Purification and characterization of phosphoglycerate kinase from Fasciola hepatica
Phosphoglycerate kinase (EC 2.7.2.3) of Fasciola hepatica was purified 375-fold to homogeneity. The enzyme was monomeric, and had a molecular weight of 47 900 and a sedimentation coefficient of 3.0–3.5 S. The enzyme was composed of 397 amino acids and was relatively rich in sulfur amino acids contai...
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Veröffentlicht in: | Molecular and biochemical parasitology 1981-01, Vol.2 (5), p.309-321 |
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Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Phosphoglycerate kinase (EC 2.7.2.3) of
Fasciola hepatica was purified 375-fold to homogeneity. The enzyme was monomeric, and had a molecular weight of 47 900 and a sedimentation coefficient of 3.0–3.5 S. The enzyme was composed of 397 amino acids and was relatively rich in sulfur amino acids containing 13 methionine and 2 cysteine residues per mole. The enzyme possessed a highly reactive essential sulfhydryl group and was inhibited irreversibly by iodoacetamide and
N-ethyl-maleimide and reversibly by
p-chloromercuribenzoate and 5,5′-dithio-bis(2-nitrobenzoic acid). Initial velocity studies suggested that reaction occurred via a sequential mechanism. The
K
m values for 3-phosphoglycerate and ATP were 1.26 and 0.90 mM, respectively. ADP was a noncompetitive inhibitor with respect to both ATP and 3-phosphoglycerate. |
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ISSN: | 0166-6851 1872-9428 |
DOI: | 10.1016/0166-6851(81)90083-9 |