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Literature summary for 2.7.2.3 extracted from

  • Noel, N.; Flanagan, J.M.; Flanagan, J.; Ramirez Bajo, M.J.; Kalko, S.G.; Manu, M.d.e.l.M.; Garcia Fuster, J.L.; Perez de la Ossa, P.; Carreras, J.; Beutler, E.; Vives Corrons, J.L.
    Two new phosphoglycerate kinase mutations associated with chronic haemolytic anaemia and neurological dysfunction in two patients from Spain (2006), Br. J. Haematol., 132, 523-529.
    View publication on PubMed

Application

Application Comment Organism
medicine two missense mutations in patients of Spanish origin with a severe life-long chronic haemolytic anaemia associated with progressive neurological impairment. One patient with an amino acid change of Ile to Asn at 46th position from the NH2-terminal serine residue, the second patient with a Ser319Asn amino acid substitution. In both cases, the mutations do not modify any of the PGK binding sites for ATP or 3-phospho-D-glycerate, so their consequence is related to a loss of enzyme stability rather than a decrease of enzyme catalytic function Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P00558
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-

Source Tissue

Source Tissue Comment Organism Textmining
blood
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Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 3-phospho-D-glycerate
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Homo sapiens ADP + 1,3-diphosphoglycerate
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?

Synonyms

Synonyms Comment Organism
PGK1
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Homo sapiens