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J Biol Chem, Vol. 273, Issue 22, 13658-13662, May 29, 1998
Identification of an FAD Superfamily Containing
Protoporphyrinogen Oxidases, Monoamine Oxidases, and Phytoene
Desaturase
EXPRESSION AND CHARACTERIZATION OF PHYTOENE DESATURASE OF
MYXOCOCCUS XANTHUS
Tamara A.
Dailey and
Harry A.
Dailey
From the Department of Microbiology, Department of Biochemistry and
Molecular Biology, University of Georgia, Athens, Georgia
30602-7229
A large number of FAD-containing proteins have
previously been shown to contain a signature sequence that is referred
to as the dinucleotide binding motif. Protoporphyrinogen oxidase (PPO), the penultimate enzyme of the heme biosynthetic pathway, is an FAD-containing protein that catalyzes the six electron oxidation of
protoporphyrinogen IX. Sequence analysis demonstrates the presence of
the dinucleotide binding motif at the amino-terminal end of the
protein. Analysis of the current data base reveals that PPO has
significant sequence similarities to mammalian monoamine oxidases (MAO)
A and B, as well as to bacterial and plant phytoene desaturases (PHD).
Previously MAOs have been shown to contain FAD, but there are no
publications demonstrating the presence of FAD in purified PHDs. We
have carried out the expression and purification of PHD from the
bacterium Myxococcus xanthus and demonstrate the presence of noncovalently bound FAD. Sequence analysis demonstrate that PPO is
closely related to bacterial PHDs and more distantly to plant PHDs and
animal MAOs. Interestingly bacterial MAOs are no more closely related
to PPOs, PHDs, and animal MAO's than they are to the unrelated
Pseudomonas phenyl hydroxylase. All of the related
sequences contain not only the basic putative dinucleotide binding
motif that is found frequently for FAD-binding proteins, but they also
have high similarity in an approximately 60-residue long region that
extends beyond the dinucleotide motif. This region is not found among
any other proteins in the current data base and, therefore, we propose
that this region is a signature motif for a superfamily of
FAD-containing enzymes that is comprised of PPOs, animal MAOs, and
PHDs.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 1998 by the American Society for Biochemistry and Molecular Biology.
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