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Evidence for the presence of a critical histidine residue at the active site in glyceraldehyde-3-phosphate dehydrogenase of Ehrlich ascites carcinoma cells

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Title Evidence for the presence of a critical histidine residue at the active site in glyceraldehyde-3-phosphate dehydrogenase of Ehrlich ascites carcinoma cells
 
Creator Ghosh, Swapna
Ray, Manju
Ray, Subhankar
 
Subject Glyceraldehyde-3-phosphate dehydrogenase
Ehrlich ascites carcinoma cell
Active site histidine
Diethyl pyrocarbonate (DEPC)
Inactivation
 
Description 7-13
Ehrlich ascites carcinoma (EAC) cell glyceraldehyde-3-phosphate dehydrogenase (GA3PD) (EC. 1.2.1.12) was completely inactivated by diethyl pyrocarbonate (DEPC), a fairly specific reagent for histidine residues in the pH range of 6.0-7.5. The rate of inactivation was dependent on pH and followed pseudo-first order reaction kinetics. The difference spectrum of the inactivated and native enzymes showed an increase in the absorption maximum at 242 nm, indicating the modification of histidine residues. Statistical analysis of the residual enzyme activity and the extent of modification indicated modification of one essential histidine residue to be responsible for loss of the catalytic activity of EAC cell GA3PD. DEPC inactivation was protected by substrates, D-glyceraldehyde-3-phosphate and NAD, indicating the presence of essential histidine residue at the substrate-binding region of the active site. Double inhibition studies also provide evidence for the presence of histidine residue at the active site.
 
Date 2009-03-31T06:08:56Z
2009-03-31T06:08:56Z
2004-02
 
Type Article
 
Identifier 0301-1208
http://hdl.handle.net/123456789/3635
 
Language en_US
 
Publisher CSIR
 
Source IJBB Vol. 41(1) [February 2004]