B6db activities : 4_3_1

	Activities \| Families \| Sequences \| Fold types \| References \| Help


	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 (0)

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	Articles on 4.3.1.27

last changed	2017/09/06 11:22

Family