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Plant Physiol, January 2001, Vol. 125, pp. 378-386
Molecular and Biochemical Characterization of a Cytokinin Oxidase
from Maize1
Kristin D.
Bilyeu,*
Jean L.
Cole,
James G.
Laskey,
Wayne R.
Riekhof,
Thomas J.
Esparza,
Michelle D.
Kramer, and
Roy O.
Morris
Department of Biochemistry, University of Missouri, Columbia,
Missouri 65211
It is generally accepted that cytokinin oxidases, which oxidatively
remove cytokinin side chains to produce adenine and the corresponding
isopentenyl aldehyde, play a major role in regulating cytokinin levels
in planta. Partially purified fractions of cytokinin oxidase from
various species have been studied for many years, but have yet to
clearly reveal the properties of the enzyme or to define its biological
significance. Details of the genomic organization of the recently
isolated maize (Zea mays) cytokinin oxidase gene
(ckx1) and some of its Arabidopsis homologs are now presented. Expression of an intronless ckx1 in
Pichia pastoris allowed production of large amounts of
recombinant cytokinin oxidase and facilitated detailed kinetic and
cofactor analysis and comparison with the native enzyme. The enzyme is
a flavoprotein containing covalently bound flavin adenine dinucleotide,
but no detectable heavy metals. Expression of the oxidase in maize
tissues is described.
1
This research was supported by grants from the
Monsanto Corporation and the Illinois-Missouri Biotechnology Alliance.
*
Corresponding author; e-mail bilyeuk{at}missouri.edu; fax
573-882-5635.
© 2001 American Society of Plant Physiologists
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