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Literature summary for 2.3.1.304 extracted from

  • Shozui, F.; Sun, J.; Song, Y.; Yamada, M.; Sakai, K.; Matsumoto, K.; Takase, K.; Taguchi, S.
    A new beneficial mutation in Pseudomonas sp. 61-3 polyhydroxyalkanoate (PHA) synthase for enhanced cellular content of 3-hydroxybutyrate-based PHA explored using its enzyme homolog as a mutation template (2010), Biosci. Biotechnol. Biochem., 74, 1710-1712.
    View publication on PubMed
Search for more literature for 2.3.1.304

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichai coli altering its content of polyhydroxyalkanoates Pseudomonas sp.
expression of wild-type and mutant enzymes in Escherichia coli altering its content of polyhydroxyalkanoates Pseudomonas sp.

Protein Variants

Protein Variants Comment Organism
Q481K site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase Pseudomonas sp.
Q481K/Q508L site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase Pseudomonas sp.
Q481M site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase Pseudomonas sp.
Q481M/Q508L site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase Pseudomonas sp.
Q481R site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase Pseudomonas sp.
Q481R/Q508L site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase Pseudomonas sp.
Q508L site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase Pseudomonas sp.
S325T site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase Pseudomonas sp.
S325T/Q508L site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase Pseudomonas sp.
S477R site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase Pseudomonas sp.
S477R/Q508L site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase Pseudomonas sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n Pseudomonas sp.
-
 [(R)-3-hydroxyacyl]n+1 + CoA
-
 ?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n Pseudomonas sp.
-
 [(R)-3-hydroxybutanoate]n+1 + CoA
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
-
 Pseudomonas sp. [(R)-3-hydroxyacyl]n+1 + CoA
-
 ?
3-hydroxybutyryl-CoA + [(R)-3-hydroxyacyl]n mutant enzymes Pseudomonas sp. [(R)-3-hydroxyacyl]n+1 + CoA
-
 ?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
-
 Pseudomonas sp. [(R)-3-hydroxybutanoate]n+1 + CoA
-
 ?
additional information the monomer composition of the wild-type cells contains more medium-chain length monomer in the PHAs, with highest content for 3-hydroxyoctanoate, overview. The enzyme mutants show a shift in substrate specificity and produce PHAs with a higher content of 3-hydroxybutanoate Pseudomonas sp. ?
-
 ?

Synonyms

Synonyms Comment Organism
class I PHA synthase
-
 Pseudomonas sp.
class II PHA synthase
-
 Pseudomonas sp.
PHA synthase 1
-
 Pseudomonas sp.
polyhydroxyalkanoate synthase
-
 Pseudomonas sp.
type I PHA synthase
-
 Pseudomonas sp.
type II PHA synthase
-
 Pseudomonas sp.