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Enzyme kinetics and molecular modeling studies of G6PD<sub>Mahidol</sub> associated with acute hemolytic anemia

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Title Enzyme kinetics and molecular modeling studies of G6PDMahidol associated with acute hemolytic anemia
 
Creator 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
 
Subject G6PD
Achang people
Acute hemolytic anemia
Enzyme kinetics
Crystal structure
 
Description 316-324
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.
 
Date 2011-10-21T11:01:25Z
2011-10-21T11:01:25Z
2011-10
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/12939
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.48(5) [October 2011]