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Literature summary for 3.1.2.2 extracted from

  • Lee, L.; Liaw, Y.; Lee, Y.; Shaw, J.
    Enhanced preference for pi-bond containing substrates is correlated to Pro110 in the substrate-binding tunnel of Escherichia coli thioesterase I/protease I/lysophospholipase L1 (2007), Biochim. Biophys. Acta, 1774, 959-967.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
L109P mutation shifts the substrate-preference from medium-to-long acyl chains to shorter acyl-chains of triglyceride and p-nitrophenyl ester, and increases the preference for aromatic-amino acid-derived esters. kcat for lauroyl-CoA is 17.8fold lower than wild-type value, Km-value for lauroyl-CoA is 1.3fold higher than wild-type value Escherichia coli
P110A kcat for lauroyl-CoA is 2.7fold lower than wild-type value, Km-value for lauroyl-CoA is 1.3fold lower than wild-type value Escherichia coli
P110A/L109P kcat for lauroyl-CoA is 12fold lower than wild-type value, Km-value for lauroyl-CoA is 2fold lower than wild-type value Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.073
-
lauroyl-CoA mutant enzyme P110A/L109P Escherichia coli
0.113
-
lauroyl-CoA mutant enzyme P110A Escherichia coli
0.146
-
lauroyl-CoA native enzyme Escherichia coli
0.185
-
lauroyl-CoA mutant enzyme L109P Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0ADA1
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
lauroyl-CoA + H2O
-
Escherichia coli CoA + laurate
-
?
stearoyl-CoA + H2O
-
Escherichia coli CoA + stearate
-
?

Synonyms

Synonyms Comment Organism
thioesterase I/protease I/lysophospholipase L1 multifunctional enzyme with thioesterase, esterase, arylesterase, protease and lysophospholipase activities Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.052 2.1 lauroyl-CoA native enzyme Escherichia coli
0.57
-
lauroyl-CoA mutant enzyme L109P Escherichia coli
0.84
-
lauroyl-CoA mutant enzyme P110A/L109P Escherichia coli
3.8
-
lauroyl-CoA mutant enzyme P110A Escherichia coli
10.13
-
lauroyl-CoA native enzyme Escherichia coli