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Literature summary for 2.7.7.13 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

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

Localization

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Substrates and Products (Substrate)

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

Synonyms

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

General Information

General Information Comment Organism
metabolism the enzyme catalyzes a step in the mannose activation pathways and glycoconjugate biosynthesis in Leishmania, overview Leishmania infantum
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
physiological function the GDP-mannose pyrophosphorylase is involved in glycosylation and essential for amastigote survival Leishmania infantum