Literature summary for 2.7.7.13 extracted from

Daligaux, P.; Bernadat, G.; Tran, L.; Cave, C.; Loiseau, P.; Pomel, S.; Ha-Duong, T.
Comparative study of structural models of Leishmania donovani and human GDP-mannose pyrophosphorylases (2016), Eur. J. Med. Chem., 107, 109-118.

Crystallization (Commentary)

Crystallization (Comment)	Organism
comparison of structural models of the GDP-mannose diphosphorylases from human and Leishmania donovani. Residues Leu14, Val15, Ala60, Leu92 and Pro97 surround the hydrophobic bicycle of the nucleotide, while the amine groups of the latter interact with Glu88. The ribose ring belonging to the substrate is bound to protein residues Asn116 and Ser117. The magnesium ion is chelated by Asp118 and Asp226, and the diphosphate group makes electrostatic interactions with residues Arg21 and Lys31, which belong to the GGXGXRLXPLX5PK diphosphorylase signature	Leishmania donovani
comparison of structural models of the GDP-mannose diphosphorylases from human and Leishmania donovani. The human active site is site very similar to the Leishmania donovani one. Leishmania donovani GDP-mannose diphosphorylase makes more interactions with its substrate than the human enzyme does	Homo sapiens

Crystallization (Comment)

Organism

comparison of structural models of the GDP-mannose diphosphorylases from human and Leishmania donovani. Residues Leu14, Val15, Ala60, Leu92 and Pro97 surround the hydrophobic bicycle of the nucleotide, while the amine groups of the latter interact with Glu88. The ribose ring belonging to the substrate is bound to protein residues Asn116 and Ser117. The magnesium ion is chelated by Asp118 and Asp226, and the diphosphate group makes electrostatic interactions with residues Arg21 and Lys31, which belong to the GGXGXRLXPLX5PK diphosphorylase signature

Leishmania donovani

comparison of structural models of the GDP-mannose diphosphorylases from human and Leishmania donovani. The human active site is site very similar to the Leishmania donovani one. Leishmania donovani GDP-mannose diphosphorylase makes more interactions with its substrate than the human enzyme does

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9Y5P6	-	-
Leishmania donovani	E9BG32	-	-
Leishmania donovani BPK282A1	E9BG32	-	-

Synonyms

Synonyms	Comment	Organism
GMPPB	-	Homo sapiens
LDBPK_230120	-	Leishmania donovani

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Release 2023.1 (January 2023)