Literature summary for 1.13.11.91 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
Pseudomonas aeruginosa	Q9I0N5	-	-
Pseudomonas aeruginosa DSM 22644	Q9I0N5	-	-

Synonyms

Synonyms	Comment	Organism
PA2602	-	Pseudomonas aeruginosa

General Information

General Information	Comment	Organism
metabolism	active-site cluster models and comparison of CDO, EC 1.13.11.20, and 3-mercaptopropionate dioxygenase MDO. The enzymes have different iron(III)-superoxo-bound structures due to differences in ligand coordination. The differences in the second-coordination sphere and particularly 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. Both enzymes have an open-shell singlet-spin iron(III)-superoxo reactant with the substrate bound as a bidentate ligand in the equatorial plane, in MDO the quintet spin state is within 1 kcal/mol. MDO binds the substrate through two anionic bonds of the substrate carboxylate and thiolate groups, and a strong hydrogen-bonding interaction of a Tyr residue towards the superoxo group in MDO is found	Pseudomonas aeruginosa

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Release 2023.1 (January 2023)