Literature summary extracted from

Ren, X.; Tu, C.; Bhatt, D.; Perry, J.J.; Tainer, J.A.; Cabelli, D.E.; Silverman, D.N.
Kinetic and structural characterization of human manganese superoxide dismutase containing 3-fluorotyrosines (2006), J. Mol. Struct., 790, 168-173.

No PubMed abstract available

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.15.1.1	crystal structures of unfluorinated and fluorinated enzyme are nearly superimposable. Ratio kcat/Km decreases from 0.8 per mM and s for wild-type to 0.03 per mM and s for the fluorinated mutant which is in significant part due to 3-fluorotyrosine residues distant from the active-site metal	Homo sapiens

Protein Variants

EC Number	Protein Variants	Comment	Organism
1.15.1.1	additional information	replacement of all of the nine tyosine residues in each of the four enzyme subunits by 3-fluorotyrosine. Crystal structures of unfluorinated and fluorinated enzyme are nearly superimposable. Ratio kcat/Km decreases from 0.8 per mM and s for wild-type to 0.03 per mM and s for the fluorinated mutant which is in significant part due to 3-fluorotyrosine residues distant from the active-site metal	Homo sapiens
1.15.1.1	Y34F	about 12fold decrease in kcat value	Homo sapiens

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.15.1.1	Homo sapiens	-	manganese superoxide dismutase	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.15.1.1	O2- + H+	-	Homo sapiens	O2 + H2O2	-	?

Turnover Number [1/s]

EC Number	Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
1.15.1.1	1100	-	O2-	pH 7.5, 25°C, mutant Y34F with fluorinated Tyr-residues	Homo sapiens
1.15.1.1	3300	-	O2-	pH 7.5, 25°C, mutant Y34F	Homo sapiens
1.15.1.1	4600	-	O2-	pH 7.5, 25°C, wild-type with fluorinated Tyr-residues	Homo sapiens
1.15.1.1	40000	-	O2-	pH 7.5, 25°C, wild-type	Homo sapiens

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Release 2023.1 (January 2023)