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EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.265more donor and acceptor binding sites and mechanism, catalytic mechanism, detailed overview Mycolicibacterium smegmatis ? - -
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.265more 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 Mycobacterium tuberculosis ? - -
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.265more 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 Mycolicibacterium smegmatis ? - -
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.265more donor and acceptor binding sites and mechanism, catalytic mechanism, detailed overview Mycolicibacterium smegmatis ATCC 700084 ? - -
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.265more 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 Mycolicibacterium smegmatis ATCC 700084 ? - -
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.265more 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 Mycobacterium tuberculosis H37Rv ? - -
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.265more 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 Mycobacterium tuberculosis ATCC 25618 ? - -
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.265more donor and acceptor binding sites and mechanism, catalytic mechanism, detailed overview Mycolicibacterium smegmatis mc(2)155 ? - -
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.265more 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 Mycolicibacterium smegmatis mc(2)155 ? - -
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.265palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol - Mycobacterium tuberculosis CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol - ?
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