PMID: 5908634Feb 1, 1966

Choline kinase and phosphorylcholine phosphatase in plants

Plant Physiology
K TanakaA F Gohlke

Abstract

Choline kinase was present in barley and wheat roots and leaves of barley, wheat, tobacco, spinach and squash plants. The kinase was purified 25-fold from spinach leaves. The enzyme had a broad pH optimum between 7.5 and 10.0. Mg(++) was required for activity and in the presence of Mg(++) the enzyme was relatively stable. Maximum enzyme activity was obtained when the Mg(++): ATP ratio was 1:1. The K(m) was 1 x 10(-4)m. The kinase from leaves was similar to that from rapeseed or from yeast, except that the leaf and seed enzymes were not inhibited by compounds which attach sulfhydryl groups. Only a very slow hydrolysis of phosphorylcholine by similar plant extracts was observed. This phosphatase activity was purified 200- or 300-fold and appeared to be caused by a nonspecific acid phosphatase. The activity of both the kinase and the phosphatase did not seem sufficient to account for the rapid equilibration of the large phosphorylcholine reservoir of plants with exogenous P(32)-labeled orthophosphate.

References

Apr 1, 1952·Biochimica Et Biophysica Acta·H G HERS

Citations

Mar 1, 1970·Comparative Biochemistry and Physiology·S S Kumar, E Hodgson
Jan 9, 1999·The Plant Journal : for Cell and Molecular Biology·M L NuccioA D Hanson
Nov 1, 1971·Proceedings of the National Academy of Sciences of the United States of America·K D Johnson, H Kende
Sep 1, 1972·Proceedings of the National Academy of Sciences of the United States of America·J M LordH Beevers
Jun 1, 1990·Proceedings of the National Academy of Sciences of the United States of America·E GoutR Douce
Apr 22, 2006·Biochimica Et Biophysica Acta·Vinay ChoubeyUday Bandyopadhyay
Aug 24, 1970·Biochemical and Biophysical Research Communications·P N Setty, P S Krishnan
Nov 1, 1976·Archives of Biochemistry and Biophysics·B A Macher, J B Mudd

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