Conference paper

Substrate Binding Kinetics and its Role in the Cytochrome P450 Hydroxylation Sequence

J. Blanck ; Central Institute of Molecular Biology of the Academy of Sciences of the GDR, Department of Biocatalysis, 1115 Berlin-Buch, Lindenberger Weg 70, GDR
G. Smettan ; Central Institute of Molecular Biology of the Academy of Sciences of the GDR, Department of Biocatalysis, 1115 Berlin-Buch, Lindenberger Weg 70, GDR
G.-R. Janig ; Central Institute of Molecular Biology of the Academy of Sciences of the GDR, Department of Biocatalysis, 1115 Berlin-Buch, Lindenberger Weg 70, GDR
K. Ruckpaul ; Central Institute of Molecular Biology of the Academy of Sciences of the GDR, Department of Biocatalysis, 1115 Berlin-Buch, Lindenberger Weg 70, GDR

Abstract

The kinetics of the binding of type I and type II substrates
to cytochrome P450LM has been investigated. Type I substrates are
preferentially bound compared to type II compounds. The rate
constants range between 103 and 105 [M-1 s-1], indicating possible
interference with rate limiting steps. Substrates bind to the reduced
cytochrome with considerably lower rate constants. The results
are in favour of the sequential reaction mechanism. The solubilized
enzyme preparation shows properties similar to the microsomal
enzyme system.

Keywords

Hrčak ID:

196366

URI

https://hrcak.srce.hr/196366

Publication date:

30.3.1977.

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