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Literature summary for 2.3.1.304 extracted from

  • Rehm, B.H.; Antonio, R.V.; Spiekermann, P.; Amara, A.A.; Steinbuchel, A.
    Molecular characterization of the poly(3-hydroxybutyrate) (PHB) synthase from Ralstonia eutropha: in vitro evolution, site-specific mutagenesis and development of a PHB synthase protein model (2002), Biochim. Biophys. Acta, 1594, 178-190.
    View publication on PubMed
Search for more literature for 2.3.1.304

Cloned(Commentary)

Cloned (Comment) Organism
mutant enzymes expressed in Escherichia coli Cupriavidus necator

Protein Variants

Protein Variants Comment Organism
A372_C382del no detectable activity Cupriavidus necator
C438G no detectable activity Cupriavidus necator
D281_D290del no detectable activity Cupriavidus necator
E267K 40% of wild-type activity Cupriavidus necator
E578_A589del no detectable activity Cupriavidus necator
L446K 15% of wild-type activity, no change in substrate specificity Cupriavidus necator
additional information fusion proteins composed of an N-terminal class II PHA synthase region (PhaCPa from Pseudomonas aeruginosa) and a C-terminal class I PHA synthase region (PhaCRe from Ralstonia eutropha) are constructed Cupriavidus necator
T231I no detectable activity Cupriavidus necator
T323S no detectable activity Cupriavidus necator
V585_A589del no detectable activity Cupriavidus necator
Y445F 38% of wild-type activity, no change in substrate specificity Cupriavidus necator

Organism

Organism UniProt Comment Textmining
Cupriavidus necator
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
-
 Cupriavidus necator [(R)-3-hydroxybutanoate](n+1) + CoA
-
 ?

Synonyms

Synonyms Comment Organism
class I PHA synthase
-
 Cupriavidus necator
poly(3-hydroxybutyrate) synthase
-
 Cupriavidus necator