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Literature summary for 4.1.1.23 extracted from

  • Vardi-Kilshtain, A.; Doron, D.; Major, D.T.
    Quantum and classical simulations of orotidine monophosphate decarboxylase: support for a direct decarboxylation mechanism (2013), Biochemistry, 52, 4382-4390.
    View publication on PubMed
Search for more literature for 4.1.1.23

Organism

Organism UniProt Comment Textmining
Methanobacterium thermoautotrophicus O26232
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Methanobacterium thermoautotrophicus DSM 1053 O26232
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information computed kinetic isotope effects support a direct decarboxylation mechanism. Data suggest a role for Lys72 in stabilizing the transition state in the catalysis of orotidine 5'-phosphate and, to a somewhat lesser extent, in 5-fluoro-orotidine 5'-phosphate Methanobacterium thermoautotrophicus ?
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additional information computed kinetic isotope effects support a direct decarboxylation mechanism. Data suggest a role for Lys72 in stabilizing the transition state in the catalysis of orotidine 5'-phosphate and, to a somewhat lesser extent, in 5-fluoro-orotidine 5'-phosphate Methanobacterium thermoautotrophicus DSM 1053 ?
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