EC 2.4.1.345 - Phosphatidyl-myo-inositol α-mannosyltransferase

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IntEnz Enzyme Nomenclature
EC 2.4.1.345

Names

Accepted name:
phosphatidyl-myo-inositol α-mannosyltransferase
Other names:
mannosyltransferase PimA
PimA
guanosine diphosphomannose-phosphatidyl-inositol α-mannosyltransferase [ambiguous]
Systematic name:
GDP-α-D-mannose:1-phosphatidyl-1D-myo-inositol 2-α-D-mannosyltransferase (configuration-retaining)

Reaction

Cofactor

Comments:

Requires Mg2+. The enzyme, found in Corynebacteriales, is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIMs).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0043750
UniProtKB/Swiss-Prot:

References

  1. Kordulakova, J., Gilleron, M., Mikusova, K., Puzo, G., Brennan, P. J., Gicquel, B., Jackson, M.
    Definition of the first mannosylation step in phosphatidylinositol mannoside synthesis. PimA is essential for growth of mycobacteria.
    J. Biol. Chem. 277 : 31335-31344 (2002). [PMID: 12068013]
  2. Gu, X., Chen, M., Wang, Q., Zhang, M., Wang, B., Wang, H.
    Expression and purification of a functionally active recombinant GDP-mannosyltransferase (PimA) from Mycobacterium tuberculosis H37Rv.
    Protein Expr. Purif. 42 : 47-53 (2005). [PMID: 15939292]
  3. Giganti, D., Albesa-Jove, D., Urresti, S., Rodrigo-Unzueta, A., Martinez, M. A., Comino, N., Barilone, N., Bellinzoni, M., Chenal, A., Guerin, M. E., Alzari, P. M.
    Secondary structure reshuffling modulates glycosyltransferase function at the membrane.
    Nat. Chem. Biol. 11 : 16-18 (2015). [PMID: 25402770]
  4. Rodrigo-Unzueta, A., Martinez, M. A., Comino, N., Alzari, P. M., Chenal, A., Guerin, M. E.
    Molecular Basis of Membrane Association by the Phosphatidylinositol Mannosyltransferase PimA Enzyme from Mycobacteria.
    J. Biol. Chem. 291 : 13955-13963 (2016). [PMID: 27189944]

[EC 2.4.1.345 created 2017]