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Literature summary for 3.7.1.9 extracted from

  • Diaz, E.; Timmis, K.N.
    Identification of functional residues in a 2-hydroxymuconic semialdehyde hydrolase. A new member of the alpha/beta hydrolase-fold family of enzymes which cleaves carbon-carbon bonds (1995), J. Biol. Chem., 270, 6403-6411.
    View publication on PubMed
Search for more literature for 3.7.1.9

Protein Variants

Protein Variants Comment Organism
C254S 1% of the activity of wild-type enzyme, expressed at lower levels than the other mutant enzymes Pseudomonas putida
D228A activity below detection Pseudomonas putida
D65V activity below detection. Unstable, decreases in cellular extrects after 10 min Pseudomonas putida
F108M 18% of the activity of wild-type enzyme, enzyme displays greater thermostability than the wild-type enzyme Pseudomonas putida
H249A 26% of the activity of wild-type enzyme, expressed at lower levels than the other mutant enzymes, severe decrease in protein stability compared to wild-type enzyme Pseudomonas putida
H256A activity below detection Pseudomonas putida
H36A 15% of the activity of wild-type enzyme, severe decrease in protein stability over that of the wild-type enzyme Pseudomonas putida
S107A activity below detection Pseudomonas putida
S107C 0.44% of the activity of wild-type enzyme Pseudomonas putida
S152A 80% of the activity of wild-type enzyme, severe decrease in protein stability over that of the wild-type enzyme Pseudomonas putida

Inhibitors

Inhibitors Comment Organism Structure
3,4-dichloroisocoumarin
-
 Pseudomonas putida
diethyl dicarbonate
-
 Pseudomonas putida
diisopropyl fluorophosphate
-
 Pseudomonas putida
NEM
-
 Pseudomonas putida
phenylmethylsulfonyl fluoride
-
 Pseudomonas putida
tosyl-Phe chloromethyl ketone
-
 Pseudomonas putida

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0075
-
 3-methylcatechol ring-fission product mutant F108M Pseudomonas putida
0.0076
-
 3-methylcatechol ring-fission product mutant S152A Pseudomonas putida
0.0134
-
 3-methylcatechol ring-fission product mutant H249A Pseudomonas putida
0.0136
-
 3-methylcatechol ring-fission product
-
 Pseudomonas putida
0.023
-
 3-methylcatechol ring-fission product mutant H36A Pseudomonas putida
0.085
-
 catechol ring-fission product
-
 Pseudomonas putida
0.14
-
 catechol ring-fission product mutant H36A Pseudomonas putida
0.155
-
 catechol ring-fission product mutant S152A Pseudomonas putida
0.231
-
 catechol ring-fission product mutant H249A Pseudomonas putida
0.35
-
 catechol ring-fission product mutant F108M Pseudomonas putida

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Pseudomonas putida enzyme of the hydrolytic branch of the meta-cleavage pathway for the catabolism of catechol and alkyl-substituted catechols ?
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-methylcatechol ring-fission product + H2O
-
 Pseudomonas putida ?
-
 ?
catechol ring-fission product + H2O
-
 Pseudomonas putida ?
-
 ?
additional information enzyme of the hydrolytic branch of the meta-cleavage pathway for the catabolism of catechol and alkyl-substituted catechols Pseudomonas putida ?
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
42
-
 wild-type enzyme loses 50% of its activity after 15 min, mutant enzyme H36A loses 50% of its initial activity after 1.6 min, mutant enzyme F108M loses 60% of its initial activity after 60 min, mutant enzyme S152A loses 50% of its initial activity after 2.2 min, mutant enzyme H249A loses 50% of its initial activity after 1.1 min Pseudomonas putida