EC Number | Cloned (Comment) | Organism |
---|---|---|
3.7.1.9 | gene pheD encoded in the phe lower operon of the TOU catabolic pathway, DNA and amino acid sequence determination and analysis, genetic organization, recombinant expression in Escherichia coli strain JM109 | Pseudomonas sp. |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.7.1.9 | additional information | - |
additional information | steady-state kinetic analysis | Pseudomonas sp. | |
3.7.1.9 | 0.0164 | - |
2-hydroxy-6-oxohepta-2,4-dienoate | recombinant enzyme, pH 7.5, 25°C | Pseudomonas sp. | |
3.7.1.9 | 0.2315 | - |
2-hydroxy-5-methylmuconate-6-semialdehyde | recombinant enzyme, pH 7.5, 25°C | Pseudomonas sp. | |
3.7.1.9 | 0.232 | - |
2-hydroxymuconate-6-semialdehyde | recombinant enzyme, pH 7.5, 25°C | Pseudomonas sp. |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.7.1.9 | 30000 | - |
x * 30000, recombinant enzyme, SDS-PAGE, x * 31323.5, sequence calculation | Pseudomonas sp. |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.7.1.9 | 2-hydroxy-5-methylmuconate-6-semialdehyde + H2O | Pseudomonas sp. | - |
? | - |
? | |
3.7.1.9 | 2-hydroxy-5-methylmuconate-6-semialdehyde + H2O | Pseudomonas sp. OX1 | - |
? | - |
? | |
3.7.1.9 | 2-hydroxy-6-oxohepta-2,4-dienoate + H2O | Pseudomonas sp. | - |
formate + 2-oxopent-4-enoate | - |
? | |
3.7.1.9 | 2-hydroxy-6-oxohepta-2,4-dienoate + H2O | Pseudomonas sp. OX1 | - |
formate + 2-oxopent-4-enoate | - |
? | |
3.7.1.9 | 2-hydroxymuconate-6-semialdehyde + H2O | Pseudomonas sp. | - |
formate + 2-oxopent-4-enoate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.7.1.9 | Pseudomonas sp. | G3KFX4 | gene pheD encoded in the phe lower operon of the TOU catabolic pathway | - |
3.7.1.9 | Pseudomonas sp. OX1 | G3KFX4 | gene pheD encoded in the phe lower operon of the TOU catabolic pathway | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.7.1.9 | recombinant enzyme from Escherichia coli strain JM109 by anion exchange chromatography and gel filtration | Pseudomonas sp. |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.7.1.9 | 1.18 | - |
purified recombinant enzyme, substrate 2-hydroxy-5-methylmuconate-6-semialdehyde, pH 7.5, 25°C | Pseudomonas sp. |
3.7.1.9 | 3.87 | - |
purified recombinant enzyme, substrate 2-hydroxymuconate-6-semialdehyde, pH 7.5, 25°C | Pseudomonas sp. |
3.7.1.9 | 28.4 | - |
purified recombinant enzyme, substrate 2-hydroxy-6-oxohepta-2,4-dienoate, pH 7.5, 25°C | Pseudomonas sp. |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.7.1.9 | 2-hydroxy-5-methylmuconate-6-semialdehyde + H2O | - |
Pseudomonas sp. | ? | - |
? | |
3.7.1.9 | 2-hydroxy-5-methylmuconate-6-semialdehyde + H2O | prepared from 4-methylcatechol | Pseudomonas sp. | ? | - |
? | |
3.7.1.9 | 2-hydroxy-5-methylmuconate-6-semialdehyde + H2O | - |
Pseudomonas sp. OX1 | ? | - |
? | |
3.7.1.9 | 2-hydroxy-5-methylmuconate-6-semialdehyde + H2O | prepared from 4-methylcatechol | Pseudomonas sp. OX1 | ? | - |
? | |
3.7.1.9 | 2-hydroxy-6-oxohepta-2,4-dienoate + H2O | - |
Pseudomonas sp. | formate + 2-oxopent-4-enoate | - |
? | |
3.7.1.9 | 2-hydroxy-6-oxohepta-2,4-dienoate + H2O | prepared from 3-methylcatechol, best substrate | Pseudomonas sp. | formate + 2-oxopent-4-enoate | - |
? | |
3.7.1.9 | 2-hydroxy-6-oxohepta-2,4-dienoate + H2O | - |
Pseudomonas sp. OX1 | formate + 2-oxopent-4-enoate | - |
? | |
3.7.1.9 | 2-hydroxy-6-oxohepta-2,4-dienoate + H2O | prepared from 3-methylcatechol, best substrate | Pseudomonas sp. OX1 | formate + 2-oxopent-4-enoate | - |
? | |
3.7.1.9 | 2-hydroxymuconate-6-semialdehyde + H2O | - |
Pseudomonas sp. | formate + 2-oxopent-4-enoate | - |
? | |
3.7.1.9 | 2-hydroxymuconate-6-semialdehyde + H2O | prepared from catechol | Pseudomonas sp. | formate + 2-oxopent-4-enoate | - |
? | |
3.7.1.9 | additional information | the enzyme shows the ability to hydrolyze all the three ring cleavage products from catechols although with different efficiency | Pseudomonas sp. | ? | - |
? | |
3.7.1.9 | additional information | the enzyme shows the ability to hydrolyze all the three ring cleavage products from catechols although with different efficiency | Pseudomonas sp. OX1 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.7.1.9 | ? | x * 30000, recombinant enzyme, SDS-PAGE, x * 31323.5, sequence calculation | Pseudomonas sp. |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.7.1.9 | 2-hydroxymuconic semialdehyde hydrolase | - |
Pseudomonas sp. |
3.7.1.9 | HMSH | - |
Pseudomonas sp. |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.7.1.9 | 25 | - |
assay at | Pseudomonas sp. |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.7.1.9 | 1.15 | - |
2-hydroxy-5-methylmuconate-6-semialdehyde | recombinant enzyme, pH 7.5, 25°C | Pseudomonas sp. | |
3.7.1.9 | 18.2 | - |
2-hydroxymuconate-6-semialdehyde | recombinant enzyme, pH 7.5, 25°C | Pseudomonas sp. | |
3.7.1.9 | 36.53 | - |
2-hydroxy-6-oxohepta-2,4-dienoate | recombinant enzyme, pH 7.5, 25°C | Pseudomonas sp. |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.7.1.9 | 7.5 | - |
assay at | Pseudomonas sp. |
EC Number | Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|---|
3.7.1.9 | Pseudomonas sp. | sequence calculation | - |
5.93 |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.7.1.9 | evolution | DNA sequence analysis shows the gene order within the operons to be pheCDEFGHI (phe operon) and xyl-likeQKIH (xyl-like operon), identical to the order found for the isofunctional genes of meta operons in the toluene/xylene pathway of TOL plasmid pWW0 from Pseudomonas putida mt-2 and the phenol/methylphenol pathway of pVIl50 from Pseudomonas sp. CF600. The nucleotide and the deduced amino acid sequences are homologous to the equivalent gene and enzyme sequences from other Pseudomonas meta pathways, sequence analyses and homology studies | Pseudomonas sp. |
3.7.1.9 | metabolism | the hydrolytic branch of the TOU catabolic pathway involves direct formation of 2-hydroxypent-2,4-dienoate from the meta-cleavage product of catechol catalyzed by the enzyme. Catabolism of 3-methylcatechol and catechol through the hydrolytic branch and the oxalocrotonate branch, respectively, overview | Pseudomonas sp. |
3.7.1.9 | additional information | genetic analysis of the Pseudomonas sp. OX1 TOU meta pathway involving the enzyme | Pseudomonas sp. |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.7.1.9 | 50 | - |
2-hydroxy-5-methylmuconate-6-semialdehyde | recombinant enzyme, pH 7.5, 25°C | Pseudomonas sp. | |
3.7.1.9 | 780 | - |
2-hydroxymuconate-6-semialdehyde | recombinant enzyme, pH 7.5, 25°C | Pseudomonas sp. | |
3.7.1.9 | 2200 | - |
2-hydroxy-6-oxohepta-2,4-dienoate | recombinant enzyme, pH 7.5, 25°C | Pseudomonas sp. |