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Pyridoxal-dependent decarboxylases acting on ornithine, lysine, arginine and
related substrates can be classified into two different families on the basis
of sequence similarities [1,2]. The first family consists of:
Prokaryotic ornithine decarboxylase (EC 220.127.116.11) (ODC). ODC catalyzes the
transformation of ornithine into putrescine.
Prokaryotic lysine decarboxylase (EC 18.104.22.168) (LDC). LDC catalyzes the
transformation of lysine into cadaverine.
Escherichia coli biodegradative arginine decarboxylase (EC 22.214.171.124) (ADC).
ADC catalyzes the transformation of arginine into agmatine.
Bacillus subtilis hypothetical protein yaaO.
One of the regions of sequence similarity contains a conserved lysine residue
which is known, in Escherichia coli LDC  and in ADC , to be the site of
attachment of the pyridoxal-phosphate group. We have used this region as a
These enzymes are collectively known as group III decarboxylases .
November 1997 / Text revised.
PROSITE method (with tools and information) covered by this documentation:
Unpublished observations (1993).
Sandmeier E., Hale T.I., Christen P.
Eur. J. Biochem. 221:997-1002(1994).
Meng S.-Y., Bennett G.N.
Nucleotide sequence of the Escherichia coli cad operon: a system for neutralization of low extracellular pH.
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