Literature summary for 1.13.11.20 extracted from

Yeh, C.G.; Pierides, C.; Jameson, G.N.L.; de Visser, S.P.
Structure and functional differences of cysteine and 3-mercaptopropionate dioxygenases A computational study (2021), Chemistry, 27, 13793-13806 .

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q16878	-	-

General Information

General Information	Comment	Organism
metabolism	active-site cluster models and comparison of CDO and 3-mercaptopropionate dioxygenase MDO, EC 1.13.11.91. The enzymes have different iron(III)-superoxo-bound structures due to differences in ligand coordination. The differences in the second-coordination sphere and the position of a positively charged Arg residue result in changes in substrate positioning, mobility and enzymatic turnover. For both enzymes, the second oxygen atom transfer has the highest barriers with magnitudes of 14.2 and 15.8 kcal/mol, respectively. In CDO with its 3-His ligand system, there are close-lying singlet, triplet and quintet spin-state surfaces along the mechanism, and the reaction will be influenced by the equilibration between these spin states and the ease of spin state change	Homo sapiens

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Release 2023.1 (January 2023)