EC Number | Cloned (Comment) | Organism |
---|---|---|
3.7.1.8 | BphD mutants expressed in a pET-14b vector as an N-terminal His6 fusion protein | Paraburkholderia xenovorans |
3.7.1.14 | - |
Escherichia coli |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.7.1.8 | H263 mutant by hanging drop vapor diffusion, to 2 A resolution | Escherichia coli |
3.7.1.14 | hanging drop vapor diffusion method, the X-ray structure of a succinate-H263A MhpC complex shows concerted movements in the positions of both Phe173 and Trp264 that line the approach to Arg188 | Escherichia coli |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.7.1.8 | C261A | 2fold decreased turnover rate, Cys-261 seems to be not involved in catalysis | Escherichia coli |
3.7.1.8 | F173D | 1.5fold increased Km value, 100fold decreased turnover rate | Escherichia coli |
3.7.1.8 | F173G | 8fold increased Km value, 3.5fold decreased turnover rate | Escherichia coli |
3.7.1.8 | H263A | overal structure similar, but asymmetry of the enzyme dimer more pronounced than for the native enzyme | Escherichia coli |
3.7.1.8 | N109A | similar Km value as wild-type, 200fold decreased turnover rate | Escherichia coli |
3.7.1.8 | N109H | similar Km value as wild-type, 350fold decreased turnover rate | Escherichia coli |
3.7.1.8 | R188K | 5fold increased Km value,35fold decreased turnover rate | Escherichia coli |
3.7.1.8 | R188Q | first step of enzyme reaction, keto-enol tautomerization, becomes rate-limiting, 11fold increased Km value, 300fold decreased turnover rate | Escherichia coli |
3.7.1.8 | R190K | similar Km value as wild-type, 700fold decreased turnover rate | Paraburkholderia xenovorans |
3.7.1.8 | R190Q | 14fold increased Km value, 400fold decreased turnover rate | Paraburkholderia xenovorans |
3.7.1.8 | W264G | 16fold increased Km value, 10fold decreased turnover rate | Escherichia coli |
3.7.1.14 | C261A | 1.4fold decrease in kcat/Km for (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | Escherichia coli |
3.7.1.14 | F173D | 158fold decrease in kcat/Km for (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | Escherichia coli |
3.7.1.14 | F173G | 32fold decrease in kcat/Km for (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | Escherichia coli |
3.7.1.14 | N109A | 125fold decrease in kcat/Km for (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | Escherichia coli |
3.7.1.14 | N109H | 217fold decrease in kcat/Km for (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | Escherichia coli |
3.7.1.14 | R188K | 217fold decrease in kcat/Km for (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | Escherichia coli |
3.7.1.14 | R188Q | 2941fold decrease in kcat/Km for (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | Escherichia coli |
3.7.1.14 | W264G | 196fold decrease in kcat/Km for (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.7.1.8 | 0.002 | - |
meta-ring fission intermediate | wild-type | Paraburkholderia xenovorans | |
3.7.1.8 | 0.002 | - |
meta-ring fission intermediate | R188K | Paraburkholderia xenovorans | |
3.7.1.8 | 0.004 | - |
meta-ring fission intermediate | N109A | Escherichia coli | |
3.7.1.8 | 0.004 | - |
meta-ring fission intermediate | N109H | Escherichia coli | |
3.7.1.8 | 0.0042 | - |
meta-ring fission intermediate | C261A | Escherichia coli | |
3.7.1.8 | 0.0068 | - |
meta-ring fission intermediate | wild-type | Escherichia coli | |
3.7.1.8 | 0.01 | - |
meta-ring fission intermediate | F173D | Escherichia coli | |
3.7.1.8 | 0.0282 | - |
meta-ring fission intermediate | R188Q | Paraburkholderia xenovorans | |
3.7.1.8 | 0.038 | - |
meta-ring fission intermediate | R188K | Escherichia coli | |
3.7.1.8 | 0.058 | - |
meta-ring fission intermediate | F173G | Escherichia coli | |
3.7.1.8 | 0.077 | - |
meta-ring fission intermediate | R188Q | Escherichia coli | |
3.7.1.14 | 0.004 | - |
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°C, mutant enzyme N109A | Escherichia coli | |
3.7.1.14 | 0.004 | - |
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°C, mutant enzyme N109H | Escherichia coli | |
3.7.1.14 | 0.0042 | - |
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°C, mutant enzyme C261A | Escherichia coli | |
3.7.1.14 | 0.0068 | - |
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°, wild-type enzyme | Escherichia coli | |
3.7.1.14 | 0.01 | - |
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°C, mutant enzyme F173D | Escherichia coli | |
3.7.1.14 | 0.038 | - |
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°C, mutant enzyme R188K | Escherichia coli | |
3.7.1.14 | 0.058 | - |
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°C, mutant enzyme F173G | Escherichia coli | |
3.7.1.14 | 0.077 | - |
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°C, mutant enzyme R188Q | Escherichia coli | |
3.7.1.14 | 0.125 | - |
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°C, mutant enzyme W264G | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.7.1.14 | (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate + H2O | Escherichia coli | the enzyme is involved in 3-phenylpropanoate catabolism | (2E)-2-hydroxypenta-2,4-dienoate + succinate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.7.1.8 | Escherichia coli | - |
- |
- |
3.7.1.8 | Paraburkholderia xenovorans | - |
LB400 | - |
3.7.1.14 | Escherichia coli | P77044 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.7.1.8 | BphD mutants purified by affinity chromatography to more than 95% homogeneity | Paraburkholderia xenovorans |
3.7.1.8 | MhpC mutants purified by anion exchange chromatography to more than 95% homogeneity | Escherichia coli |
3.7.1.14 | - |
Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.7.1.8 | meta-ring fission intermediate + H2O | catalysis of the hydrolytic C-C cleavage on biphenyl degradation pathway | Paraburkholderia xenovorans | ? | - |
? | |
3.7.1.8 | meta-ring fission intermediate + H2O | catalysis of the hydrolytic C-C cleavage on phenylpropionic acid pathway | Escherichia coli | ? | - |
? | |
3.7.1.14 | (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate + H2O | - |
Escherichia coli | (2E)-2-hydroxypenta-2,4-dienoate + succinate | - |
? | |
3.7.1.14 | (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate + H2O | the enzyme is involved in 3-phenylpropanoate catabolism | Escherichia coli | (2E)-2-hydroxypenta-2,4-dienoate + succinate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.7.1.8 | BphD | - |
Paraburkholderia xenovorans |
3.7.1.8 | MhpC | - |
Escherichia coli |
3.7.1.14 | 2-hydroxy-6-ketonona-2,4-diene-1,9-dioic acid 5,6-hydrolase | - |
Escherichia coli |
3.7.1.14 | MhpC | - |
Escherichia coli |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.7.1.14 | 25 | - |
assay at | Escherichia coli |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.7.1.8 | 0.009 | - |
meta-ring fission intermediate | R188K | Paraburkholderia xenovorans | |
3.7.1.8 | 0.016 | - |
meta-ring fission intermediate | R188Q | Paraburkholderia xenovorans | |
3.7.1.8 | 0.08 | - |
meta-ring fission intermediate | N109H | Escherichia coli | |
3.7.1.8 | 0.1 | - |
meta-ring fission intermediate | R188Q | Escherichia coli | |
3.7.1.8 | 0.13 | - |
meta-ring fission intermediate | N109A | Escherichia coli | |
3.7.1.8 | 0.26 | - |
meta-ring fission intermediate | F173D | Escherichia coli | |
3.7.1.8 | 0.74 | - |
meta-ring fission intermediate | R188K | Escherichia coli | |
3.7.1.8 | 2 | 8 | meta-ring fission intermediate | wild-type | Escherichia coli | |
3.7.1.8 | 6.5 | - |
meta-ring fission intermediate | wild-type | Paraburkholderia xenovorans | |
3.7.1.8 | 7.5 | - |
meta-ring fission intermediate | F173G | Escherichia coli | |
3.7.1.8 | 12 | - |
meta-ring fission intermediate | C261A | Escherichia coli | |
3.7.1.14 | 0.08 | - |
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°C, mutant enzyme N109H | Escherichia coli | |
3.7.1.14 | 0.1 | - |
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°C, mutant enzyme R188Q | Escherichia coli | |
3.7.1.14 | 0.13 | - |
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°C, mutant enzyme N109A | Escherichia coli | |
3.7.1.14 | 0.26 | - |
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°C, mutant enzyme F173D | Escherichia coli | |
3.7.1.14 | 0.74 | - |
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°C, mutant enzyme R188K | Escherichia coli | |
3.7.1.14 | 2 | 8 | (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°, wild-type enzyme | Escherichia coli | |
3.7.1.14 | 2.7 | - |
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°C, mutant enzyme W264G | Escherichia coli | |
3.7.1.14 | 7.5 | - |
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°C, mutant enzyme F173G | Escherichia coli | |
3.7.1.14 | 12 | - |
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°C, mutant enzyme C261A | Escherichia coli |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.7.1.14 | 8 | - |
assay at | Escherichia coli |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.7.1.14 | physiological function | the enzyme is involved in 3-phenylpropanoate catabolism | Escherichia coli |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.7.1.14 | 1.4 | - |
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°C, mutant enzyme R188Q | Escherichia coli | |
3.7.1.14 | 19 | - |
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°C, mutant enzyme N109H | Escherichia coli | |
3.7.1.14 | 19 | - |
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°C, mutant enzyme R188K | Escherichia coli | |
3.7.1.14 | 21 | - |
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°C, mutant enzyme W264G | Escherichia coli | |
3.7.1.14 | 26 | - |
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°C, mutant enzyme F173D | Escherichia coli | |
3.7.1.14 | 33 | - |
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°C, mutant enzyme N109A | Escherichia coli | |
3.7.1.14 | 130 | - |
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°C, mutant enzyme F173G | Escherichia coli | |
3.7.1.14 | 2900 | - |
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°C, mutant enzyme C261A | Escherichia coli | |
3.7.1.14 | 4118 | - |
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate | pH 8.0, 25°, wild-type enzyme | Escherichia coli |