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Literature summary extracted from

  • Bertini, L.; Cafaro, V.; Proietti, S.; Caporale, C.; Capasso, P.; Caruso, C.; Di Donato, A.
    Deepening TOL and TOU catabolic pathways of Pseudomonas sp. OX1: cloning, sequencing and characterization of the lower pathways (2013), Biochimie, 95, 241-250.
    View publication on PubMed

Cloned(Commentary)

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.

KM Value [mM]

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.

Molecular Weight [Da]

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.

Natural Substrates/ Products (Substrates)

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
-
 ?

Organism

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
-

Purification (Commentary)

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.

Specific Activity [micromol/min/mg]

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.

Substrates and Products (Substrate)

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 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.7.1.9 ? x * 30000, recombinant enzyme, SDS-PAGE, x * 31323.5, sequence calculation Pseudomonas sp.

Synonyms

EC Number Synonyms Comment Organism
3.7.1.9 2-hydroxymuconic semialdehyde hydrolase
-
 Pseudomonas sp.
3.7.1.9 HMSH
-
 Pseudomonas sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.7.1.9 25
-
 assay at Pseudomonas sp.

Turnover Number [1/s]

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.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.7.1.9 7.5
-
 assay at Pseudomonas sp.

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.7.1.9 Pseudomonas sp. sequence calculation
-
 5.93

General Information

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.

kcat/KM [mM/s]

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.