Products: -
?
2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + octanoyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-octanoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
Substrates: low activity
Products: -
Products: -
?
2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + octanoyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-octanoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
Substrates: low activity
Products: -
Products: -
?
2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + palmitoyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
Substrates: -
Products: -
Products: -
?
2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + palmitoyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
Substrates: -
Products: -
Products: -
?
2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + palmitoyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
Substrates: -
Products: -
Products: -
?
2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + palmitoyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
Substrates: -
Products: -
Products: -
?
acyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-acyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-acyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-acyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
octanoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-octanoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: low activity
Products: -
Products: -
?
octanoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-octanoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: low activity
Products: -
Products: -
?
octanoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-octanoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: low activity
Products: -
Products: -
?
palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: preferred substrate
Products: -
Products: -
?
palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
Substrates: preferred substrate
Products: -
Products: -
?
palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
Substrates: -
Products: -
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additional information
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Substrates: the active site of PatA comprises a catalytic triad consisting of the acceptor O6 atom of Manp, the imidazole ring of His126, and the carboxylate group of Glu200. In the proposed reaction mechanism, His126 acts initially as a general base to deprotonate the acceptor hydroxyl group, facilitating the nucleophilic attack on the thioester bond of palmitoyl-CoA. The carboxylic group of Glu200 contributes to the correct positioning of the imidazole ring of His126 and is involved in a charge relay system that increases the nucleophilicity of the acceptor Manp hydroxyl and modulates the pKa of His126 to act as a base in the first step and as an acid in the second step, providing protonic assistance to the departing CoA leaving group
Products: -
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additional information
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Substrates: the active site of PatA comprises a catalytic triad consisting of the acceptor O6 atom of Manp, the imidazole ring of His126, and the carboxylate group of Glu200. In the proposed reaction mechanism, His126 acts initially as a general base to deprotonate the acceptor hydroxyl group, facilitating the nucleophilic attack on the thioester bond of palmitoyl-CoA. The carboxylic group of Glu200 contributes to the correct positioning of the imidazole ring of His126 and is involved in a charge relay system that increases the nucleophilicity of the acceptor Manp hydroxyl and modulates the pKa of His126 to act as a base in the first step and as an acid in the second step, providing protonic assistance to the departing CoA leaving group
Products: -
Products: -
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additional information
?
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Substrates: the active site of PatA comprises a catalytic triad consisting of the acceptor O6 atom of Manp, the imidazole ring of His126, and the carboxylate group of Glu200. In the proposed reaction mechanism, His126 acts initially as a general base to deprotonate the acceptor hydroxyl group, facilitating the nucleophilic attack on the thioester bond of palmitoyl-CoA. The carboxylic group of Glu200 contributes to the correct positioning of the imidazole ring of His126 and is involved in a charge relay system that increases the nucleophilicity of the acceptor Manp hydroxyl and modulates the pKa of His126 to act as a base in the first step and as an acid in the second step, providing protonic assistance to the departing CoA leaving group
Products: -
Products: -
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additional information
?
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Substrates: donor and acceptor binding sites and mechanism, catalytic mechanism, detailed overview
Products: -
Products: -
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additional information
?
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Substrates: the active site of PatA comprises a catalytic triad consisting of the acceptor O6 atom of Manp, the imidazole ring of His126, and the carboxylate group of Glu200. In the proposed reaction mechanism, His126 acts initially as a general base to deprotonate the acceptor hydroxyl group, facilitating the nucleophilic attack on the thioester bond of palmitoyl-CoA. The carboxylic group of Glu200 contributes to the correct positioning of the imidazole ring of His126 and is involved in a charge relay system that increases the nucleophilicity of the acceptor Manp hydroxyl and modulates the pKa of His126 to act as a base in the first step and as an acid in the second step, providing protonic assistance to the departing CoA leaving group
Products: -
Products: -
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additional information
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Substrates: modelling of the crystal structure of PatA in complex with the Man-C16 product (PDB ID 5OCE). Analysis of PatA fatty acid chain length specificity by using the nonhydrolyzable substrates S-C12-CoA, S-C14-CoA, S-C18-CoA, and S-C20-CoA. The enzyme prefers the C14 substrate, poor or no activity with the C2 and the C20 substrates
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additional information
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Substrates: donor and acceptor binding sites and mechanism, catalytic mechanism, detailed overview
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additional information
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Substrates: the active site of PatA comprises a catalytic triad consisting of the acceptor O6 atom of Manp, the imidazole ring of His126, and the carboxylate group of Glu200. In the proposed reaction mechanism, His126 acts initially as a general base to deprotonate the acceptor hydroxyl group, facilitating the nucleophilic attack on the thioester bond of palmitoyl-CoA. The carboxylic group of Glu200 contributes to the correct positioning of the imidazole ring of His126 and is involved in a charge relay system that increases the nucleophilicity of the acceptor Manp hydroxyl and modulates the pKa of His126 to act as a base in the first step and as an acid in the second step, providing protonic assistance to the departing CoA leaving group
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additional information
?
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Substrates: donor and acceptor binding sites and mechanism, catalytic mechanism, detailed overview
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additional information
?
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Substrates: the active site of PatA comprises a catalytic triad consisting of the acceptor O6 atom of Manp, the imidazole ring of His126, and the carboxylate group of Glu200. In the proposed reaction mechanism, His126 acts initially as a general base to deprotonate the acceptor hydroxyl group, facilitating the nucleophilic attack on the thioester bond of palmitoyl-CoA. The carboxylic group of Glu200 contributes to the correct positioning of the imidazole ring of His126 and is involved in a charge relay system that increases the nucleophilicity of the acceptor Manp hydroxyl and modulates the pKa of His126 to act as a base in the first step and as an acid in the second step, providing protonic assistance to the departing CoA leaving group
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + acyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + palmitoyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
acyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-acyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + acyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
Substrates: -
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2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + acyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
Substrates: -
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2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + acyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
Substrates: -
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2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + palmitoyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
Substrates: -
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2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + palmitoyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
Substrates: -
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2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + palmitoyl-CoA
2-O-(alpha-D-mannosyl)-6-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA
Substrates: -
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acyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-acyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
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acyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-acyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
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acyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-acyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
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palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
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palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
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palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
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palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
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palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
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palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
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palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
Substrates: -
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palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
Substrates: -
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palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
Substrates: -
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palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
Substrates: -
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palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
Substrates: -
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palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
Substrates: -
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
inhibition mechanism analysis, overview
-
additional information
-
inhibition mechanism analysis, overview
-
additional information
the mutation of PatA results in isoniazid (INH) resistance in mycobacteria, implying that PatA might be a target of INH
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
Identification of the required acyltransferase step in the biosynthesis of the phosphatidylinositol mannosides of mycobacterium species.
Tuberculosis
The Molecular Mechanism of Substrate Recognition and Catalysis of the Membrane Acyltransferase PatA from Mycobacteria.
Tuberculosis
The Phosphatidyl-myo-Inositol Dimannoside Acyltransferase PatA Is Essential for Mycobacterium tuberculosis Growth In Vitro and In Vivo.
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Mycobacterium smegmatis
UniProt
brenda
i.e. Mycobacterium smegmatis
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
membrane-associated on the cytosolic side
brenda
-
membrane-associated on the cytosolic side
-
brenda
-
membrane-associated on the cytosolic side
-
brenda
PatA is an integral membrane acyltransferase tightly anchored to anionic lipid bilayers, using a two-helix structural motif and electrostatic interactions, interaction analysis and binding mechanism, PatA interaction and insertion with different lipid membrane models, overview
brenda
-
PatA is an integral membrane acyltransferase tightly anchored to anionic lipid bilayers, using a two-helix structural motif and electrostatic interactions, interaction analysis and binding mechanism, PatA interaction and insertion with different lipid membrane models, overview
-
brenda
-
PatA is an integral membrane acyltransferase tightly anchored to anionic lipid bilayers, using a two-helix structural motif and electrostatic interactions, interaction analysis and binding mechanism, PatA interaction and insertion with different lipid membrane models, overview
-
brenda
additional information
the enzyme has a large negatively charged cytoplasmic part, overview
-
brenda
additional information
-
the enzyme has a large negatively charged cytoplasmic part, overview
-
brenda
additional information
the enzyme shows a highly polarized electrostatic surface potential, which seems essential for the correct orientation of the enzyme to the cytosolic side of the plasma membrane, a key characteristic for peripheral and monotopic membrane proteins
-
brenda
additional information
-
the enzyme has a large negatively charged cytoplasmic part, overview
-
-
brenda
additional information
-
the enzyme shows a highly polarized electrostatic surface potential, which seems essential for the correct orientation of the enzyme to the cytosolic side of the plasma membrane, a key characteristic for peripheral and monotopic membrane proteins
-
-
brenda
additional information
-
the enzyme has a large negatively charged cytoplasmic part, overview
-
-
brenda
additional information
-
the enzyme shows a highly polarized electrostatic surface potential, which seems essential for the correct orientation of the enzyme to the cytosolic side of the plasma membrane, a key characteristic for peripheral and monotopic membrane proteins
-
-
brenda
additional information
the enzyme has a large negatively charged cytoplasmic part, overview
-
brenda
additional information
the enzyme shows a highly polarized electrostatic surface potential, which seems essential for the correct orientation of the enzyme to the cytosolic side of the plasma membrane, a key characteristic for peripheral and monotopic membrane proteins
-
brenda
additional information
-
the enzyme has a large negatively charged cytoplasmic part, overview
-
-
brenda
additional information
-
the enzyme shows a highly polarized electrostatic surface potential, which seems essential for the correct orientation of the enzyme to the cytosolic side of the plasma membrane, a key characteristic for peripheral and monotopic membrane proteins
-
-
brenda
additional information
-
the enzyme has a large negatively charged cytoplasmic part, overview
-
-
brenda
additional information
-
the enzyme shows a highly polarized electrostatic surface potential, which seems essential for the correct orientation of the enzyme to the cytosolic side of the plasma membrane, a key characteristic for peripheral and monotopic membrane proteins
-
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the amino-acid sequences of Mycobacterium tuberculosis and Mycobacterium smegmatis versions of PIM acyltransferase display 74% sequence identity and 84% sequence similarity. All residues that participate in both of the catalytic and substrate recognition mechanisms are strictly conserved between both proteins
evolution
the amino-acid sequences of Mycobacterium tuberculosis and Mycobacterium smegmatis versions of PIM acyltransferase display 74% sequence identity and 84% sequence similarity. All residues that participate in both of the catalytic and substrate recognition mechanisms are strictly conserved between both proteins
evolution
PatA protein homologues are conserved in mycobacteria, e.g. Mycobacterium smegmatis, Mycobacterium tuberculosis, and Mycobacterium bovis, overview. PatAmtu and PatAmsm have the same functions in regulating growth, colony surface morphology, and biofilm formation in mycobacteria, PatA sequence comparisons
evolution
PatA protein homologues are conserved in mycobacteria, e.g. Mycobacterium smegmatis, Mycobacterium tuberculosis, and Mycobacterium bovis, overview. PatAmtu and PatAmsm have the same functions in regulating growth, colony surface morphology, and biofilm formation in mycobacteria, PatA sequence comparisons
evolution
-
the amino-acid sequences of Mycobacterium tuberculosis and Mycobacterium smegmatis versions of PIM acyltransferase display 74% sequence identity and 84% sequence similarity. All residues that participate in both of the catalytic and substrate recognition mechanisms are strictly conserved between both proteins
-
evolution
-
PatA protein homologues are conserved in mycobacteria, e.g. Mycobacterium smegmatis, Mycobacterium tuberculosis, and Mycobacterium bovis, overview. PatAmtu and PatAmsm have the same functions in regulating growth, colony surface morphology, and biofilm formation in mycobacteria, PatA sequence comparisons
-
evolution
-
the amino-acid sequences of Mycobacterium tuberculosis and Mycobacterium smegmatis versions of PIM acyltransferase display 74% sequence identity and 84% sequence similarity. All residues that participate in both of the catalytic and substrate recognition mechanisms are strictly conserved between both proteins
-
evolution
-
PatA protein homologues are conserved in mycobacteria, e.g. Mycobacterium smegmatis, Mycobacterium tuberculosis, and Mycobacterium bovis, overview. PatAmtu and PatAmsm have the same functions in regulating growth, colony surface morphology, and biofilm formation in mycobacteria, PatA sequence comparisons
-
evolution
-
the amino-acid sequences of Mycobacterium tuberculosis and Mycobacterium smegmatis versions of PIM acyltransferase display 74% sequence identity and 84% sequence similarity. All residues that participate in both of the catalytic and substrate recognition mechanisms are strictly conserved between both proteins
-
evolution
-
PatA protein homologues are conserved in mycobacteria, e.g. Mycobacterium smegmatis, Mycobacterium tuberculosis, and Mycobacterium bovis, overview. PatAmtu and PatAmsm have the same functions in regulating growth, colony surface morphology, and biofilm formation in mycobacteria, PatA sequence comparisons
-
evolution
-
the amino-acid sequences of Mycobacterium tuberculosis and Mycobacterium smegmatis versions of PIM acyltransferase display 74% sequence identity and 84% sequence similarity. All residues that participate in both of the catalytic and substrate recognition mechanisms are strictly conserved between both proteins
-
evolution
-
PatA protein homologues are conserved in mycobacteria, e.g. Mycobacterium smegmatis, Mycobacterium tuberculosis, and Mycobacterium bovis, overview. PatAmtu and PatAmsm have the same functions in regulating growth, colony surface morphology, and biofilm formation in mycobacteria, PatA sequence comparisons
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malfunction
disruption of gene Rv2611c abolishes the growth of Mycobacterium tuberculosis
malfunction
disruption of gene MSMEG_2934 severely affects the groth of Mycobacterium smegmatis
malfunction
silencing of patA in axenic cultures results in bacterial death. Production of PIM is greatly reduced in patA-depleted mycobacteria. In strain TB506.1, a reduction is observed in lipid bands I, II, and III, corresponding to Ac1PIM6, Ac2PIM6, and Ac1PIM2, respectively
malfunction
deletion of patA significantly enhances isoniazid (INH) resistance in Mycobacterum smegmatis, although it reduces bacterial biofilm formation. This might be due to the fact that the patA deletion promotes the synthesis of mycolic acids through an unknown synthesis pathway other than the reported fatty acid synthase (FAS) pathway, which could effectively counteract the inhibition by INH of mycolic acid synthesis in mycobacteria. Deletion of patA affects the stress resistance and reduces cell growth
malfunction
-
disruption of gene Rv2611c abolishes the growth of Mycobacterium tuberculosis
-
malfunction
-
silencing of patA in axenic cultures results in bacterial death. Production of PIM is greatly reduced in patA-depleted mycobacteria. In strain TB506.1, a reduction is observed in lipid bands I, II, and III, corresponding to Ac1PIM6, Ac2PIM6, and Ac1PIM2, respectively
-
malfunction
-
disruption of gene MSMEG_2934 severely affects the groth of Mycobacterium smegmatis
-
malfunction
-
deletion of patA significantly enhances isoniazid (INH) resistance in Mycobacterum smegmatis, although it reduces bacterial biofilm formation. This might be due to the fact that the patA deletion promotes the synthesis of mycolic acids through an unknown synthesis pathway other than the reported fatty acid synthase (FAS) pathway, which could effectively counteract the inhibition by INH of mycolic acid synthesis in mycobacteria. Deletion of patA affects the stress resistance and reduces cell growth
-
malfunction
-
disruption of gene MSMEG_2934 severely affects the groth of Mycobacterium smegmatis
-
malfunction
-
deletion of patA significantly enhances isoniazid (INH) resistance in Mycobacterum smegmatis, although it reduces bacterial biofilm formation. This might be due to the fact that the patA deletion promotes the synthesis of mycolic acids through an unknown synthesis pathway other than the reported fatty acid synthase (FAS) pathway, which could effectively counteract the inhibition by INH of mycolic acid synthesis in mycobacteria. Deletion of patA affects the stress resistance and reduces cell growth
-
malfunction
-
disruption of gene Rv2611c abolishes the growth of Mycobacterium tuberculosis
-
malfunction
-
silencing of patA in axenic cultures results in bacterial death. Production of PIM is greatly reduced in patA-depleted mycobacteria. In strain TB506.1, a reduction is observed in lipid bands I, II, and III, corresponding to Ac1PIM6, Ac2PIM6, and Ac1PIM2, respectively
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metabolism
the enzyme is part of the PIM biosynthetic pathway in mycobacteria, overview
metabolism
the enzyme is part of the PIM biosynthetic pathway in mycobacteria, overview
metabolism
the enzyme is part of the PIM biosynthetic pathway in mycobacteria, detailed overview. Ac1PIM6 and Ac2PIM6 seems to be located in the outer leaflet of the inner membrane. Palmitic acid (C16:0) and 10-methyloctadecanoic acid (i.e. tuberculostearic acid) are the major fatty acid constituents of the biochemically isolated inner membrane. PIM2 is composed of two mannose (Man) residues attached to positions 2 and 6 of the myo-inositol ring of phosphatidyl-1D-myo-inositol (PI), whereas PIM6 is composed of a pentamannosyl group, t-alpha-Man(1->2)-alpha-Man(1->2)-alpha-Man(1->6)-alpha-Man(1->6)-alpha-Man(1->, attached to position 6 of the myo-inositol ring), in addition to the Manp residue present at position 2. The triacylated forms of PIM2 and PIM6 (Ac1PIM2 and Ac1PIM6) show major acyl forms containing two palmitic acid residues (C16) and one tuberculostearic acid residue (10-methyloctadecanoate, C19), where one fatty acyl chain is linked to the Manp residue attached to position 2 of myo-inositol, and two fatty acyl chains are located on the glycerol moiety. The tetraacylated forms, Ac2PIM2 and Ac2PIM6, are present predominantly as two populations bearing either three C16/one C19 or two C16/two C19. Two fatty acyl chains are located on the glycerol moiety, one fatty acyl chain is linked to the Manp residue attached to position 2 of myo-inositol and one fatty acyl chain is attached to position 3 of the myo-inositol unit
metabolism
the enzyme is part of the PIM biosynthetic pathway in mycobacteria, detailed overview. Ac1PIM6 and Ac2PIM6 seems to be located in the outer leaflet of the inner membrane. Palmitic acid (C16:0) and 10-methyloctadecanoic acid (i.e. tuberculostearic acid) are the major fatty acid constituents of the biochemically isolated inner membrane. PIM2 is composed of two mannose (Man) residues attached to positions 2 and 6 of the myo-inositol ring of phosphatidyl-1D-myo-inositol (PI), whereas PIM6 is composed of a pentamannosyl group, t-alpha-Man(1->2)-alpha-Man(1->2)-alpha-Man(1->6)-alpha-Man(1->6)-alpha-Man(1->, attached to position 6 of the myo-inositol ring), in addition to the Manp residue present at position 2. The triacylated forms of PIM2 and PIM6 (Ac1PIM2 and Ac1PIM6) show major acyl forms containing two palmitic acid residues (C16) and one tuberculostearic acid residue (10-methyloctadecanoate, C19), where one fatty acyl chain is linked to the Manp residue attached to position 2 of myo-inositol, and two fatty acyl chains are located on the glycerol moiety. The tetraacylated forms, Ac2PIM2 and Ac2PIM6, are present predominantly as two populations bearing either three C16/one C19 or two C16/two C19. Two fatty acyl chains are located on the glycerol moiety, one fatty acyl chain is linked to the Manp residue attached to position 2 of myo-inositol and one fatty acyl chain is attached to position 3 of the myo-inositol unit
metabolism
PatA is a membrane-associated acyltransferase that transfers a palmitoyl moiety from palmitoyl coenzyme A (palmitoyl-CoA) to the 6-position of the mannose ring linked to the 2-position of inositol in PIM1/PIM2. PIMs are based on a phosphatidyl-myo-inositol (PI) anchor and can contain one to six mannose residues and up to four acyl chains. The tri- and tetra-acylated phosphatidyl-myo-inositol dimannosides (Ac1PIM2 and Ac2PIM2, respectively) are considered both metabolic end products and intermediates in the biosynthesis of the tri- and tetra-phosphatidyl-myo-inositol hexamannosides (Ac1PIM6 and Ac2PIM6, respectively), lipomannan (LM), and lipoarabinomannan (LAM)
metabolism
proposed PIM biosynthetic pathway in mycobacteria, overview. The mannosylation steps of the PIM derivatives start in the cytosolic face of the IM with the consecutive mannosylation of PI, catalyzed by PimA and PimB to form PIM2. PIMs are further acylated by PatA and by a not yet identified acyltransferase, to form Ac1PIM2 and Ac2PIM2, at the cytosolic face of the IM, respectively. The inner leaflet of the inner mycobacterial membrane (IM) is likely composed nearly entirely of Ac2PIM2. Although Ac1PIM2/Ac2PIM2 and Ac1PIM6/Ac2PIM6 are the most abundant forms of PIMs in Mycobacterium bovis BCG, Mycobacterium tuberculosis H37Rv, and Mycobacterium smegmatis 607, all forms of PIM2 could eventually translocate to the outer leaflet of the IM
metabolism
-
the enzyme is part of the PIM biosynthetic pathway in mycobacteria, overview
-
metabolism
-
the enzyme is part of the PIM biosynthetic pathway in mycobacteria, detailed overview. Ac1PIM6 and Ac2PIM6 seems to be located in the outer leaflet of the inner membrane. Palmitic acid (C16:0) and 10-methyloctadecanoic acid (i.e. tuberculostearic acid) are the major fatty acid constituents of the biochemically isolated inner membrane. PIM2 is composed of two mannose (Man) residues attached to positions 2 and 6 of the myo-inositol ring of phosphatidyl-1D-myo-inositol (PI), whereas PIM6 is composed of a pentamannosyl group, t-alpha-Man(1->2)-alpha-Man(1->2)-alpha-Man(1->6)-alpha-Man(1->6)-alpha-Man(1->, attached to position 6 of the myo-inositol ring), in addition to the Manp residue present at position 2. The triacylated forms of PIM2 and PIM6 (Ac1PIM2 and Ac1PIM6) show major acyl forms containing two palmitic acid residues (C16) and one tuberculostearic acid residue (10-methyloctadecanoate, C19), where one fatty acyl chain is linked to the Manp residue attached to position 2 of myo-inositol, and two fatty acyl chains are located on the glycerol moiety. The tetraacylated forms, Ac2PIM2 and Ac2PIM6, are present predominantly as two populations bearing either three C16/one C19 or two C16/two C19. Two fatty acyl chains are located on the glycerol moiety, one fatty acyl chain is linked to the Manp residue attached to position 2 of myo-inositol and one fatty acyl chain is attached to position 3 of the myo-inositol unit
-
metabolism
-
PatA is a membrane-associated acyltransferase that transfers a palmitoyl moiety from palmitoyl coenzyme A (palmitoyl-CoA) to the 6-position of the mannose ring linked to the 2-position of inositol in PIM1/PIM2. PIMs are based on a phosphatidyl-myo-inositol (PI) anchor and can contain one to six mannose residues and up to four acyl chains. The tri- and tetra-acylated phosphatidyl-myo-inositol dimannosides (Ac1PIM2 and Ac2PIM2, respectively) are considered both metabolic end products and intermediates in the biosynthesis of the tri- and tetra-phosphatidyl-myo-inositol hexamannosides (Ac1PIM6 and Ac2PIM6, respectively), lipomannan (LM), and lipoarabinomannan (LAM)
-
metabolism
-
the enzyme is part of the PIM biosynthetic pathway in mycobacteria, overview
-
metabolism
-
the enzyme is part of the PIM biosynthetic pathway in mycobacteria, detailed overview. Ac1PIM6 and Ac2PIM6 seems to be located in the outer leaflet of the inner membrane. Palmitic acid (C16:0) and 10-methyloctadecanoic acid (i.e. tuberculostearic acid) are the major fatty acid constituents of the biochemically isolated inner membrane. PIM2 is composed of two mannose (Man) residues attached to positions 2 and 6 of the myo-inositol ring of phosphatidyl-1D-myo-inositol (PI), whereas PIM6 is composed of a pentamannosyl group, t-alpha-Man(1->2)-alpha-Man(1->2)-alpha-Man(1->6)-alpha-Man(1->6)-alpha-Man(1->, attached to position 6 of the myo-inositol ring), in addition to the Manp residue present at position 2. The triacylated forms of PIM2 and PIM6 (Ac1PIM2 and Ac1PIM6) show major acyl forms containing two palmitic acid residues (C16) and one tuberculostearic acid residue (10-methyloctadecanoate, C19), where one fatty acyl chain is linked to the Manp residue attached to position 2 of myo-inositol, and two fatty acyl chains are located on the glycerol moiety. The tetraacylated forms, Ac2PIM2 and Ac2PIM6, are present predominantly as two populations bearing either three C16/one C19 or two C16/two C19. Two fatty acyl chains are located on the glycerol moiety, one fatty acyl chain is linked to the Manp residue attached to position 2 of myo-inositol and one fatty acyl chain is attached to position 3 of the myo-inositol unit
-
metabolism
-
proposed PIM biosynthetic pathway in mycobacteria, overview. The mannosylation steps of the PIM derivatives start in the cytosolic face of the IM with the consecutive mannosylation of PI, catalyzed by PimA and PimB to form PIM2. PIMs are further acylated by PatA and by a not yet identified acyltransferase, to form Ac1PIM2 and Ac2PIM2, at the cytosolic face of the IM, respectively. The inner leaflet of the inner mycobacterial membrane (IM) is likely composed nearly entirely of Ac2PIM2. Although Ac1PIM2/Ac2PIM2 and Ac1PIM6/Ac2PIM6 are the most abundant forms of PIMs in Mycobacterium bovis BCG, Mycobacterium tuberculosis H37Rv, and Mycobacterium smegmatis 607, all forms of PIM2 could eventually translocate to the outer leaflet of the IM
-
metabolism
-
the enzyme is part of the PIM biosynthetic pathway in mycobacteria, overview
-
metabolism
-
the enzyme is part of the PIM biosynthetic pathway in mycobacteria, detailed overview. Ac1PIM6 and Ac2PIM6 seems to be located in the outer leaflet of the inner membrane. Palmitic acid (C16:0) and 10-methyloctadecanoic acid (i.e. tuberculostearic acid) are the major fatty acid constituents of the biochemically isolated inner membrane. PIM2 is composed of two mannose (Man) residues attached to positions 2 and 6 of the myo-inositol ring of phosphatidyl-1D-myo-inositol (PI), whereas PIM6 is composed of a pentamannosyl group, t-alpha-Man(1->2)-alpha-Man(1->2)-alpha-Man(1->6)-alpha-Man(1->6)-alpha-Man(1->, attached to position 6 of the myo-inositol ring), in addition to the Manp residue present at position 2. The triacylated forms of PIM2 and PIM6 (Ac1PIM2 and Ac1PIM6) show major acyl forms containing two palmitic acid residues (C16) and one tuberculostearic acid residue (10-methyloctadecanoate, C19), where one fatty acyl chain is linked to the Manp residue attached to position 2 of myo-inositol, and two fatty acyl chains are located on the glycerol moiety. The tetraacylated forms, Ac2PIM2 and Ac2PIM6, are present predominantly as two populations bearing either three C16/one C19 or two C16/two C19. Two fatty acyl chains are located on the glycerol moiety, one fatty acyl chain is linked to the Manp residue attached to position 2 of myo-inositol and one fatty acyl chain is attached to position 3 of the myo-inositol unit
-
metabolism
-
proposed PIM biosynthetic pathway in mycobacteria, overview. The mannosylation steps of the PIM derivatives start in the cytosolic face of the IM with the consecutive mannosylation of PI, catalyzed by PimA and PimB to form PIM2. PIMs are further acylated by PatA and by a not yet identified acyltransferase, to form Ac1PIM2 and Ac2PIM2, at the cytosolic face of the IM, respectively. The inner leaflet of the inner mycobacterial membrane (IM) is likely composed nearly entirely of Ac2PIM2. Although Ac1PIM2/Ac2PIM2 and Ac1PIM6/Ac2PIM6 are the most abundant forms of PIMs in Mycobacterium bovis BCG, Mycobacterium tuberculosis H37Rv, and Mycobacterium smegmatis 607, all forms of PIM2 could eventually translocate to the outer leaflet of the IM
-
metabolism
-
the enzyme is part of the PIM biosynthetic pathway in mycobacteria, overview
-
metabolism
-
the enzyme is part of the PIM biosynthetic pathway in mycobacteria, detailed overview. Ac1PIM6 and Ac2PIM6 seems to be located in the outer leaflet of the inner membrane. Palmitic acid (C16:0) and 10-methyloctadecanoic acid (i.e. tuberculostearic acid) are the major fatty acid constituents of the biochemically isolated inner membrane. PIM2 is composed of two mannose (Man) residues attached to positions 2 and 6 of the myo-inositol ring of phosphatidyl-1D-myo-inositol (PI), whereas PIM6 is composed of a pentamannosyl group, t-alpha-Man(1->2)-alpha-Man(1->2)-alpha-Man(1->6)-alpha-Man(1->6)-alpha-Man(1->, attached to position 6 of the myo-inositol ring), in addition to the Manp residue present at position 2. The triacylated forms of PIM2 and PIM6 (Ac1PIM2 and Ac1PIM6) show major acyl forms containing two palmitic acid residues (C16) and one tuberculostearic acid residue (10-methyloctadecanoate, C19), where one fatty acyl chain is linked to the Manp residue attached to position 2 of myo-inositol, and two fatty acyl chains are located on the glycerol moiety. The tetraacylated forms, Ac2PIM2 and Ac2PIM6, are present predominantly as two populations bearing either three C16/one C19 or two C16/two C19. Two fatty acyl chains are located on the glycerol moiety, one fatty acyl chain is linked to the Manp residue attached to position 2 of myo-inositol and one fatty acyl chain is attached to position 3 of the myo-inositol unit
-
metabolism
-
PatA is a membrane-associated acyltransferase that transfers a palmitoyl moiety from palmitoyl coenzyme A (palmitoyl-CoA) to the 6-position of the mannose ring linked to the 2-position of inositol in PIM1/PIM2. PIMs are based on a phosphatidyl-myo-inositol (PI) anchor and can contain one to six mannose residues and up to four acyl chains. The tri- and tetra-acylated phosphatidyl-myo-inositol dimannosides (Ac1PIM2 and Ac2PIM2, respectively) are considered both metabolic end products and intermediates in the biosynthesis of the tri- and tetra-phosphatidyl-myo-inositol hexamannosides (Ac1PIM6 and Ac2PIM6, respectively), lipomannan (LM), and lipoarabinomannan (LAM)
-
physiological function
the PIM acyltransferase (PatA) is an essential membrane associated acyltransferase, it transfers a palmitoyl moiety from palmitoyl-CoA to the 6-position of the mannose ring linked to 2-position of inositol in PIM1/PIM2 resulting in Ac1PIM1 and Ac1PIM2
physiological function
the PIM acyltransferase (PatA) is an essential membrane associated acyltransferase, it transfers a palmitoyl moiety from palmitoyl-CoA to the 6-position of the mannose ring linked to 2-position of inositol in PIM1/PIM2 resulting in Ac1PIM1 and Ac1PIM2
physiological function
Mycobacterium tuberculosis comprises an unusual cell envelope dominated by unique lipids and glycans that provides a permeability barrier against hydrophilic drugs and is central for its survival and virulence. Phosphatidyl-myo-inositol mannosides (PIMs) are glycolipids considered to be not only key structural components of the cell envelope but also precursors of lipomannan (LM) and lipoarabinomannan (LAM), important lipoglycans implicated in host-pathogen interactions. PatA is a membrane-associated acyltransferase that transfers a palmitoyl moiety from palmitoyl coenzyme A (palmitoyl-CoA) to the 6-position of the mannose ring linked to the 2-position of inositol in PIM1/PIM2. The function of PatA is vital for Mycobacterium tuberculosis in vitro and in vivo, requirement of PatA for viability. Gene patA is essential for growth in macrophages and in mice
physiological function
enzyme PatA is a membrane-associated acyltransferase and synthesizes phosphatidyl-myo-inositol mannosides (PIMs) in mycobacteria. PatA negatively regulates isoniazid resistance by mediating mycolic acid synthesis and controls biofilm formation by affecting lipid synthesis in mycobacteria, modelling of the positive regulation of biofilm formation by mycobacteria, overview. PatA affects colony surface morphology and biofilm formation and positively regulates stress resistance in Mycobacterium smegmatis
physiological function
enzyme PatA is a membrane-associated acyltransferase and synthesizes phosphatidyl-myo-inositol mannosides (PIMs) in mycobacteria. PatA negatively regulates isoniazid resistance by mediating mycolic acid synthesis and controls biofilm formation by affecting lipid synthesis in mycobacteria, modelling of the positive regulation of biofilm formation by mycobacteria, overview
physiological function
glycolipids are prominent components of bacterial membranes that play critical roles not only in maintaining the structural integrity of the cell but also in modulating host-pathogen interactions. PatA is an essential acyltransferase involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIMs), key structural elements and virulence factors of Mycobacterium tuberculosis. PatA dictates the acyl chain composition of the glycolipid by using an acyl chain selectivity ruler. Proposal of an interfacial catalytic mechanism that allows PatA to acylate hydrophobic PIMs anchored in the inner membrane of mycobacteria, through the use of water-soluble acyl-CoA donors. PatA preferentially binds to anionic phospholipids
physiological function
-
the PIM acyltransferase (PatA) is an essential membrane associated acyltransferase, it transfers a palmitoyl moiety from palmitoyl-CoA to the 6-position of the mannose ring linked to 2-position of inositol in PIM1/PIM2 resulting in Ac1PIM1 and Ac1PIM2
-
physiological function
-
Mycobacterium tuberculosis comprises an unusual cell envelope dominated by unique lipids and glycans that provides a permeability barrier against hydrophilic drugs and is central for its survival and virulence. Phosphatidyl-myo-inositol mannosides (PIMs) are glycolipids considered to be not only key structural components of the cell envelope but also precursors of lipomannan (LM) and lipoarabinomannan (LAM), important lipoglycans implicated in host-pathogen interactions. PatA is a membrane-associated acyltransferase that transfers a palmitoyl moiety from palmitoyl coenzyme A (palmitoyl-CoA) to the 6-position of the mannose ring linked to the 2-position of inositol in PIM1/PIM2. The function of PatA is vital for Mycobacterium tuberculosis in vitro and in vivo, requirement of PatA for viability. Gene patA is essential for growth in macrophages and in mice
-
physiological function
-
enzyme PatA is a membrane-associated acyltransferase and synthesizes phosphatidyl-myo-inositol mannosides (PIMs) in mycobacteria. PatA negatively regulates isoniazid resistance by mediating mycolic acid synthesis and controls biofilm formation by affecting lipid synthesis in mycobacteria, modelling of the positive regulation of biofilm formation by mycobacteria, overview
-
physiological function
-
the PIM acyltransferase (PatA) is an essential membrane associated acyltransferase, it transfers a palmitoyl moiety from palmitoyl-CoA to the 6-position of the mannose ring linked to 2-position of inositol in PIM1/PIM2 resulting in Ac1PIM1 and Ac1PIM2
-
physiological function
-
enzyme PatA is a membrane-associated acyltransferase and synthesizes phosphatidyl-myo-inositol mannosides (PIMs) in mycobacteria. PatA negatively regulates isoniazid resistance by mediating mycolic acid synthesis and controls biofilm formation by affecting lipid synthesis in mycobacteria, modelling of the positive regulation of biofilm formation by mycobacteria, overview. PatA affects colony surface morphology and biofilm formation and positively regulates stress resistance in Mycobacterium smegmatis
-
physiological function
-
glycolipids are prominent components of bacterial membranes that play critical roles not only in maintaining the structural integrity of the cell but also in modulating host-pathogen interactions. PatA is an essential acyltransferase involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIMs), key structural elements and virulence factors of Mycobacterium tuberculosis. PatA dictates the acyl chain composition of the glycolipid by using an acyl chain selectivity ruler. Proposal of an interfacial catalytic mechanism that allows PatA to acylate hydrophobic PIMs anchored in the inner membrane of mycobacteria, through the use of water-soluble acyl-CoA donors. PatA preferentially binds to anionic phospholipids
-
physiological function
-
the PIM acyltransferase (PatA) is an essential membrane associated acyltransferase, it transfers a palmitoyl moiety from palmitoyl-CoA to the 6-position of the mannose ring linked to 2-position of inositol in PIM1/PIM2 resulting in Ac1PIM1 and Ac1PIM2
-
physiological function
-
enzyme PatA is a membrane-associated acyltransferase and synthesizes phosphatidyl-myo-inositol mannosides (PIMs) in mycobacteria. PatA negatively regulates isoniazid resistance by mediating mycolic acid synthesis and controls biofilm formation by affecting lipid synthesis in mycobacteria, modelling of the positive regulation of biofilm formation by mycobacteria, overview. PatA affects colony surface morphology and biofilm formation and positively regulates stress resistance in Mycobacterium smegmatis
-
physiological function
-
glycolipids are prominent components of bacterial membranes that play critical roles not only in maintaining the structural integrity of the cell but also in modulating host-pathogen interactions. PatA is an essential acyltransferase involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIMs), key structural elements and virulence factors of Mycobacterium tuberculosis. PatA dictates the acyl chain composition of the glycolipid by using an acyl chain selectivity ruler. Proposal of an interfacial catalytic mechanism that allows PatA to acylate hydrophobic PIMs anchored in the inner membrane of mycobacteria, through the use of water-soluble acyl-CoA donors. PatA preferentially binds to anionic phospholipids
-
physiological function
-
the PIM acyltransferase (PatA) is an essential membrane associated acyltransferase, it transfers a palmitoyl moiety from palmitoyl-CoA to the 6-position of the mannose ring linked to 2-position of inositol in PIM1/PIM2 resulting in Ac1PIM1 and Ac1PIM2
-
physiological function
-
Mycobacterium tuberculosis comprises an unusual cell envelope dominated by unique lipids and glycans that provides a permeability barrier against hydrophilic drugs and is central for its survival and virulence. Phosphatidyl-myo-inositol mannosides (PIMs) are glycolipids considered to be not only key structural components of the cell envelope but also precursors of lipomannan (LM) and lipoarabinomannan (LAM), important lipoglycans implicated in host-pathogen interactions. PatA is a membrane-associated acyltransferase that transfers a palmitoyl moiety from palmitoyl coenzyme A (palmitoyl-CoA) to the 6-position of the mannose ring linked to the 2-position of inositol in PIM1/PIM2. The function of PatA is vital for Mycobacterium tuberculosis in vitro and in vivo, requirement of PatA for viability. Gene patA is essential for growth in macrophages and in mice
-
physiological function
-
enzyme PatA is a membrane-associated acyltransferase and synthesizes phosphatidyl-myo-inositol mannosides (PIMs) in mycobacteria. PatA negatively regulates isoniazid resistance by mediating mycolic acid synthesis and controls biofilm formation by affecting lipid synthesis in mycobacteria, modelling of the positive regulation of biofilm formation by mycobacteria, overview
-
additional information
the enzyme catalyzes the transfer of a palmitoyl moiety from palmitoyl-CoA to the 6-position of the mannose ring linked to the 2-position of inositol in PIM1/PIM2. The crystal structure of the enzyme in the presence of 6-O-palmitoyl-alpha-D-mannopyranoside unravels the acceptor binding mechanism. The acceptor mannose ring localizes in a cavity at the end of a surface-exposed long groove where the active site is located, whereas the palmitate moiety accommodates into a hydrophobic pocket deeply buried in the alpha/beta core of the protein. Both fatty acyl chains of the PIM2 acceptor are essential for the reaction to take place, highlighting their critical role in the generation of a competent active site. By the use of combined structural and quantummechanics/molecular-mechanics (QM/MM) meta-dynamics, the catalytic mechanism of PatA is described at the atomic-electronic level, detailed structural rationale for a stepwise reaction, with the generation of a tetrahedral transition state for the rate-determining step, glycolipid acceptor binding site and the catalytic mechanism of PatA, overview
additional information
-
the enzyme catalyzes the transfer of a palmitoyl moiety from palmitoyl-CoA to the 6-position of the mannose ring linked to the 2-position of inositol in PIM1/PIM2. The crystal structure of the enzyme in the presence of 6-O-palmitoyl-alpha-D-mannopyranoside unravels the acceptor binding mechanism. The acceptor mannose ring localizes in a cavity at the end of a surface-exposed long groove where the active site is located, whereas the palmitate moiety accommodates into a hydrophobic pocket deeply buried in the alpha/beta core of the protein. Both fatty acyl chains of the PIM2 acceptor are essential for the reaction to take place, highlighting their critical role in the generation of a competent active site. By the use of combined structural and quantummechanics/molecular-mechanics (QM/MM) meta-dynamics, the catalytic mechanism of PatA is described at the atomic-electronic level, detailed structural rationale for a stepwise reaction, with the generation of a tetrahedral transition state for the rate-determining step, glycolipid acceptor binding site and the catalytic mechanism of PatA, overview
additional information
the enzyme catalyzes the transfer of a palmitoyl moiety from palmitoyl-CoA to the 6-position of the mannose ring linked to the 2-position of inositol in PIM1/PIM2. The crystal structure of the enzyme in the presence of 6-O-palmitoyl-alpha-D-mannopyranoside unravels the acceptor binding mechanism. The acceptor mannose ring localizes in a cavity at the end of a surface-exposed long groove where the active site is located, whereas the palmitate moiety accommodates into a hydrophobic pocket deeply buried in the alpha/beta core of the protein. Both fatty acyl chains of the PIM2 acceptor are essential for the reaction to take place, highlighting their critical role in the generation of a competent active site. By the use of combined structural and quantummechanics/molecular-mechanics (QM/MM) meta-dynamics, the catalytic mechanism of PatA is described at the atomic-electronic level, detailed structural rationale for a stepwise reaction, with the generation of a tetrahedral transition state for the rate-determining step, glycolipid acceptor binding site and the catalytic mechanism of PatA, structure homology modeling, overview
additional information
lipid profile characterization by thin-layer chromatography
additional information
enzyme PatA inserts into anionic phospholipid monolayers and this insertion modifies the dynamics of the anionic phospholipid bilayers, DMPG lipid bilayers, detailed overview. A two-helix motif positions PatA active site for catalysis within the membrane bilayer, and a ruler mechanism is used for acyl chains recognition with acyl chains of different lengths
additional information
-
the enzyme catalyzes the transfer of a palmitoyl moiety from palmitoyl-CoA to the 6-position of the mannose ring linked to the 2-position of inositol in PIM1/PIM2. The crystal structure of the enzyme in the presence of 6-O-palmitoyl-alpha-D-mannopyranoside unravels the acceptor binding mechanism. The acceptor mannose ring localizes in a cavity at the end of a surface-exposed long groove where the active site is located, whereas the palmitate moiety accommodates into a hydrophobic pocket deeply buried in the alpha/beta core of the protein. Both fatty acyl chains of the PIM2 acceptor are essential for the reaction to take place, highlighting their critical role in the generation of a competent active site. By the use of combined structural and quantummechanics/molecular-mechanics (QM/MM) meta-dynamics, the catalytic mechanism of PatA is described at the atomic-electronic level, detailed structural rationale for a stepwise reaction, with the generation of a tetrahedral transition state for the rate-determining step, glycolipid acceptor binding site and the catalytic mechanism of PatA, overview
-
additional information
-
lipid profile characterization by thin-layer chromatography
-
additional information
-
the enzyme catalyzes the transfer of a palmitoyl moiety from palmitoyl-CoA to the 6-position of the mannose ring linked to the 2-position of inositol in PIM1/PIM2. The crystal structure of the enzyme in the presence of 6-O-palmitoyl-alpha-D-mannopyranoside unravels the acceptor binding mechanism. The acceptor mannose ring localizes in a cavity at the end of a surface-exposed long groove where the active site is located, whereas the palmitate moiety accommodates into a hydrophobic pocket deeply buried in the alpha/beta core of the protein. Both fatty acyl chains of the PIM2 acceptor are essential for the reaction to take place, highlighting their critical role in the generation of a competent active site. By the use of combined structural and quantummechanics/molecular-mechanics (QM/MM) meta-dynamics, the catalytic mechanism of PatA is described at the atomic-electronic level, detailed structural rationale for a stepwise reaction, with the generation of a tetrahedral transition state for the rate-determining step, glycolipid acceptor binding site and the catalytic mechanism of PatA, structure homology modeling, overview
-
additional information
-
enzyme PatA inserts into anionic phospholipid monolayers and this insertion modifies the dynamics of the anionic phospholipid bilayers, DMPG lipid bilayers, detailed overview. A two-helix motif positions PatA active site for catalysis within the membrane bilayer, and a ruler mechanism is used for acyl chains recognition with acyl chains of different lengths
-
additional information
-
the enzyme catalyzes the transfer of a palmitoyl moiety from palmitoyl-CoA to the 6-position of the mannose ring linked to the 2-position of inositol in PIM1/PIM2. The crystal structure of the enzyme in the presence of 6-O-palmitoyl-alpha-D-mannopyranoside unravels the acceptor binding mechanism. The acceptor mannose ring localizes in a cavity at the end of a surface-exposed long groove where the active site is located, whereas the palmitate moiety accommodates into a hydrophobic pocket deeply buried in the alpha/beta core of the protein. Both fatty acyl chains of the PIM2 acceptor are essential for the reaction to take place, highlighting their critical role in the generation of a competent active site. By the use of combined structural and quantummechanics/molecular-mechanics (QM/MM) meta-dynamics, the catalytic mechanism of PatA is described at the atomic-electronic level, detailed structural rationale for a stepwise reaction, with the generation of a tetrahedral transition state for the rate-determining step, glycolipid acceptor binding site and the catalytic mechanism of PatA, structure homology modeling, overview
-
additional information
-
enzyme PatA inserts into anionic phospholipid monolayers and this insertion modifies the dynamics of the anionic phospholipid bilayers, DMPG lipid bilayers, detailed overview. A two-helix motif positions PatA active site for catalysis within the membrane bilayer, and a ruler mechanism is used for acyl chains recognition with acyl chains of different lengths
-
additional information
-
the enzyme catalyzes the transfer of a palmitoyl moiety from palmitoyl-CoA to the 6-position of the mannose ring linked to the 2-position of inositol in PIM1/PIM2. The crystal structure of the enzyme in the presence of 6-O-palmitoyl-alpha-D-mannopyranoside unravels the acceptor binding mechanism. The acceptor mannose ring localizes in a cavity at the end of a surface-exposed long groove where the active site is located, whereas the palmitate moiety accommodates into a hydrophobic pocket deeply buried in the alpha/beta core of the protein. Both fatty acyl chains of the PIM2 acceptor are essential for the reaction to take place, highlighting their critical role in the generation of a competent active site. By the use of combined structural and quantummechanics/molecular-mechanics (QM/MM) meta-dynamics, the catalytic mechanism of PatA is described at the atomic-electronic level, detailed structural rationale for a stepwise reaction, with the generation of a tetrahedral transition state for the rate-determining step, glycolipid acceptor binding site and the catalytic mechanism of PatA, overview
-
additional information
-
lipid profile characterization by thin-layer chromatography
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ACYLT_MYCS2
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
304
0
33554
Swiss-Prot
-
ACYLT_MYCTO
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
316
0
35160
Swiss-Prot
Secretory Pathway (Reliability: 1)
ACYLT_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
316
0
35126
Swiss-Prot
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
enzyme PatA displays an alpha/beta architecture, with an acyl-binding pocket that runs along the enzyme's core and perpendicular to a long groove that contains the reaction center. The crystal structure provides unique insight into membrane association, acyl-donor recognition and catalysis
additional information
-
enzyme PatA displays an alpha/beta architecture, with an acyl-binding pocket that runs along the enzyme's core and perpendicular to a long groove that contains the reaction center. The crystal structure provides unique insight into membrane association, acyl-donor recognition and catalysis
-
additional information
-
enzyme PatA displays an alpha/beta architecture, with an acyl-binding pocket that runs along the enzyme's core and perpendicular to a long groove that contains the reaction center. The crystal structure provides unique insight into membrane association, acyl-donor recognition and catalysis
-
additional information
enzyme PatA displays an alpha/beta architecture, with an acyl-binding pocket that runs along the enzyme's core and perpendicular to a long groove that contains the reaction center. The crystal structure provides unique insight into membrane association, acyl-donor recognition and catalysis
additional information
-
enzyme PatA displays an alpha/beta architecture, with an acyl-binding pocket that runs along the enzyme's core and perpendicular to a long groove that contains the reaction center. The crystal structure provides unique insight into membrane association, acyl-donor recognition and catalysis
-
additional information
-
enzyme PatA displays an alpha/beta architecture, with an acyl-binding pocket that runs along the enzyme's core and perpendicular to a long groove that contains the reaction center. The crystal structure provides unique insight into membrane association, acyl-donor recognition and catalysis
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, cyrstallization attempts in the presence of Ac1PIM1/Ac2PIM1, Ac1PIM2/Ac2PIM2, or their deacylated analogues are unsuccessful. Crystallization of the enzyme in the presence of mannose phosphate, X-ray diffraction structure detremination and analysis at 2.42 A resolution, molecular replacement method and modelling
using 100mM Tris-HCl pH 7.0, 230 mM MgCl2 and 12-16% (w/v) PEG 8000
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D131A
the mutant shows about 35% activity compared to the wild type enzyme
E149A
the mutant shows about 75% activity compared to the wild type enzyme
E200A
F182W/L197W
the mutant shows less than 3% activity compared to the wild type enzyme
H126A
H284A
the mutant shows about 50% activity compared to the wild type enzyme
R164A
the mutant shows about 78% activity compared to the wild type enzyme
D131A
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
the mutant shows about 35% activity compared to the wild type enzyme
-
E149A
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
the mutant shows about 75% activity compared to the wild type enzyme
-
E200A
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
the mutant shows less than 3% activity compared to the wild type enzyme
-
H126A
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
the mutant shows less than 3% activity compared to the wild type enzyme
-
R164A
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
the mutant shows about 78% activity compared to the wild type enzyme
-
additional information
E200A
the mutant shows less than 3% activity compared to the wild type enzyme
H126A
the mutant shows less than 3% activity compared to the wild type enzyme
additional information
construction of a patA conditional mutant strain TB506.1, silencing of patA is bactericidal in batch cultures. Level of pimA expression remains unaltered in the strain in absence of anhydrotetracycline, while in presence of anhydrotetracycline, pimA is exclusively repressed in mutant strain TB99 and patA is exclusively repressed in TB506.1.The mRNA levels of rv2612c remain constant in strains TB99 and TB506.1. The phenotype is associated with significantly reduced levels of Ac1PIM2, an important structural component of the mycobacterial inner membrane. During macrophage infection and in a mouse model of infection, a dramatic decrease in viable counts is observed upon silencing of the patA gene. Production of PIM is greatly reduced in patA-depleted mycobacteria
additional information
Mycobacterium tuberculosis PatAmtu and Mycobacterium smegmatis PatAmsm share functions in regulating mycobacterial growth, colony surface morphology, and biofilm formation. The cross-complemented strain can compensate for the phenotypic changes in the patA-deleted strain, a transposon insertion mutant strain of Mycolicibacterium smegmatis. Phenotypes, overview. The patA deletion promotes the synthesis of mycolic acids to counteract isoniazid (INH) inhibition of the synthesis of mycolic acids
additional information
-
construction of a patA conditional mutant strain TB506.1, silencing of patA is bactericidal in batch cultures. Level of pimA expression remains unaltered in the strain in absence of anhydrotetracycline, while in presence of anhydrotetracycline, pimA is exclusively repressed in mutant strain TB99 and patA is exclusively repressed in TB506.1.The mRNA levels of rv2612c remain constant in strains TB99 and TB506.1. The phenotype is associated with significantly reduced levels of Ac1PIM2, an important structural component of the mycobacterial inner membrane. During macrophage infection and in a mouse model of infection, a dramatic decrease in viable counts is observed upon silencing of the patA gene. Production of PIM is greatly reduced in patA-depleted mycobacteria
-
additional information
-
Mycobacterium tuberculosis PatAmtu and Mycobacterium smegmatis PatAmsm share functions in regulating mycobacterial growth, colony surface morphology, and biofilm formation. The cross-complemented strain can compensate for the phenotypic changes in the patA-deleted strain, a transposon insertion mutant strain of Mycolicibacterium smegmatis. Phenotypes, overview. The patA deletion promotes the synthesis of mycolic acids to counteract isoniazid (INH) inhibition of the synthesis of mycolic acids
-
additional information
-
construction of a patA conditional mutant strain TB506.1, silencing of patA is bactericidal in batch cultures. Level of pimA expression remains unaltered in the strain in absence of anhydrotetracycline, while in presence of anhydrotetracycline, pimA is exclusively repressed in mutant strain TB99 and patA is exclusively repressed in TB506.1.The mRNA levels of rv2612c remain constant in strains TB99 and TB506.1. The phenotype is associated with significantly reduced levels of Ac1PIM2, an important structural component of the mycobacterial inner membrane. During macrophage infection and in a mouse model of infection, a dramatic decrease in viable counts is observed upon silencing of the patA gene. Production of PIM is greatly reduced in patA-depleted mycobacteria
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additional information
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Mycobacterium tuberculosis PatAmtu and Mycobacterium smegmatis PatAmsm share functions in regulating mycobacterial growth, colony surface morphology, and biofilm formation. The cross-complemented strain can compensate for the phenotypic changes in the patA-deleted strain, a transposon insertion mutant strain of Mycolicibacterium smegmatis. Phenotypes, overview. The patA deletion promotes the synthesis of mycolic acids to counteract isoniazid (INH) inhibition of the synthesis of mycolic acids
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additional information
generation of a transposon insertion mutant strain of Mycolicibacterium smegmatis. The mutant strain displays a smoother surface than the wild-type strain on 7H10 medium plates. The transposon insertion-induced mutation gene is identified as patA by sequencing of the insertion site. The wild-type strain presents a typical wrinkled surface, whereas the patA-deleted strain has a relatively smooth surface and lacks a wrinkled surface. Expression of wild-type patA restores colony morphology. Mycobacterium tuberculosis PatAmtu and Mycobacterium smegmatis PatAmsm share functions in regulating mycobacterial growth, colony surface morphology, and biofilm formation. The cross-complemented strain can compensate for the phenotypic changes in the patA-deleted strain. Phenotypes, overview. The patA deletion promotes the synthesis of mycolic acids to counteract isoniazid (INH) inhibition of the synthesis of mycolic acids
additional information
-
generation of a transposon insertion mutant strain of Mycolicibacterium smegmatis. The mutant strain displays a smoother surface than the wild-type strain on 7H10 medium plates. The transposon insertion-induced mutation gene is identified as patA by sequencing of the insertion site. The wild-type strain presents a typical wrinkled surface, whereas the patA-deleted strain has a relatively smooth surface and lacks a wrinkled surface. Expression of wild-type patA restores colony morphology. Mycobacterium tuberculosis PatAmtu and Mycobacterium smegmatis PatAmsm share functions in regulating mycobacterial growth, colony surface morphology, and biofilm formation. The cross-complemented strain can compensate for the phenotypic changes in the patA-deleted strain. Phenotypes, overview. The patA deletion promotes the synthesis of mycolic acids to counteract isoniazid (INH) inhibition of the synthesis of mycolic acids
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additional information
-
generation of a transposon insertion mutant strain of Mycolicibacterium smegmatis. The mutant strain displays a smoother surface than the wild-type strain on 7H10 medium plates. The transposon insertion-induced mutation gene is identified as patA by sequencing of the insertion site. The wild-type strain presents a typical wrinkled surface, whereas the patA-deleted strain has a relatively smooth surface and lacks a wrinkled surface. Expression of wild-type patA restores colony morphology. Mycobacterium tuberculosis PatAmtu and Mycobacterium smegmatis PatAmsm share functions in regulating mycobacterial growth, colony surface morphology, and biofilm formation. The cross-complemented strain can compensate for the phenotypic changes in the patA-deleted strain. Phenotypes, overview. The patA deletion promotes the synthesis of mycolic acids to counteract isoniazid (INH) inhibition of the synthesis of mycolic acids
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Mycolicibacterium smegmatis strain mc(2)155 by nickel affinity chromatography, dialysis, and gel filtration
TALON Co2+ affinity resin column chromatography, and Superdex 200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)pLysS, Rosetta-gami (DE3)pLysS, and C41(DE3)cells
gene patA or Rv2611c, patA is part of a predicted operon including pimA (rv2610c) and rv2609c, quantitative reverse transcription PCR enzyme expression analysis
gene patA, recombinant expression of His-tagged enzyme in Mycolicibacterium smegmatis strain mc(2)155
gene Rv2611c, the third gene of a cluster of five ORFs potentially organized as a single transcriptional unit and likely to be involved in the synthesis of PIMs
patA, sequence comparisons
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
patA expression is downregulated by anhydrotetracycline
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
drug development
enzyme PatA is a target for drug discovery programs against the major human pathogen, Mycobacterium tuberculosis. The mycobacterial cell envelope, with phosphatidyl-myo-inositol mannosides (PIMs) as key virulence factors and important components of the cell envelope, is a major factor in this intrinsic drug resistance
drug development
the enzyme might be a drug target, e.g. for isoniazid
drug development
the enzyme might be a drug target, e.g. for isoniazid
drug development
-
enzyme PatA is a target for drug discovery programs against the major human pathogen, Mycobacterium tuberculosis. The mycobacterial cell envelope, with phosphatidyl-myo-inositol mannosides (PIMs) as key virulence factors and important components of the cell envelope, is a major factor in this intrinsic drug resistance
-
drug development
-
the enzyme might be a drug target, e.g. for isoniazid
-
drug development
-
the enzyme might be a drug target, e.g. for isoniazid
-
drug development
-
the enzyme might be a drug target, e.g. for isoniazid
-
drug development
-
enzyme PatA is a target for drug discovery programs against the major human pathogen, Mycobacterium tuberculosis. The mycobacterial cell envelope, with phosphatidyl-myo-inositol mannosides (PIMs) as key virulence factors and important components of the cell envelope, is a major factor in this intrinsic drug resistance
-
drug development
-
the enzyme might be a drug target, e.g. for isoniazid
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kordulakova, J.; Gilleron, M.; Puzo, G.; Brennan, P.J.; Gicquel, B.; Mikusova, K.; Jackson, M.
Identification of the required acyltransferase step in the biosynthesis of the phosphatidylinositol mannosides of Mycobacterium species
J. Biol. Chem.
278
36285-36295
2003
Mycobacterium tuberculosis (P9WMB5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WMB5)
brenda
Albesa-Jove, D.; Svetlikova, Z.; Tersa, M.; Sancho-Vaello, E.; Carreras-Gonzalez, A.; Bonnet, P.; Arrasate, P.; Eguskiza, A.; Angala, S.K.; Cifuente, J.O.; Kordulakova, J.; Jackson, M.; Mikusova, K.; Guerin, M.E.
Structural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA
Nat. Commun.
7
10906
2016
Mycolicibacterium smegmatis (A0QWG5), Mycolicibacterium smegmatis, Mycolicibacterium smegmatis mc(2)155 / ATCC 700084 (A0QWG5)
brenda
Svetlikova, Z.; Barath, P.; Jackson, M.; Kordulakova, J.; Mikusova, K.
Purification and characterization of the acyltransferase involved in biosynthesis of the major mycobacterial cell envelope glycolipid-monoacylated phosphatidylinositol dimannoside
Protein Expr. Purif.
100
33-39
2014
Mycolicibacterium smegmatis (A0QWG5), Mycolicibacterium smegmatis mc(2)155 / ATCC 700084 (A0QWG5)
brenda
Tersa, M.; Raich, L.; Albesa-Jove, D.; Trastoy, B.; Prandi, J.; Gilleron, M.; Rovira, C.; Guerin, M.E.
The molecular mechanism of substrate recognition and catalysis of the membrane acyltransferase PatA from Mycobacteria
ACS Chem. Biol.
13
131-140
2018
Mycobacterium tuberculosis (P9WMB5), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 (P9WMB5), Mycobacterium tuberculosis H37Rv (P9WMB5), Mycolicibacterium smegmatis (A0QWG5), Mycolicibacterium smegmatis ATCC 700084 (A0QWG5), Mycolicibacterium smegmatis mc(2)155 (A0QWG5)
brenda
Sancho-Vaello, E.; Albesa-Jove, D.; Rodrigo-Unzueta, A.; Guerin, M.
Structural basis of phosphatidyl-myo-inositol mannosides biosynthesis in mycobacteria
Biochim. Biophys. Acta
1862
1355-1367
2017
Mycobacterium tuberculosis (P9WMB5), Mycobacterium tuberculosis ATCC 25618 (P9WMB5), Mycobacterium tuberculosis H37Rv (P9WMB5), Mycolicibacterium smegmatis (A0QWG5), Mycolicibacterium smegmatis ATCC 700084 (A0QWG5), Mycolicibacterium smegmatis mc(2)155 (A0QWG5)
brenda
Boldrin, F.; Anso, I.; Alebouyeh, S.; Sevilla, I.A.; Geijo, M.; Garrido, J.M.; Marina, A.; Cioetto Mazzabo, L.; Segafreddo, G.; Guerin, M.E.; Manganelli, R.; Prados-Rosales, R.
The phosphatidyl-myo-inositol dimannoside acyltransferase PatA is essential for Mycobacterium tuberculosis growth in vitro and in vivo
J. Bacteriol.
203
e00439-20
2021
Mycobacterium tuberculosis (P9WMB5), Mycobacterium tuberculosis ATCC 25618 (P9WMB5), Mycobacterium tuberculosis H37Rv (P9WMB5)
brenda
Wang, K.; Deng, Y.; Cui, X.; Chen, M.; Ou, Y.; Li, D.; Guo, M.; Li, W.
PatA regulates isoniazid resistance by mediating mycolic acid synthesis and controls biofilm formation by affecting lipid synthesis in mycobacteria
Microbiol. Spectr.
11
e0092823
2023
Mycobacterium tuberculosis (P9WMB5), Mycobacterium tuberculosis ATCC 25618 (P9WMB5), Mycobacterium tuberculosis H37Rv (P9WMB5), Mycolicibacterium smegmatis (A0QWG5), Mycolicibacterium smegmatis ATCC 700084 (A0QWG5), Mycolicibacterium smegmatis mc(2)155 (A0QWG5)
brenda
Anso, I.; Basso, L.G.M.; Wang, L.; Marina, A.; Paez-Perez, E.D.; Jaeger, C.; Gavotto, F.; Tersa, M.; Perrone, S.; Contreras, F.X.; Prandi, J.; Gilleron, M.; Linster, C.L.; Corzana, F.; Lowary, T.L.; Trastoy, B.; Guerin, M.E.
Molecular ruler mechanism and interfacial catalysis of the integral membrane acyltransferase PatA
Sci. Adv.
7
eabj4565
2021
Mycolicibacterium smegmatis (A0QWG5), Mycolicibacterium smegmatis ATCC 700084 (A0QWG5), Mycolicibacterium smegmatis mc(2)155 (A0QWG5)
brenda
EXTERNAL LINKS (specific for EC-Number 2.3.1.265)
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