Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/12939
Title: Enzyme kinetics and molecular modeling studies of G6PDMahidol associated with acute hemolytic anemia
Authors: Lu, Hui-Ru
Tang, Qiong-Ling
Wang, Xin
Li, Hong-Jun
Yang, Yin-Feng
Li, Dan-Yi
Tong, Shu-Fen
Zhang, Chun-Hua
Zhu, Yue-Chun
Keywords: G6PD
Achang people
Acute hemolytic anemia
Enzyme kinetics
Crystal structure
Issue Date: Oct-2011
Publisher: NISCAIR-CSIR, India
Abstract: G6PDMahidol enzyme is the most common variant in the Achang Chinese ethnic group and clinically manifests as class II. In this study, G6PDMahidol enzyme was characterized by molecular modeling to understand its kinetics. G6PDMahidol, G6PDG487A and G6PDWT proteins were heterologously expressed in the G6PD-deficient DF213 E. coli strain, purified and their steady-state kinetic parameters were determined. Compared with G6PDWT, the Km and Vmax of NADP+ with G6PDG487A were about 28-fold and 12-fold lower, respectively. The Ki values of dehydroepiandrosterone (DHEA), NADPH and ATP with G6PDG487A showed 29.5-fold, 2.36-fold reduction and 1.83-fold increase, respectively. A molecular modeling of G6PDG487A was performed based on the X-ray structure of human G6PD (PDB: 2BH9). It is suggested that Ser-163 might affect the stability of G6PDG487A -helix d and -strand E, besides the conformation of -strand D. In conclusion, the biochemical and structural properties of G6PDG487A and G6PDWT enzymes are significantly different, which may be responsible for clinical diversity of G6PD deficiencies.
Description: 316-324
URI: http://hdl.handle.net/123456789/12939
ISSN: 0975-0959 (Online); 0301-1208 (Print)
Appears in Collections:IJBB Vol.48(5) [October 2011]

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