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Phosphoglycerate mutase has essential arginyl residues.

C L Borders¹, B A Wilson

¹Department of Chemistry, College of Wooster, Wooster, Ohio 44691, USA.

Biochemical and Biophysical Research Communications

|December 20, 1976

Summary

Butanedione inactivates phosphoglycerate mutase by modifying arginyl residues. Cofactors and substrates protect specific sites, suggesting a role for these arginines in enzyme activity.

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Area of Science:

Biochemistry
Enzymology

Background:

Phosphoglycerate mutase catalyzes a key step in glycolysis.
Enzyme activity is regulated by various factors, including chemical modification.

Purpose of the Study:

To investigate the inactivation mechanism of phosphoglycerate mutase by butanedione.
To identify the specific amino acid residues modified by butanedione and their role in enzyme function.

Main Methods:

Enzyme kinetics assays to measure phosphoglycerate mutase activity.
Chemical modification of enzyme with butanedione in borate buffer.
Amino acid residue analysis to determine modification sites.

Main Results:

Butanedione inactivates phosphoglycerate mutase, with inactivation correlating to arginyl residue modification.
At 0.13 mM butanedione, one arginyl residue per subunit is modified.
At 0.50 mM butanedione, three arginyl residues per subunit are modified, with two protected by cofactor and substrate.

Conclusions:

Arginyl residues are critical for phosphoglycerate mutase activity.
The binding of cofactor (2,3-diphosphoglycerate) and substrate (3-phosphoglycerate) protects specific arginyl residues from modification, indicating their involvement in substrate binding or catalysis.

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