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

BRENDA support

Literature summary for 2.3.1.304 extracted from

  • Matsumoto, K.; Aoki, E.; Takase, K.; Doi, Y.; Taguchi, S.
    In vivo and in vitro characterization of Ser477X mutations in polyhydroxyalkanoate (PHA) synthase 1 from Pseudomonas sp. 61-3 effects of beneficial mutations on enzymatic activity, substrate specificity, and molecular weight of PHA (2006), Biomacromolecules, 7, 2436-2442 .
    View publication on PubMed
Search for more literature for 2.3.1.304

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli JM109 cells Pseudomonas sp. 61-3

Protein Variants

Protein Variants Comment Organism
E130D/S477R the double mutant exhibits synergistic effects on both an increase in polyhydroxyalkanoate production (from 9 wt % to 27 wt %) and an alteration of substrate specificity Pseudomonas sp. 61-3
S325C/S477R the double mutant exhibits synergistic effects on both an increase in polyhydroxyalkanoate production (from 9 wt % to 21 wt %) and an alteration of substrate specificity Pseudomonas sp. 61-3
S325T/S477R the double mutant exhibits synergistic effects on both an increase in polyhydroxyalkanoate production (from 9 wt % to 17 wt %) and an alteration of substrate specificity Pseudomonas sp. 61-3
S477A the mutation results in a shift in substrate specificity to smaller monomer units Pseudomonas sp. 61-3
S477F the mutation results in a shift in substrate specificity to smaller monomer units Pseudomonas sp. 61-3
S477G the mutation greatly enhances activity toward all different sizes of substrates with carbon numbers ranging from 4 to 12 Pseudomonas sp. 61-3
S477H the mutation results in a shift in substrate specificity to smaller monomer units Pseudomonas sp. 61-3
S477R the mutation contributes to a shift in substrate specificity to smaller monomers containing a 3-hydroxybutyrate unit rather than to an enhancement in catalytic activity Pseudomonas sp. 61-3
S477R the mutation results in a shift in substrate specificity to smaller monomer units Pseudomonas sp. 61-3
S477R/Q481K the double mutant exhibits synergistic effects on both a decrease in polyhydroxyalkanoate production (from 9 wt % to 1 wt %) and an alteration of substrate specificity Pseudomonas sp. 61-3
S477R/Q481M the double mutant exhibits synergistic effects on both a decrease in polyhydroxyalkanoate production (from 9 wt % to 6 wt %) and an alteration of substrate specificity Pseudomonas sp. 61-3
S477R/Q481R the double mutant exhibits synergistic effects on both a decrease in polyhydroxyalkanoate production (from 9 wt % to 0.2 wt %) and an alteration of substrate specificity Pseudomonas sp. 61-3
S477Y the mutation results in a shift in substrate specificity to smaller monomer units Pseudomonas sp. 61-3

Organism

Organism UniProt Comment Textmining
Pseudomonas sp. 61-3
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyalkanoate]
-
 Pseudomonas sp. 61-3 CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyalkanoate]
-
 ?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
-
 Pseudomonas sp. 61-3 CoA + poly[(R)-3-hydroxybutyrate]n+1
-
 ?

Synonyms

Synonyms Comment Organism
PHA synthase 1
-
 Pseudomonas sp. 61-3
polyhydroxyalkanoate synthase 1
-
 Pseudomonas sp. 61-3