Literature summary for 5.1.2.2 extracted from

Mitra, B.; Kallarakal, A.T.; Kozarich, J.W.; Gerlt, J.A.; Clifton, J.G.; Petsko, G.A.; Kenyon, G.L.
Mechanism of the reaction catalyzed by mandelate racemase: importance of electrophilic catalysis by glutamic acid 317 (1995), Biochemistry, 34, 2777-2787.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
mutant E317Q	Pseudomonas putida

Protein Variants

Protein Variants	Comment	Organism
E317Q	E317Q with 3400fold reduced turnover number for (R)-mandelate and 29000fold reduced turnover number for (S)-mandelate. E317Q mutant enzyme does not catalyze detectable elimination of Br- from either enantiomer of p-(bromomethyl)mandelate. E317Q mutant enzyme is irreversibly inactivated by racemic alpha-phenylglycidate at a rate comparable to that measured for wild type enzyme	Pseudomonas putida

Inhibitors

Inhibitors	Comment	Organism	Structure
DL-alpha-Phenylglycidate	wild type enzyme and mutant E317Q	Pseudomonas putida

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.4	-	(R)-mandelate	wild type enzyme	Pseudomonas putida
2.4	-	(R)-mandelate	E317Q mutant	Pseudomonas putida

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas putida	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
wild type and mutant E317Q	Pseudomonas putida

Substrates and Products (Substrate)

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

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.012	-	(S)-Mandelate	mutant E317Q	Pseudomonas putida
350	-	(S)-Mandelate	wild type enzyme	Pseudomonas putida
500	-	(R)-mandelate	wild type enzyme	Pseudomonas putida

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Release 2023.1 (January 2023)