Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • 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 (2018), ACS Chem. Biol., 13, 131-140 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.265 gene MSMEG_2934, recombinant enzyme expression Mycolicibacterium smegmatis
2.3.1.265 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 Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.265 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 Mycolicibacterium smegmatis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.265 additional information inhibition mechanism analysis, overview Mycobacterium tuberculosis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.265 membrane
-
 Mycobacterium tuberculosis 16020
-
2.3.1.265 membrane
-
 Mycolicibacterium smegmatis 16020
-
2.3.1.265 additional information the enzyme has a large negatively charged cytoplasmic part, overview Mycobacterium tuberculosis
-
-
2.3.1.265 additional information the enzyme has a large negatively charged cytoplasmic part, overview Mycolicibacterium smegmatis
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.265 palmitoyl-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
-
 ?
2.3.1.265 palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol Mycolicibacterium smegmatis
-
 CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
 ?
2.3.1.265 palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol Mycolicibacterium smegmatis ATCC 700084
-
 CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
 ?
2.3.1.265 palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol Mycobacterium tuberculosis H37Rv
-
 CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
 ?
2.3.1.265 palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol Mycobacterium tuberculosis ATCC 25618
-
 CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
 ?
2.3.1.265 palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol Mycolicibacterium smegmatis mc(2)155
-
 CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
 ?
2.3.1.265 palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol Mycobacterium tuberculosis
-
 CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
-
 ?
2.3.1.265 palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol Mycolicibacterium smegmatis
-
 CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
-
 ?
2.3.1.265 palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol Mycolicibacterium smegmatis ATCC 700084
-
 CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
-
 ?
2.3.1.265 palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol Mycobacterium tuberculosis H37Rv
-
 CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
-
 ?
2.3.1.265 palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol Mycobacterium tuberculosis ATCC 25618
-
 CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
-
 ?
2.3.1.265 palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol Mycolicibacterium smegmatis mc(2)155
-
 CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.265 Mycobacterium tuberculosis P9WMB5
-
-
2.3.1.265 Mycobacterium tuberculosis ATCC 25618 P9WMB5
-
-
2.3.1.265 Mycobacterium tuberculosis H37Rv P9WMB5
-
-
2.3.1.265 Mycolicibacterium smegmatis A0QWG5 i.e. Mycobacterium smegmatis
-
2.3.1.265 Mycolicibacterium smegmatis ATCC 700084 A0QWG5 i.e. Mycobacterium smegmatis
-
2.3.1.265 Mycolicibacterium smegmatis mc(2)155 A0QWG5 i.e. Mycobacterium smegmatis
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.265 recombinant enzyme Mycolicibacterium smegmatis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.265 additional information donor and acceptor binding sites and mechanism, catalytic mechanism, detailed overview Mycolicibacterium smegmatis ?
-
-
2.3.1.265 additional information donor and acceptor binding sites and mechanism, catalytic mechanism, detailed overview Mycolicibacterium smegmatis ATCC 700084 ?
-
-
2.3.1.265 additional information donor and acceptor binding sites and mechanism, catalytic mechanism, detailed overview Mycolicibacterium smegmatis mc(2)155 ?
-
-
2.3.1.265 palmitoyl-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
-
 ?
2.3.1.265 palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
 Mycolicibacterium smegmatis CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
 ?
2.3.1.265 palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
 Mycolicibacterium smegmatis ATCC 700084 CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
 ?
2.3.1.265 palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
 Mycobacterium tuberculosis H37Rv CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
 ?
2.3.1.265 palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
 Mycobacterium tuberculosis ATCC 25618 CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
 ?
2.3.1.265 palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
 Mycolicibacterium smegmatis mc(2)155 CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
 ?
2.3.1.265 palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
 Mycobacterium tuberculosis CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
-
 ?
2.3.1.265 palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
 Mycolicibacterium smegmatis CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
-
 ?
2.3.1.265 palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
 Mycolicibacterium smegmatis ATCC 700084 CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
-
 ?
2.3.1.265 palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
 Mycobacterium tuberculosis H37Rv CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
-
 ?
2.3.1.265 palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
 Mycobacterium tuberculosis ATCC 25618 CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
-
 ?
2.3.1.265 palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
 Mycolicibacterium smegmatis mc(2)155 CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.265 membrane acyltransferase
-
 Mycobacterium tuberculosis
2.3.1.265 membrane acyltransferase
-
 Mycolicibacterium smegmatis
2.3.1.265 MSMEG_2934
-
 Mycolicibacterium smegmatis
2.3.1.265 PatA ambiguous Mycobacterium tuberculosis
2.3.1.265 PatA ambiguous Mycolicibacterium smegmatis
2.3.1.265 phosphatidylinositol mannoside acyltransferase UniProt Mycobacterium tuberculosis
2.3.1.265 phosphatidylinositol mannoside acyltransferase UniProt Mycolicibacterium smegmatis
2.3.1.265 PIM acyltransferase UniProt Mycobacterium tuberculosis
2.3.1.265 PIM acyltransferase UniProt Mycolicibacterium smegmatis
2.3.1.265 Rv2611c
-
 Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
2.3.1.265 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 Mycobacterium tuberculosis
2.3.1.265 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 Mycolicibacterium smegmatis
2.3.1.265 metabolism the enzyme is part of the PIM biosynthetic pathway in mycobacteria, overview Mycobacterium tuberculosis
2.3.1.265 metabolism the enzyme is part of the PIM biosynthetic pathway in mycobacteria, overview Mycolicibacterium smegmatis
2.3.1.265 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 Mycobacterium tuberculosis
2.3.1.265 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 Mycolicibacterium smegmatis