Identification of the reactive cysteine residue in human placenta aldose reductase

Si Qi Liu, Aruni Bhatnagar, Naseem Ansari, Satish Srivastava

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

Modification of human placental aldose reductase by iodoacetate (IAA) led to a mol/mol binding of IAA, a 40% decrease in the kcat, a 3-5-fold increase in the Km,NADPH and Km,glyceraldehyde and a 600-fold increase in the Ki,sorbinil; determined at pH 6.0. NADPH and 2′-monophosphoadenosine 5′-diphosphoribose but neither glyceraldehyde nor sorbinil, prevented carboxymethylation-induced changes. Cleavage of [14C]IAA-modified enzyme by trypsin resulted in two radiolabeled peptides: Val-297 to Lys-307 and Val-297 to Phe-315. In both these peptides Cys-298 was the only radiolabeled residue. It is suggested that Cys-298 regulates the kinetic and inhibition properties of the enzyme, but does not participate in catalysis.

Original languageEnglish (US)
Pages (from-to)268-272
Number of pages5
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume1164
Issue number3
DOIs
StatePublished - Aug 7 1993

Fingerprint

Iodoacetates
Aldehyde Reductase
Placenta
Glyceraldehyde
Cysteine
NADP
Peptides
Enzymes
Catalysis
Trypsin
Kinetics
sorbinil

Keywords

  • Aldose reductase
  • Enzyme modification
  • Reactive residue

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Structural Biology

Cite this

Identification of the reactive cysteine residue in human placenta aldose reductase. / Liu, Si Qi; Bhatnagar, Aruni; Ansari, Naseem; Srivastava, Satish.

In: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, Vol. 1164, No. 3, 07.08.1993, p. 268-272.

Research output: Contribution to journalArticle

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