Does sorbinil bind to the substrate binding site of aldose reductase?

Si Qi Liu, Aruni Bhatnagar, Satish Srivastava

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)2427-2429
Number of pages3
JournalBiochemical Pharmacology
Volume44
Issue number12
DOIs
StatePublished - Dec 15 1992

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Aldehyde Reductase
Benzyl Alcohol
Binding Sites
Substrates
Aldehydes
Coenzymes
Diabetes Complications
Enzymes
Catalytic Domain
Nucleotides
sorbinil

ASJC Scopus subject areas

  • Pharmacology

Cite this

Does sorbinil bind to the substrate binding site of aldose reductase? / Liu, Si Qi; Bhatnagar, Aruni; Srivastava, Satish.

In: Biochemical Pharmacology, Vol. 44, No. 12, 15.12.1992, p. 2427-2429.

Research output: Contribution to journalArticle

Liu, Si Qi ; Bhatnagar, Aruni ; Srivastava, Satish. / Does sorbinil bind to the substrate binding site of aldose reductase?. In: Biochemical Pharmacology. 1992 ; Vol. 44, No. 12. pp. 2427-2429.
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