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- Name help_outline a 1,2-diacyl-sn-glycero-3-phospho-[α-D-mannopyranosyl-(1↔6)-D-myo-inositol] Identifier CHEBI:87673 Charge -1 Formula C17H26O18PR2 SMILEShelp_outline O=P([O-])(O[C@@H]1[C@@H]([C@@H]([C@H]([C@@H]([C@H]1O)O)O)O)O[C@@H]2[C@H]([C@H]([C@@H]([C@H](O2)CO)O)O)O)OC[C@@H](COC(*)=O)OC(*)=O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline GDP-α-D-mannose Identifier CHEBI:57527 (Beilstein: 6630718) help_outline Charge -2 Formula C16H23N5O16P2 InChIKeyhelp_outline MVMSCBBUIHUTGJ-GDJBGNAASA-L SMILEShelp_outline Nc1nc2n(cnc2c(=O)[nH]1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)O[C@H]2O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]2O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 52 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a 2,6-O-bis(α-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol Identifier CHEBI:136624 Charge -1 Formula C23H36O23PR2 SMILEShelp_outline [C@@H]1([C@@H]([C@@H]([C@@H]([C@H]([C@@H]1O)O)O)O[C@@H]2[C@H]([C@H]([C@@H]([C@H](O2)CO)O)O)O)OP(OC[C@@H](COC(=O)*)OC(=O)*)(=O)[O-])O[C@@H]3[C@H]([C@H]([C@@H]([C@H](O3)CO)O)O)O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline GDP Identifier CHEBI:58189 Charge -3 Formula C10H12N5O11P2 InChIKeyhelp_outline QGWNDRXFNXRZMB-UUOKFMHZSA-K SMILEShelp_outline Nc1nc2n(cnc2c(=O)[nH]1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 169 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:52440 | RHEA:52441 | RHEA:52442 | RHEA:52443 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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| EC numbers help_outline |
Publications
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New insights into the early steps of phosphatidylinositol mannoside biosynthesis in mycobacteria: PimB' is an essential enzyme of Mycobacterium smegmatis.
Guerin M.E., Kaur D., Somashekar B.S., Gibbs S., Gest P., Chatterjee D., Brennan P.J., Jackson M.
Phosphatidyl-myo-inositol mannosides (PIMs) are key glycolipids of the mycobacterial cell envelope. They are considered not only essential structural components of the cell but also important molecules implicated in host-pathogen interactions. Although their chemical structures are well establishe ... >> More
Phosphatidyl-myo-inositol mannosides (PIMs) are key glycolipids of the mycobacterial cell envelope. They are considered not only essential structural components of the cell but also important molecules implicated in host-pathogen interactions. Although their chemical structures are well established, knowledge of the enzymes and sequential events leading to their biosynthesis is still incomplete. Here we show for the first time that although both mannosyltransferases PimA and PimB' (MSMEG_4253) recognize phosphatidyl-myo-inositol (PI) as a lipid acceptor, PimA specifically catalyzes the transfer of a Manp residue to the 2-position of the myo-inositol ring of PI, whereas PimB' exclusively transfers to the 6-position. Moreover, whereas PimB' can catalyze the transfer of a Manp residue onto the PI-monomannoside (PIM1) product of PimA, PimA is unable in vitro to transfer Manp onto the PIM1 product of PimB'. Further assays using membranes from Mycobacterium smegmatis and purified PimA and PimB' indicated that the acylation of the Manp residue transferred by PimA preferentially occurs after the second Manp residue has been added by PimB'. Importantly, genetic evidence is provided that pimB' is an essential gene of M. smegmatis. Altogether, our results support a model wherein Ac1PIM2, a major form of PIMs produced by mycobacteria, arises from the consecutive action of PimA, followed by PimB', and finally the acyltransferase MSMEG_2934. The essentiality of these three enzymes emphasizes the interest of novel anti-tuberculosis drugs targeting the initial steps of PIM biosynthesis. << Less
J. Biol. Chem. 284:25687-25696(2009) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Characterization of the Corynebacterium glutamicum deltapimB' deltamgtA double deletion mutant and the role of Mycobacterium tuberculosis orthologues Rv2188c and Rv0557 in glycolipid biosynthesis.
Mishra A.K., Batt S., Krumbach K., Eggeling L., Besra G.S.
In this study, utilizing a Corynebacterium glutamicum DeltapimB' DeltamgtA double deletion mutant, we unequivocally assign the in vivo functions of Rv2188c as an Ac(1)PIM(1):mannosyltransferase (originally termed PimB'(Mt) [Mycobacterium tuberculosis PimB']) and Rv0557 as a GlcAGroAc(2):mannosyltr ... >> More
In this study, utilizing a Corynebacterium glutamicum DeltapimB' DeltamgtA double deletion mutant, we unequivocally assign the in vivo functions of Rv2188c as an Ac(1)PIM(1):mannosyltransferase (originally termed PimB'(Mt) [Mycobacterium tuberculosis PimB']) and Rv0557 as a GlcAGroAc(2):mannosyltransferase (originally termed PimB(Mt)), which we have reassigned as PimB(Mt) and MgtA(Mt), respectively, in Mycobacterium tuberculosis. << Less
J. Bacteriol. 191:4465-4472(2009) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Acceptor substrate discrimination in phosphatidyl-myo-inositol mannoside synthesis: structural and mutational analysis of mannosyltransferase Corynebacterium glutamicum PimB'.
Batt S.M., Jabeen T., Mishra A.K., Veerapen N., Krumbach K., Eggeling L., Besra G.S., Futterer K.
Long term survival of the pathogen Mycobacterium tuberculosis in humans is linked to the immunomodulatory potential of its complex cell wall glycolipids, which include the phosphatidylinositol mannoside (PIM) series as well as the related lipomannan and lipoarabinomannan glycoconjugates. PIM biosy ... >> More
Long term survival of the pathogen Mycobacterium tuberculosis in humans is linked to the immunomodulatory potential of its complex cell wall glycolipids, which include the phosphatidylinositol mannoside (PIM) series as well as the related lipomannan and lipoarabinomannan glycoconjugates. PIM biosynthesis is initiated by a set of cytosolic α-mannosyltransferases, catalyzing glycosyl transfer from the activated saccharide donor GDP-α-D-mannopyranose to the acceptor phosphatidyl-myo-inositol (PI) in an ordered and regio-specific fashion. Herein, we report the crystal structure of mannosyltransferase Corynebacterium glutamicum PimB' in complex with nucleotide to a resolution of 2.0 Å. PimB' attaches mannosyl selectively to the 6-OH of the inositol moiety of PI. Two crystal forms and GDP-versus GDP-α-d-mannopyranose-bound complexes reveal flexibility of the nucleotide conformation as well as of the structural framework of the active site. Structural comparison, docking of the saccharide acceptor, and site-directed mutagenesis pin regio-selectivity to a conserved Asp residue in the N-terminal domain that forces presentation of the correct inositol hydroxyl to the saccharide donor. << Less
J. Biol. Chem. 285:37741-37752(2010) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.