Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.3.1.16 extracted from

  • Matsumoto, Y.; Yasutake, Y.; Takeda, Y.; Tamura, T.; Yokota, A.; Wada, M.
    Crystallization and preliminary X-ray diffraction studies of D-threo-3-hydroxyaspartate dehydratase isolated from Delftia sp. HT23 (2013), Acta Crystallogr. Sect. F, 69, 1131-1134.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.3.1.16

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of recombinant D-THA DH is carried out using a Rhodococcus erythropolis expression system Delftia sp.

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals of D-THA DH belong to space group I4(1)22, with unit-cell parameters a = b = 157.3, c = 157.9 A. Single wavelength anomalous diffraction data are collected to a resolution of 2.0 A Delftia sp.

Organism

Organism UniProt Comment Textmining
Delftia sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Delftia sp.

Synonyms

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