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Literature summary for 4.1.1.23 extracted from

  • Fujihashi, M.; Ishida, T.; Kuroda, S.; Kotra, L.P.; Pai, E.F.; Miki, K.
    Substrate distortion contributes to the catalysis of orotidine 5-monophosphate decarboxylase (2013), J. Am. Chem. Soc., 135, 17432-17443.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structures with ligand anlogues. Enzyme can distort the bond between the aromatic ring of a ligand and its C6 substituent, regardless of the latter's charge or size. The distortion contributes 3.7 kcal/mol to the catalysis. In their respective complexes, 6-methyl-UMP displays significant distortion of its methyl substituent bond, 6-amino-UMP shows the competition between the K72 and C6 substituents for a position close to D70, and the methyl and ethyl esters of orotidine 5'-monophosphate both induce rotation of the carboxylate group substituent out of the plane of the pyrimidine ring. In addition, the bond between the carboxylate group and the pyrimidine ring is distorted Methanothermobacter thermautotrophicus

Organism

Organism UniProt Comment Textmining
Methanothermobacter thermautotrophicus O26232
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Methanothermobacter thermautotrophicus DSM 1053 O26232
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