EC Number | Cloned (Comment) | Organism |
---|---|---|
2.3.1.304 | expression of wild-type and mutant enzymes in Escherichai coli altering its content of polyhydroxyalkanoates | Pseudomonas sp. |
2.3.1.304 | expression of wild-type and mutant enzymes in Escherichia coli altering its content of polyhydroxyalkanoates | Pseudomonas sp. |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.3.1.304 | 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. |
2.3.1.304 | 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. |
2.3.1.304 | 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. |
2.3.1.304 | 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. |
2.3.1.304 | 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. |
2.3.1.304 | 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. |
2.3.1.304 | 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. |
2.3.1.304 | 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. |
2.3.1.304 | 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. |
2.3.1.304 | 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. |
2.3.1.304 | 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. |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.304 | 3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n | Pseudomonas sp. | - |
[(R)-3-hydroxyacyl]n+1 + CoA | - |
? | |
2.3.1.304 | 3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n | Pseudomonas sp. | - |
[(R)-3-hydroxybutanoate]n+1 + CoA | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.1.304 | Pseudomonas sp. | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.304 | 3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n | - |
Pseudomonas sp. | [(R)-3-hydroxyacyl]n+1 + CoA | - |
? | |
2.3.1.304 | 3-hydroxybutyryl-CoA + [(R)-3-hydroxyacyl]n | mutant enzymes | Pseudomonas sp. | [(R)-3-hydroxyacyl]n+1 + CoA | - |
? | |
2.3.1.304 | 3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n | - |
Pseudomonas sp. | [(R)-3-hydroxybutanoate]n+1 + CoA | - |
? | |
2.3.1.304 | 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. | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.1.304 | class I PHA synthase | - |
Pseudomonas sp. |
2.3.1.304 | class II PHA synthase | - |
Pseudomonas sp. |
2.3.1.304 | PHA synthase 1 | - |
Pseudomonas sp. |
2.3.1.304 | polyhydroxyalkanoate synthase | - |
Pseudomonas sp. |
2.3.1.304 | type I PHA synthase | - |
Pseudomonas sp. |
2.3.1.304 | type II PHA synthase | - |
Pseudomonas sp. |