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Literature summary extracted from

  • Alonso, J.M.; Garrido-Pertierra, A.
    Carboxymethylhydroxymuconic semialdehyde dehydrogenase in the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli (1982), Biochim. Biophys. Acta, 719, 165-167.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.60 m-hydroxybenzaldehyde
-
 Escherichia coli
1.2.1.60 NADH
-
 Escherichia coli
1.2.1.60 p-Hydroxybenzaldehyde
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.60 0.006
-
 5-carboxymethyl-2-hydroxymuconate semialdehyde
-
 Escherichia coli
1.2.1.60 0.052
-
 NAD+
-
 Escherichia coli
1.2.1.60 3.6
-
 NADP+
-
 Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.60 58000
-
 4 * 58000, SDS-PAGE Escherichia coli
1.2.1.60 210000
-
 gel filtration Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.60 5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+ Escherichia coli involved in the meta-cleavage pathway of 4-hydroxyphenylacetate 5-carboxymethyl-2-hydroxymuconate + NADH
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.60 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.60 to homogeneity, chromatography techniques Escherichia coli

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.2.1.60 cell culture
-
 Escherichia coli
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.2.1.60 54
-
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.60 5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+ involved in the meta-cleavage pathway of 4-hydroxyphenylacetate Escherichia coli 5-carboxymethyl-2-hydroxymuconate + NADH
-
 ?
1.2.1.60 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

EC Number Subunits Comment Organism
1.2.1.60 tetramer 4 * 58000, SDS-PAGE Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.60 7.8
-
 less active in Tris-HCl buffer than in phosphate or glycine/NaOH buffers Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.60 NAD+ strict dependency for NAD+ reduction Escherichia coli
1.2.1.60 NADP+ 89% lower activity compared to NAD+ Escherichia coli