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Literature summary extracted from

  • Pomel, S.; Rodrigo, J.; Hendra, F.; Cave, C.; Loiseau, P.M.
    In silico analysis of a therapeutic target in Leishmania infantum: the guanosine-diphospho-D-mannose pyrophosphorylase (2012), Parasite, 19, 63-70.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
2.7.7.13 drug development the enzyme is a target for inhibitor design for anti-leishmanial therapy Leishmania infantum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.7.13 cytosol
-
 Leishmania infantum 5829
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.13 GTP + alpha-D-mannose 1-phosphate Leishmania infantum
-
 diphosphate + GDP-mannose
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.13 Leishmania infantum A4I048 clone JPCM5 (MCAN/ES/98/LLM-877)
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.13 GTP + alpha-D-mannose 1-phosphate
-
 Leishmania infantum diphosphate + GDP-mannose
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.7.13 GDP-MP
-
 Leishmania infantum
2.7.7.13 guanosine-diphospho-D-mannose pyrophosphorylase
-
 Leishmania infantum

General Information

EC Number General Information Comment Organism
2.7.7.13 metabolism the enzyme catalyzes a step in the mannose activation pathways and glycoconjugate biosynthesis in Leishmania, overview Leishmania infantum
2.7.7.13 additional information a common motif of amino acids binds to the mannose moiety of the substrate and is specific to the catalytic site of the parasite enzyme, molecular dynamics and homology modeling, overview. Sequence comparison to the human enzyme Leishmania infantum
2.7.7.13 physiological function the GDP-mannose pyrophosphorylase is involved in glycosylation and essential for amastigote survival Leishmania infantum