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Literature summary for 1.1.1.363 extracted from

  • Cosgrove, M.S.; Gover, S.; Naylor, C.E.; Vandeputte-Rutten, L.; Adams, M.J.; Levy, H.R.
    An examination of the role of asp-177 in the His-Asp catalytic dyad of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: X-ray structure and pH dependence of kinetic parameters of the D177N mutant enzyme (2000), Biochemistry, 39, 15002-15011.
    View publication on PubMed
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Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion technique, determination of the three-dimensional structure of the D177N mutant enzyme by X-ray cryocrystallography in the presence of NAD+ and in the presence of glucose 6-phosphate plus NADPH. The structure of a glucose 6-phosphate complex of a mutant (Q365C) with normal enzyme activity is also determined and substrate binding compared Leuconostoc mesenteroides

Protein Variants

Protein Variants Comment Organism
D177N absence of a negatively charged aspartate at 177 accounts for the decrease in catalytic activity at pH 7.8 Leuconostoc mesenteroides

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
54000
-
 2 * 54000 Leuconostoc mesenteroides

Organism

Organism UniProt Comment Textmining
Leuconostoc mesenteroides P11411
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Leuconostoc mesenteroides

Subunits

Subunits Comment Organism
homodimer 2 * 54000 Leuconostoc mesenteroides

Synonyms

Synonyms Comment Organism
G6PD
-
 Leuconostoc mesenteroides

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
 log-log plots of the dependence of kcat and kcat/Km on pH for both D177N and wild-type enzyme. The kcat profile for mutant enzyme D177N shows a nearly linear increase from pH 5 until wild-type-like activity is regained at pH 10. Above pH 10 the kcat decreases precipitously. Linear regression of the data in the pH range 5-10 produces a slope of 0.9 Leuconostoc mesenteroides