Premium
The reduction‐oxidation status may influence the degradation of glyceraldehyde‐3‐phosphate dehydrogenase
Author(s) -
Knecht Erwin,
Roche Enrique
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)81008-0
Subject(s) - glyceraldehyde 3 phosphate dehydrogenase , proteolysis , dehydrogenase , proteases , biochemistry , nad+ kinase , chemistry , elastase , intracellular , glyceraldehyde , degradation (telecommunications) , enzyme , telecommunications , computer science
NADH and NADPH accelerate the ‘in vitro’ rate of proteolysis of glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH) by elastase and other proteases, including lysosomal proteases. NAD + and NADP + have the opposite effect. Since there is a good correlation between proteolytic susceptibility of proteins and their ‘in vivo’ degradation rates, a possible role of the reduction‐oxidation status in controlling the intracellular degradation of GAPDH is advanced.