Literature summary for 4.3.1.27 extracted from

Matsumoto, Y.; Yasutake, Y.; Takeda, Y.; Tamura, T.; Yokota, A.; Wada, M.
Structural insights into the substrate stereospecificity of D-threo-3-hydroxyaspartate dehydratase from Delftia sp. HT23 a useful enzyme for the synthesis of optically pure L-threo- and D-erythro-3-hydroxyaspartate (2015), Appl. Microbiol. Biotechnol., 99, 7137-7150 .

Search for more literature for 4.3.1.27

Application

Application	Comment	Organism
synthesis	optically pure synthesis of L-threo-3-hydroxyaspartate and D-threo-3-hydroxyaspartate, promising intermediates for the synthesis of beta-benzyloxyaspartate by using a purified enzyme as a biocatalyst for the resolution of racemic DL-threo-3-hydroxyaspartate and DL-erythro-3-hydroxyaspartate. Considering 50% of the theoretical maximum, efficient yields of L-threo-3-hydroxyaspartate (38.9 %) and D-erythro-3-hydroxyaspartate (48.9 %) as isolated crystals are achieved with more than 99 % enantiomeric excess	Delftia sp. HT23

Crystallization (Commentary)

Crystallization (Comment)	Organism
sitting drop or hanging drop vapor diffusion method at 20°C, crystal structures of the enzyme in complex with the inhibitor D-erythro-3-hydroxyaspartate, crystal structure of the poorly active H351A mutant complexed with its substrate L-erythro-3-hydroxyaspartate, and H351A mutant enzyme complexed with the reaction intermediate 2-amino maleic acid	Delftia sp. HT23

Protein Variants

Protein Variants	Comment	Organism
C353A	mutations significantly decreases the activity toward threo-3-hydroxy-D-aspartate and erythro-3-hydroxy-L-aspartate	Delftia sp. HT23
H351A	mutations significantly decreases the activity toward threo-3-hydroxy-D-aspartate and erythro-3-hydroxy-L-aspartate	Delftia sp. HT23

General Stability

General Stability	Organism
Mg2+ is not required for the structural stabilization of the enzyme	Delftia sp. HT23

Inhibitors

Inhibitors	Comment	Organism	Structure
erythro-3-hydroxy-D-aspartate	-	Delftia sp. HT23

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	one Mg2+ is located between His351 and Cys353 at the active site. The other Mg2+ is chelated by the beta-carboxyl O atom and the beta-hydroxyl O atom of erythro-3-hydroxy-D-aspartate, forming a erythro-3-hydroxy-D-aspartate-Mg2+ complex	Delftia sp. HT23

Organism

Organism	UniProt	Comment	Textmining
Delftia sp. HT23	B2DFG5	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Delftia sp. HT23

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
0.12	-	pH 8.0, 30°C, mutant enzyme H351A, substrate: threo-3-hydroxy-D-aspartate	Delftia sp. HT23
21.1	-	pH 8.0, 30°C, wild-type enzyme, substrate: threo-3-hydroxy-D-aspartate	Delftia sp. HT23

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
threo-3-hydroxy-D-aspartate	the substrate specificity of the enzyme is determined by the orientation of the Cbeta-OH at the active site, whose spatial arrangement is compatible with the 3R configuration of 3-hydroxyaspartate. The enzyme also catalyzes the dehydration of erythro-3-hydroxy-L-aspartate	Delftia sp. HT23	oxaloacetate + NH3	-	?

Synonyms

Synonyms	Comment	Organism
D-THA DH	-	Delftia sp. HT23
D-threo-3-hydroxyaspartate dehydratase	-	Delftia sp. HT23

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Delftia sp. HT23

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Delftia sp. HT23

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	dependent on	Delftia sp. HT23

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)