Literature summary for 1.15.1.1 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

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Protein Variants	Comment	Organism
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
Y34F	about 12fold decrease in kcat value	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	manganese superoxide dismutase	-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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

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Release 2023.1 (January 2023)