| Literature References | 1. MARTIN, C., CAMI, B., YEH, P., STRAGIER, P., PARSOT, C. AND PATTE, J.-C.
Pseudomonas aeruginosa diaminopimelate decarboxylase: evolutionary
relationship with other amino acid decarboxylases.
MOL.BIOL.EVOL. 5 549-559 (1988).
2. SANDMEIER, E., HALE, T.I. AND CHRISTEN, P.
Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid
decarboxylases.
EUR.J.BIOCHEMISTRY 221 997-1002 (1994).
3. RASTOGI, R., DULSON, J. AND ROTHSTEIN, S.J.
Cloning of tomato (Lycopersicon esculentum Mill.) arginine decarboxylase
gene and its expression during fruit ripening.
PLANT PHYSIOL. 103 829-834 (1993).
4. POULIN, R., LU, L., ACKERMANN, B., BEY, P. AND PEGG, A.E.
Mechanism of the irreversible inactivation of mouse ornithine decarboxylase
by alpha-difluoromethylornithine. Characterization of sequences at the
inhibitor and coenzyme binding sites.
J.BIOL.CHEM. 267 150-158 (1992).
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| Documentation | Pyridoxal-dependent decarboxylases that act on ornithine-, lysine-,
arginine- and related substrates can be classified into different families
on the basis of sequence similarity [1,2]. One of these families includes:
eukaryotic ornithine decarboxylase (ODC), which catalyses the transformation
of ornithine into putrescine; prokaryotic diaminopimelic acid decarboxylase
(DAPDC), which catalyses the conversion of diaminopimelic acid into lysine,
the final step of lysine biosynthesis; Pseudomonas syringae pv. tabaci
protein, tabA, which is probably involved in tabtoxin biosynthesis and
is similar to DAPDC; and bacterial and plant biosynthetic arginine
decarboxylase (ADC), which catalyses the transformation of arginine
into agmatine, the first step in putrescine synthesis from arginine.
Although these proteins, which are known collectively as group IV
decarboxylases [2], probably share a common evolutionary origin, their
levels of sequence similarity are low, being confined to a few short
conserved regions.
The tomato ADC gene contains an open reading frame encoding a polypeptide
of 502 amino acids and a predicted molecular mass of ~55 kD [3]. The
predicted amino acid sequence shares 47 and 38% identify with oat and
E.coli ADCs, respectively. Gel blot hybridisation experiments show that,
in tomato, ADC is encoded by a single gene and is expressed as a transcript
of ~2.2kb in the fruit pericarp and leaf tissues [3].
ARGDCRBXLASE is a 9-element fingerprint that provides a signature for
arginine decarboxylases. The fingerprint was derived from an initial
alignment of 3 sequences: the motifs were drawn from conserved regions
spanning virtually the full alignment length, focusing on those sections
that characterise the arginine decarboxylases but distinguish them from
the rest of the ODA family. Four iterations on SPTR37_10f were required to
reach convergence, at which point a true set comprising 13 sequences was
identified. Several partial matches were also found: Q9ZKH4 and O25176 are
arginine carboxylases that match only 5 motifs; and O69203 is a closely
related diaminopimelate decarboxylase that matches 2 motifs.
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