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

BRENDA support

Literature summary extracted from

  • Jia, Y.; Yuan, W.; Wodzinska, J.; Park, C.; Sinskey, A.J.; Stubbe, J.
    Mechanistic studies on class I polyhydroxybutyrate (PHB) synthase from Ralstonia eutropha: class I and III synthases share a similar catalytic mechanism (2001), Biochemistry, 40, 1011-1019.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.304 C319A less than 0.0005% of the wild-type activity Cupriavidus necator
2.3.1.304 D480N 0.004% of the wild-type activity Cupriavidus necator
2.3.1.304 H481Q 20% of the wild-type activity Cupriavidus necator
2.3.1.304 H508Q less than 0.0005% of the wild-type activity Cupriavidus necator

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.304 Cupriavidus necator
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.304 3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n Ralstonia eutropha synthase possesses an essential catalytic dyad (C319-H508) in which the C319 is involved in covalent catalysis. A conserved Asp, D480, is not required for acylation of C319 by sT-CoA and is proposed to function as a general base catalyst to activate the hydroxyl of HBCoA for ester formation Cupriavidus necator [(R)-3-hydroxybutanoate](n+1) + CoA
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.304 dimer it is suggested that a dimeric form of the enzyme is involved in elongation Cupriavidus necator

Synonyms

EC Number Synonyms Comment Organism
2.3.1.304 class I polyhydroxybutyrate synthase
-
 Cupriavidus necator