2.3.1.265: phosphatidylinositol dimannoside acyltransferase
This is an abbreviated version!
For detailed information about phosphatidylinositol dimannoside acyltransferase, go to the full flat file.
Word Map on EC 2.3.1.265
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2.3.1.265
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mannosides
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mycobacterial
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6-position
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glycolipids
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phosphatidyl-myo-inositol
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phospholipid
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palmitoyl
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mannose
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lipomannan
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host-pathogen
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lipoarabinomannan
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envelope
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smegmatis
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palmitoyl-coa
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mannosyltransferases
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palmitate
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transacylase
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lipoglycans
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fluidity
- 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
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mannosyltransferases
- palmitate
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transacylase
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lipoglycans
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fluidity
Reaction
Synonyms
acyltransferase PatA, membrane acyltransferase, MSMEG 2934 protein, MSMEG_2934, PatA, phosphatidylinositol mannoside acyltransferase, PIM acyltransferase, PIM2 acyltransferase, ptfP1, Rv2611c
ECTree
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Substrates Products
Substrates Products on EC 2.3.1.265 - phosphatidylinositol dimannoside acyltransferase
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REACTION DIAGRAM
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
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
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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
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-
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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
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-
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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
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-
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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
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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
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-
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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
preferred substrate
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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
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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
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-
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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
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
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-
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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
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
preferred substrate
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-
?
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
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-
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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
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-
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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
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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
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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
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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
-
-
-
?
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
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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
-
-
-
?
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
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?
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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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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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-
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additional information
?
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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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donor and acceptor binding sites and mechanism, catalytic mechanism, detailed overview
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-
-
additional information
?
-
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
-
-
-
additional information
?
-
donor and acceptor binding sites and mechanism, catalytic mechanism, detailed overview
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
donor and acceptor binding sites and mechanism, catalytic mechanism, detailed overview
-
-
-
additional information
?
-
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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