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Pyridoxal-dependent decarboxylase, pyridoxal binding domain
crystal structure of a d,l-lysine complex of diaminopimelate decarboxylase
Identifiers
Symbol	Orn_Arg_deC_N
Pfam	PF02784
Pfam clan	CL0036
InterPro	IPR022644
PROSITE	PDOC00685
SCOP2	1qu4 / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Pyridoxal-dependent decarboxylase, C-terminal sheet domain
a dimer interface mutant of ornithine decarboxylase reveals structure of gem diamine intermediate
Identifiers
Symbol	Orn_DAP_Arg_deC
Pfam	PF00278
InterPro	IPR022643
PROSITE	PDOC00685
SCOP2	1qu4 / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

In molecular biology, group IV pyridoxal-dependent decarboxylases are a family of enzymes comprising ornithine decarboxylase EC 4.1.1.17, lysine decarboxylase EC 4.1.1.18, arginine decarboxylase EC 4.1.1.19 and diaminopimelate decarboxylaseEC 4.1.1.20. It is also known as the Orn/Lys/Arg decarboxylase class-II family.

Pyridoxal-5'-phosphate-dependent amino acid decarboxylases can be divided into four groups based on amino acid sequence. Group IV comprises eukaryotic ornithine and lysine decarboxylase and the prokaryotic biosynthetic type of arginine decarboxylase and diaminopimelate decarboxylase.

Members of this family while most probably evolutionary related, do not share extensive regions of sequence similarities. The proteins contain a conserved lysine residue which is known, in mouse ODC to be the site of attachment of the pyridoxal-phosphate group. The proteins also contain a stretch of three consecutive glycine residues and has been proposed to be part of a substrate-binding region.

See also

• Group I pyridoxal-dependent decarboxylases
• Group II pyridoxal-dependent decarboxylases
• Group III pyridoxal-dependent decarboxylases

References

1. ^ Sandmeier E, Hale TI, Christen P (May 1994). "Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases". Eur. J. Biochem. 221 (3): 997–1002. doi:10.1111/j.1432-1033.1994.tb18816.x. PMID 8181483.
2. Poulin R, Lu L, Ackermann B, Bey P, Pegg AE (January 1992). "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 (1): 150–8. PMID 1730582.
3. Moore RC, Boyle SM (August 1990). "Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli". J. Bacteriol. 172 (8): 4631–40. doi:10.1128/jb.172.8.4631-4640.1990. PMC 213298. PMID 2198270.

• Protein domains