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Rapid kinetics of an N-terminal mutant of cyanobacterial ribulose-1,5-bisphosphate carboxylase/oxygenase.

作者信息

Brändén R, Keys A J, Parry M A

机构信息

Department of Biochemistry and Biophysics, University of Göteborg, Sweden.

出版信息

Biochim Biophys Acta. 1990 Mar 1;1037(3):328-31. doi: 10.1016/0167-4838(90)90033-c.

DOI:10.1016/0167-4838(90)90033-c
PMID:2106915
Abstract

The transient changes in absorption of visible light upon addition of ribulose 1,5-bisphosphate to Co2(+)-activated ribulose-1,5-bisphosphate carboxylase/oxygenase were used to show altered catalytic properties of a mutant form of the enzyme from Anacystis nidulans. The mutant form of the enzyme had a modified N-terminus and a 10-fold greater Km for ribulose 1,5-bisphosphate than the natural cyanobacterial enzyme.

摘要

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