EC Number | Application | Comment | Organism |
---|---|---|---|
4.2.1.51 | industry | overexpression of pheAfbr and/or wild-type aroF is helpful for the enhancement of the key enzymes in L-phenylalanine biosynthesis, which is an important prerequisite for improved production of L-phenylalanine with engineered strains | Escherichia coli |
EC Number | Cloned (Comment) | Organism |
---|---|---|
4.2.1.51 | expressed in different engineered Escherichia coli WSH-Z06 strains (pAP-B, pAP-B01, pAP-B02 and pAP-B03) | Escherichia coli |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
4.2.1.51 | T326P | mutant harboring pheAfbr retains more than 70% of CM and PDT activities even in the presence of 200 mM L-phenylalanine, has potential in overproduction of L-phenylalanine | Escherichia coli |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
4.2.1.51 | L-phenylalanine | feedback inhibition. PDT of Escherichia coli WSH-Z06 is almost completely inhibited by 10 mM L-phenylalanine (92.9% activity loss). PDT of Escherichia coli WSH-Z06 (pAP-B03) exhibits strong resistance to 200 mM L-phenylalanine, manifested by the high residual activities (10 mM L-phenylalanine with only 7.1% loss of activity) | Escherichia coli |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
4.2.1.51 | 43100 | - |
x * 43100, SDS-PAGE | Escherichia coli |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.2.1.51 | Escherichia coli | C7EXK8 | the enzyme possesses prephenate dehydratase (EC 4.2.1.51) and chorismate mutase activity (EC 5.4.99.5); K06 | - |
4.2.1.51 | Escherichia coli K06 | C7EXK8 | the enzyme possesses prephenate dehydratase (EC 4.2.1.51) and chorismate mutase activity (EC 5.4.99.5); K06 | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
4.2.1.51 | 3100 | - |
strain WSH-Z06 (pAP-B) | Escherichia coli |
4.2.1.51 | 18000 | - |
strain WSH-Z06 (pAP-B03) | Escherichia coli |
4.2.1.51 | 18600 | - |
strain WSH-Z06 (pAP-B01) | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.2.1.51 | prephenate | - |
Escherichia coli | phenylpyruvate + H2O + CO2 | - |
? | |
4.2.1.51 | prephenate | - |
Escherichia coli K06 | phenylpyruvate + H2O + CO2 | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.2.1.51 | ? | x * 43100, SDS-PAGE | Escherichia coli |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.2.1.51 | chorismate mutase-prephenate dehydratase | the enzyme also possesses chorismate mutase activity (EC 5.4.99.5) | Escherichia coli |
4.2.1.51 | CMPDT | the enzyme also possesses chorismate mutase activity (EC 5.4.99.5) | Escherichia coli |
4.2.1.51 | PheA | - |
Escherichia coli |
EC Number | General Information | Comment | Organism |
---|---|---|---|
4.2.1.51 | malfunction | use of a T326P mutation in the regulation domain of pheA (pheAfbr) for L-phenylalanine production. Overexpression of pheAfbr and/or wild-type aroF is helpful for the enhancement of the key enzymes in L-phenylalanine biosynthesis | Escherichia coli |