View in Gene3D

CATH Superfamily 2.40.37.20

D-serine dehydratase-like domain

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
D-serine dehydratase-like domain
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
« Back to all FunFams

FunFam 1: D-3-hydroxyaspartate aldolase

There are 2 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
D-threonine aldolase. [EC: 4.1.2.42]
(1) D-threonine = glycine + acetaldehyde. (2) D-allothreonine = glycine + acetaldehyde.
  • Activated by divalent metal cations (e.g. Co(2+), Ni(2+), Mn(2+) or Mg(2+)).
  • The reaction is reversible, which can lead to the interconversion of D-threonine and D-allothreonine.
  • Several other D-beta-hydroxy-alpha-amino acids, such as D-beta- phenylserine, D-beta-hydroxy-alpha-aminovaleric acid and D-beta-3,4- dihydroxyphenylserine, can also act as substrate.
 1 O82872
3-hydroxy-D-aspartate aldolase. [EC: 4.1.3.41]
(1) Threo-3-hydroxy-D-aspartate = glycine + glyoxylate. (2) D-erythro-3-hydroxyaspartate = glycine + glyoxylate.
  • The enzyme, purified from the bacterium Paracoccus denitrificansy IFO 13301, is strictly D-specific as to the alpha-position of the substrate, but accepts both the threo and erythro forms at the beta- position.
  • The erythro form is a far better substrate (about 100 fold).
  • The enzyme can also accept D-allothreonine, D-threonine, erythro-3- phenyl-D-serine and threo-3-phenyl-D-serine.
  • Different from EC 4.1.3.14.
  • Requires a divalent cation, such as Mg(2+), Mn(2+) or Co(2+).
 1 Q8GRC8