In:
Parasitology, Cambridge University Press (CUP), Vol. 140, No. 7 ( 2013-06), p. 897-906
Abstract:
Glucose-6-phosphate dehydrogenase (G6PD), a regulatory enzyme of the pentose phosphate pathway from Brugia malayi , was cloned, expressed and biochemically characterized. The Km values for glucose-6-phosphate and nicotinamide adenine dinucleotide phosphate (NADP) were 0·25 and 0·014 m m respectively. The rBmG6PD exhibited an optimum pH of 8·5 and temperature, 40 °C. Adenosine 5′ [ γ -thio] triphosphate (ATP- γ -S), adenosine 5′ [ β , γ -imido] triphosphate (ATP- β , γ -NH), adenosine 5′ [ β -thio] diphosphate (ADP- β -S), Na + , K + , Li + and Cu ++ ions were found to be strong inhibitors of rBmG6PD. The rBmG6PD, a tetramer with subunit molecular weight of 75 kDa contains 0·02 mol of SH group per mol of monomer. Blocking the SH group with SH-inhibitors, led to activation of rBmG6PD activity by N -ethylmaleimide. CD analysis indicated that rBmG6PD is composed of 37% α -helices and 26% β -sheets. The unfolding equilibrium of rBmG6PD with GdmCl/urea showed the triphasic unfolding pattern along with the highly stable intermediate obtained by GdmCl.
Type of Medium:
Online Resource
ISSN:
0031-1820
,
1469-8161
DOI:
10.1017/S0031182013000115
Language:
English
Publisher:
Cambridge University Press (CUP)
Publication Date:
2013
detail.hit.zdb_id:
1491287-9
SSG:
12
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