Activities | Families | Sequences | Fold types | References | Help
B6db activities: 4.3.1.27

4.3.1.27
Description Threo-3-hydroxy-D-aspartate ammonia-lyase
Alternative names D-threo-3-hydroxyaspartate dehydratase;
threo-3-hydroxy-D-aspartate ammonia-lyase (oxaloacetate-forming)
Catalyzed reaction threo-3-hydroxy-D-aspartate = oxaloacetate + NH3
Cofactor Pyridoxal-phosphate and Mn(II).
Comments A pyridoxal-phosphate protein. The enzyme, purified from the bacterium Delftia sp. HT23, also has activity against L-threo-3-hydroxyaspartate, L-erythro-3-hydroxyaspartate, and D-serine.
Different from EC 4.3.1.20, erythro-3-hydroxy-L-aspartate ammonia-lyase and EC4.3.1.16, threo-3-hydroxy-L-aspartate ammonia-lyase.

Requires a divalent cation such as Mn2+, Co2+ or Ni2+.

D-threo-3-Hydroxyaspartate dehydratase (D-THA DH) isolated from the soil bacterium Delftia sp. The amino-acid sequence of D-THA DH shows significant similarity to that of two eukaryotic D-serine dehydratases derived from Saccharomyces cerevisiae and chicken kidney. D-THA DH is classified into the fold-type III group of pyridoxal enzymes and is the first example of a fold-type III dehydratase derived from a prokaryote.
PDB 4PB5;
Organisms -Eubacteria
 

Family 

4.3.1.27 (11)
 
Links Enzyme (activities) 4.3.1.27
BRENDA (activities) 4.3.1.27
KEGG (pathways) 4.3.1.27
PLPMDB (PLP mutants) 4.3.1.27
 
References
 Matsumoto, Y.; Yasutake, Y.; Takeda, Y.; Tamura, T.; Yokota, A.; Wada, M. (2015) 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 Appl Microbiol Biotechnol 99 7137-50.

 Matsumoto Y, Yasutake Y, Takeda Y, Tamura T, Yokota A, Wada M. (2013) Crystallization and preliminary X-ray diffraction studies of D-threo-3-hydroxyaspartate dehydratase isolated from Delftia sp. HT23. Acta Crystallogr Sect F Struct Biol Cryst Commun 69 1131-4.

 Maeda T, Takeda Y, Murakami T, Yokota A, Wada M. (2010) Purification, characterization and amino acid sequence of a novel enzyme, D-threo-3-hydroxyaspartatedehydratase, from Delftia sp. HT23 J Biochem 148 705-12.

Articles on 4.3.1.27
 
last changed 2017/09/06 11:22

B6db activities