Literature summary extracted from

Maggio, E.T.; Kenyon, G.L.; Mildvan, A.S.; Hegeman, G.D.
Mandelate racemase from Pseudomonas putida. Magnetic resonance and kinetic studies of the mechanism of catalysis (1975), Biochemistry, 14, 1131-1139.

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
5.1.2.2	3-Hydroxy-2-naphthoic acid	noncompetitive inhibition	Pseudomonas putida
5.1.2.2	4-Hydroxycoumarin	noncompetitive	Pseudomonas putida
5.1.2.2	benzoate	mixed-type inhibition	Pseudomonas putida
5.1.2.2	DL-alpha-Phenylglycerate	competitive	Pseudomonas putida
5.1.2.2	naphthoate	mixed-type inhibition	Pseudomonas putida
5.1.2.2	salicylate	competitive	Pseudomonas putida

Metals/Ions

EC Number	Metals/Ions	Comment	Organism	Structure
5.1.2.2	Mn2+	enzyme binds 0.9 mol Mn2+ per mol of subunit with a dissociation constant of 0.008 mM. Also six additional Mn2+ bind to the enzyme much more weakly, with a dissociation constant of 1.5 mM	Pseudomonas putida

Organism

EC Number	Organism	UniProt	Comment	Textmining
5.1.2.2	Pseudomonas putida	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
5.1.2.2	D-mandelate	-	Pseudomonas putida	L-mandelate	-	?

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)