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Literature summary for 4.1.1.17 extracted from

  • Yamaguchi, Y.; Takatsuka, Y.; Kamio, Y.
    Two segments in bacterial antizyme P22 are essential for binding and enhance degradation of lysine/ornithine decarboxylase in Selenomonas ruminantium (2008), J. Bacteriol., 190, 442-446.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Selenomonas ruminantium degradation of lysine/ornithine decarboxylase by ATP-requiring protease(s) is accelerated by the binding of P22, which is a ribosomal protein of this strain, binding and activity analysis of wild-type and mutant P22s, segments A and B in P22 are crucial for P22 binding to LDC/ODC, overview ?
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Organism

Organism UniProt Comment Textmining
Selenomonas ruminantium
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information degradation of lysine/ornithine decarboxylase by ATP-requiring protease(s) is accelerated by the binding of P22, which is a ribosomal protein of this strain, binding and activity analysis of wild-type and mutant P22s, segments A and B in P22 are crucial for P22 binding to LDC/ODC, overview Selenomonas ruminantium ?
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?

Synonyms

Synonyms Comment Organism
LDC/ODC
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Selenomonas ruminantium
lysine/ornithine decarboxylase
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Selenomonas ruminantium