Identification of the reactive cysteine residue in human placenta aldose reductase

Si Qi Liu; Aruni Bhatnagar; Naseem H. Ansari; Satish K. Srivastava

doi:10.1016/0167-4838(93)90258-S

Identification of the reactive cysteine residue in human placenta aldose reductase

Si Qi Liu, Aruni Bhatnagar, Naseem H. Ansari, Satish K. Srivastava

Biochemistry & Molecular Biology

Research output: Contribution to journal › Article › peer-review

24 Scopus citations

Abstract

Modification of human placental aldose reductase by iodoacetate (IAA) led to a mol/mol binding of IAA, a 40% decrease in the k_cat, a 3-5-fold increase in the K_m,NADPH and K_{m,glyceraldehyde} and a 600-fold increase in the K_i,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 language	English (US)
Pages (from-to)	268-272
Number of pages	5
Journal	Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume	1164
Issue number	3
DOIs	https://doi.org/10.1016/0167-4838(93)90258-S
State	Published - Aug 7 1993

Keywords

Aldose reductase
Enzyme modification
Reactive residue

ASJC Scopus subject areas

Structural Biology
Biophysics
Biochemistry
Molecular Biology

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10.1016/0167-4838(93)90258-S

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title = "Identification of the reactive cysteine residue in human placenta aldose reductase",

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.",

keywords = "Aldose reductase, Enzyme modification, Reactive residue",

author = "Liu, {Si Qi} and Aruni Bhatnagar and Ansari, {Naseem H.} and Srivastava, {Satish K.}",

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T1 - Identification of the reactive cysteine residue in human placenta aldose reductase

AU - Liu, Si Qi

AU - Bhatnagar, Aruni

AU - Ansari, Naseem H.

AU - Srivastava, Satish K.

PY - 1993/8/7

Y1 - 1993/8/7

N2 - 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.

AB - 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.

KW - Aldose reductase

KW - Enzyme modification

KW - Reactive residue

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IS - 3

ER -

Identification of the reactive cysteine residue in human placenta aldose reductase

Abstract

Keywords

ASJC Scopus subject areas

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