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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.
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.
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. (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 2014/02/24 11:57

B6db activities