InterPro domain: IPR036633
General Information
- Identifier IPR036633
- Description Orn/Lys/Arg decarboxylase, C-terminal domain superfamily
- Number of genes 123
- Gene duplication stats Loading...
- Associated GO terms GO:0003824
Abstract
Pyridoxal-dependent decarboxylases are bacterial proteins acting on ornithine, lysine, arginine and related substrates [ 1 ].One of the regions of sequence similarity contains a conserved lysine residue, which is the site of attachment of the pyridoxal-phosphate group. Ornithine decarboxylase is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. Arginine decarboxylase catalyzes the decarboxylation of arginine and lysine decarboxylase catalyzes the decarboxylation of lysine. Members of this superfamily are widely found in all three forms of life [ 2 , 2 , 3 , 4 , 5 , 6 , 7 , 8 , 9 , 10 , 11 , 12 , 13 , 14 ].
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2. Structural motifs for pyridoxal-5'-phosphate binding in decarboxylases: an analysis based on the crystal structure of the Lactobacillus 30a ornithine decarboxylase. Protein Sci. 4, 849-54
3. The GTP effector site of ornithine decarboxylase from Lactobacillus 30a: kinetic and structural characterization. Biochemistry 36, 16147-54
4. Stereospecificity for the hydrogen transfer and molecular evolution of pyridoxal enzymes. Biosci. Biotechnol. Biochem. 60, 181-7
5. Evolutionary relationships among pyridoxal-5'-phosphate-dependent enzymes. Regio-specific alpha, beta and gamma families. Eur. J. Biochem. 219, 953-60
6. Pyridoxal phosphate-dependent enzymes. Biochim. Biophys. Acta 1248, 81-96
7. Identification of the amino acid residues conferring substrate specificity upon Selenomonas ruminantium lysine decarboxylase. Curr. Med. Chem. 63, 1843-6
8. Pyridoxal 5'-phosphate enzymes as targets for therapeutic agents. Chem Rec 14, 1291-324
9. Exploring the pyridoxal 5'-phosphate-dependent enzymes. Structure 6, 275-87
10. Common structural elements in the architecture of the cofactor-binding domains in unrelated families of pyridoxal phosphate-dependent enzymes. Proteins 35, 250-61
11. Structure, evolution and action of vitamin B6-dependent enzymes. Curr. Opin. Struct. Biol. 8, 759-69
12. The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes. Adv. Enzymol. Relat. Areas Mol. Biol. 74, 129-84
13. From cofactor to enzymes. The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes. null 1, 436-47
14. The manifold of vitamin B6 dependent enzymes. Biosci. Biotechnol. Biochem. 8, R1-6