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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
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
additional information
?
-
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 + 2,6-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 + 2,6-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 + 2,6-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 + 2,6-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 + 2,6-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 + 2,6-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
-
-
?
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 + 2,6-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 + 2,6-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 + 2,6-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
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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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-
-
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
?
-
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
?
-
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
-
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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 + 2,6-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 + 2,6-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 + 2,6-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 + 2,6-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 + 2,6-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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
-
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
-
malfunction
disruption of gene MSMEG_2934 severely affects the groth of Mycobacterium smegmatis
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
-
disruption of gene Rv2611c abolishes the growth of Mycobacterium tuberculosis
-
malfunction
-
disruption of gene Rv2611c abolishes the growth of Mycobacterium tuberculosis
-
malfunction
-
disruption of gene MSMEG_2934 severely affects the groth of Mycobacterium smegmatis
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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
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, 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, 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, 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, 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
-
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
-
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
-
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
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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
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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
-
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
-
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
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E200A
site-directed mutagenesis, inactive enzyme mutant
H126A
site-directed mutagenesis, inactive enzyme mutant
E200A
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site-directed mutagenesis, inactive enzyme mutant
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H126A
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site-directed mutagenesis, inactive enzyme mutant
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E200A
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site-directed mutagenesis, inactive enzyme mutant
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H126A
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site-directed mutagenesis, inactive enzyme mutant
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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
F182W/L197W
the mutant shows less than 3% activity compared to the wild type enzyme
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
E200A
-
site-directed mutagenesis, inactive enzyme mutant
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H126A
-
site-directed mutagenesis, inactive enzyme mutant
-
E200A
-
site-directed mutagenesis, inactive enzyme mutant
-
H126A
-
site-directed mutagenesis, inactive enzyme mutant
-
E149A
-
the mutant shows about 75% activity compared to the wild type enzyme
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E200A
-
the mutant shows less than 3% activity compared to the wild type enzyme
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H126A
-
the mutant shows less than 3% activity compared to the wild type enzyme
-
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
-
E200A
the mutant shows less than 3% activity compared to the wild type enzyme
E200A
site-directed mutagenesis, inactive enzyme mutant
H126A
the mutant shows less than 3% activity compared to the wild type enzyme
H126A
site-directed mutagenesis, inactive enzyme mutant
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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
Mycolicibacterium smegmatis (A0QWG5), Mycobacterium tuberculosis (P9WMB5), Mycobacterium tuberculosis, Mycolicibacterium smegmatis ATCC 700084 (A0QWG5), Mycobacterium tuberculosis H37Rv (P9WMB5), Mycobacterium tuberculosis ATCC 25618 (P9WMB5), 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
Mycolicibacterium smegmatis (A0QWG5), Mycobacterium tuberculosis (P9WMB5), Mycolicibacterium smegmatis ATCC 700084 (A0QWG5), Mycobacterium tuberculosis H37Rv (P9WMB5), Mycobacterium tuberculosis ATCC 25618 (P9WMB5), Mycolicibacterium smegmatis mc(2)155 (A0QWG5)
brenda