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Biliverdin reductase: substrate specificity and kinetics.

R B Frydman¹, M L Tomaro, J Rosenfeld

¹Facultad de Farmacia y Bioquimica, Universidad de Buenos Aires, Argentina.

Biochimica Et Biophysica Acta

|December 18, 1987

Summary

Biliverdin reductase activity depends on the number of propionate residues in biliverdin. Forms 1 and 3 exhibit cooperative kinetics, while form 2 follows Michaelian kinetics.

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Area of Science:

Biochemistry
Enzymology

Background:

Biliverdin reductase (BVR) plays a crucial role in heme catabolism.
Understanding BVR substrate specificity is key to elucidating its physiological functions.

Purpose of the Study:

To investigate the substrate specificity of rat liver biliverdin reductase forms.
To characterize the kinetic properties of different BVR molecular forms.

Main Methods:

Utilized synthetic biliverdins with varying side chains to test substrate activity.
Analyzed enzyme kinetics using nonlinear regression and a cooperative dimer model.
Compared substrate reduction rates across different BVR molecular forms (1, 2, and 3).

Main Results:

Biliverdin reductase requires at least two propionate residues for substrate activity.

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Molecular forms 1 and 3 displayed sigmoidal kinetics, indicative of cooperative binding.

Molecular form 2 exhibited classical Michaelian kinetics.

Specific biliverdin isomers were reduced at significantly different rates by forms 1 and 3.

Conclusions:

Rat liver biliverdin reductase exhibits distinct substrate specificities and kinetic behaviors based on its molecular form.
The enzyme's kinetic data support a moderate cooperative dimer model for forms 1 and 3.
Side chain composition of biliverdin significantly influences its interaction with BVR.