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| rdf:type | |
| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
S-adenosylmethionine decarboxylase proenzyme
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| http://www.biopax.org/relea... |
DCAM_YEAST
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| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
4.1.1.50,
AdoMetDC,
S-adenosylmethionine decarboxylase alpha chain,
S-adenosylmethionine decarboxylase beta chain,
SAMDC
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| http://www.biopax.org/relea... |
FUNCTION: S-adenosylmethionine decarboxylase is essential for normal growth, sporulation, maintenance of ds-RNA virus, biosynthesis of spermine and spermidine. CATALYTIC ACTIVITY: S-adenosyl-L-methionine = (5-deoxy-5- adenosyl)(3-aminopropyl)-methylsulfonium salt + CO(2). COFACTOR: Pyruvoyl group. PATHWAY: Amine and polyamine biosynthesis; S- adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N- terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain (By similarity). MISCELLANEOUS: Present with 7060 molecules/cell in log phase SD medium. SIMILARITY: Belongs to the eukaryotic AdoMetDC family. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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