Ornithine decarboxylase antizyme

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Ornithine decarboxylase antizyme
Ornithine decarboxylase antizyme
	NMR structure of antizyme isoform 1 from rat
Identifiers
Symbol	ODC_AZ
Pfam	PF02100
InterPro	IPR002993
PROSITE	PDOC01039
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

In molecular biology, Ornithine decarboxylase antizyme (ODC-AZ) is an ornithine decarboxylase inhibitor. It binds to, and destabilises, ornithine decarboxylase (ODC), a key enzyme in polyamine synthesis. ODC is then rapidly degraded.^[1] It was first characterized in 1981.^[2] The expression of ODC-AZ requires programmed, ribosomal frameshifting which is modulated according to the cellular concentration of polyamines. High levels of polyamines induce a +1 ribosomal frameshift in the translation of mRNA for the antizyme leading to the expression of a full-length protein. At least two forms of ODC-AZ exist in mammals ^[3] and the protein has been found in Drosophila (protein Gutfeeling^[4]) as well as in Saccharomyces yeast (encoded by the OAZ1 gene).^[5]

Human genes encoding Ornithine decarboxylase antizymes are OAZ1, OAZ2, and OAZ3.

References

^ Matsufuji S, Matsufuji T, Miyazaki Y, Murakami Y, Atkins JF, Gesteland RF, Hayashi S (January 1995). "Autoregulatory frameshifting in decoding mammalian ornithine decarboxylase antizyme". Cell. 80 (1): 51–60. doi:10.1016/0092-8674(95)90450-6. PMID 7813017.
^ Heller JS, Canellakis ES (1981). "Cellular control of ornithine decarboxylase activity by its antizyme". J. Cell. Physiol. 107 (2): 209–17. doi:10.1002/jcp.1041070206. PMID 7251680.
^ Ivanov IP, Gesteland RF, Atkins JF (September 1998). "A second mammalian antizyme: conservation of programmed ribosomal frameshifting". Genomics. 52 (2): 119–29. doi:10.1006/geno.1998.5434. PMID 9782076.
^ Salzberg, A.; Golden, K.; Bodmer, R.; Bellen, H. J. (1996-09-01). "Gutfeeling, a Drosophila Gene Encoding an Antizyme-like Protein, Is Required for Late Differentiation of Neurons and Muscles". Genetics. 144 (1): 183–196. ISSN 0016-6731. PMC 1207492.
^ SGD entry for OAZ1 gene

This article incorporates text from the public domain Pfam and InterPro: IPR002993

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v t e Carbon–carbon lyases (EC 4.1)
4.1.1: Carboxy-lyases	Acetoacetate decarboxylase Adenosylmethionine decarboxylase Arginine decarboxylase Aromatic L-amino acid decarboxylase Glutamate decarboxylase Histidine decarboxylase Lysine decarboxylase Malonyl-CoA decarboxylase Ornithine decarboxylase Oxaloacetate decarboxylase Phosphoenolpyruvate carboxykinase Phosphoenolpyruvate carboxylase Phosphoribosylaminoimidazole carboxylase Pyrophosphomevalonate decarboxylase Pyruvate decarboxylase RuBisCO Uridine monophosphate synthetase/Orotidine 5'-phosphate decarboxylase Uroporphyrinogen III decarboxylase
4.1.2: Aldehyde-lyases	Fructose-bisphosphate aldolase Aldolase A Aldolase B Aldolase C 2-hydroxyphytanoyl-CoA lyase Threonine aldolase
4.1.3: Oxo-acid-lyases	Isocitrate lyase 3-hydroxy-3-methylglutaryl-CoA lyase
4.1.99: Other	Tryptophanase Photolyase CPD lyase Spore photoproduct lyase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)