Literature summary for 5.1.1.13 extracted from

Ohtaki, A.; Nakano, Y.; Iizuka, R.; Arakawa, T.; Yamada, K.; Odaka, M.; Yohda, M.
Structure of aspartate racemase complexed with a dual substrate analogue, citric acid, and implications for the reaction mechanism (2008), Proteins Struct. Funct. Bioinform., 70, 1167-1174.

Search for more literature for 5.1.1.13

Crystallization (Commentary)

Crystallization (Comment)	Organism
catalytically inactive mutant C82A in complex with citric acid, 2.0 A resolution. Citric acid binds to the catalytic site, which induces a conformational change to close the active site. Residue R48 is responsible for recognizing carboxyl groups of the substrates L-/D-aspartates and stabilizing a reaction intermediate, and L164 is responsible for stabilizing a closed state structure	Pyrococcus horikoshii

Protein Variants

Protein Variants	Comment	Organism
C82A	catalytically inactive. Crystallization data in complex with citric acid	Pyrococcus horikoshii

Inhibitors

Inhibitors	Comment	Organism	Structure
Citric acid	competitive	Pyrococcus horikoshii

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.7	-	L-aspartate	pH 8.0, 70°C	Pyrococcus horikoshii

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus horikoshii	O58403	strain OT3	-
Pyrococcus horikoshii OT-3	O58403	strain OT3	-

Reaction

Reaction	Comment	Organism	Reaction ID
L-aspartate = D-aspartate	one-base mechanism, residue C194 plays the role of the base for not only L-aspartate but also D-aspartate	Pyrococcus horikoshii	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-aspartate	-	Pyrococcus horikoshii	D-aspartate	-	?
L-aspartate	-	Pyrococcus horikoshii OT-3	D-aspartate	-	?

Synonyms

Synonyms	Comment	Organism
PhAspR	-	Pyrococcus horikoshii

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
7.4	-	Citric acid	pH 8.0, 70°C	Pyrococcus horikoshii

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Release 2023.1 (January 2023)