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Literature summary for 1.2.1.60 extracted from
- Carboxymethylhydroxymuconic semialdehyde dehydrogenase in the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli (1982), Biochim. Biophys. Acta, 719, 165-167.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| m-hydroxybenzaldehyde | - |
Escherichia coli |  |
| NADH | - |
Escherichia coli | |
| p-Hydroxybenzaldehyde | - |
Escherichia coli | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.006 | - |
5-carboxymethyl-2-hydroxymuconate semialdehyde | - |
Escherichia coli | |
| 0.052 | - |
NAD+ | - |
Escherichia coli | |
| 3.6 | - |
NADP+ | - |
Escherichia coli | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 58000 | - |
4 * 58000, SDS-PAGE | Escherichia coli |
| 210000 | - |
gel filtration | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+ | Escherichia coli | involved in the meta-cleavage pathway of 4-hydroxyphenylacetate | 5-carboxymethyl-2-hydroxymuconate + NADH | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| to homogeneity, chromatography techniques | Escherichia coli |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| cell culture | - |
Escherichia coli | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 54 | - |
- |
Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+ | involved in the meta-cleavage pathway of 4-hydroxyphenylacetate | Escherichia coli | 5-carboxymethyl-2-hydroxymuconate + NADH | - |
? | |
| 5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NADP+ | 11% of the activity compared to the reduction with NAD+ | Escherichia coli | 5-carboxymethyl-2-hydroxymuconate + NADPH | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| tetramer | 4 * 58000, SDS-PAGE | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.8 | - |
less active in Tris-HCl buffer than in phosphate or glycine/NaOH buffers | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | strict dependency for NAD+ reduction | Escherichia coli | |
| NADP+ | 89% lower activity compared to NAD+ | Escherichia coli | |
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Release 2023.1 (January 2023)
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