TY - JOUR
T1 - Does sorbinil bind to the substrate binding site of aldose reductase?
AU - Liu, Si Qi
AU - Bhatnagar, Aruni
AU - Srivastava, Satish K.
N1 - Funding Information:
Acknowledgements--This work was supported in part by NIH Grants DK 36118 and EY 01677.
PY - 1992/12/15
Y1 - 1992/12/15
N2 - With benzyl alcohol as the varied substrate, sorbinil was found to be a competitive inhibitor of aldose reductase, an enzyme implicated in the etiology of secondary diabetic complications. The Kissorbinil and the Vmax/Km (V/K) benzyl alcohol decreased at low pH with a pk of 7.5 and 7.7, respectively. These observations suggest that both sorbinil and benzyl alcohol bind to the same site on the enzyme. Active site inhibition by sorbinil is consistent with non-competitive inhibition patterns of sorbinil with nucleotide coenzyme or aldehyde as the varied substrate in the direction of aldehyde reduction.
AB - With benzyl alcohol as the varied substrate, sorbinil was found to be a competitive inhibitor of aldose reductase, an enzyme implicated in the etiology of secondary diabetic complications. The Kissorbinil and the Vmax/Km (V/K) benzyl alcohol decreased at low pH with a pk of 7.5 and 7.7, respectively. These observations suggest that both sorbinil and benzyl alcohol bind to the same site on the enzyme. Active site inhibition by sorbinil is consistent with non-competitive inhibition patterns of sorbinil with nucleotide coenzyme or aldehyde as the varied substrate in the direction of aldehyde reduction.
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U2 - 10.1016/0006-2952(92)90693-D
DO - 10.1016/0006-2952(92)90693-D
M3 - Article
C2 - 1472112
AN - SCOPUS:0026677840
SN - 0006-2952
VL - 44
SP - 2427
EP - 2429
JO - Biochemical Pharmacology
JF - Biochemical Pharmacology
IS - 12
ER -