BRENDA - Enzyme Database
show all sequences of 3.1.1.102

Effect of hydrolysis products on the enzymatic degradation of polyethylene terephthalate nanoparticles by a polyester hydrolase from Thermobifida fusca

Barth, M.; Oeser, T.; Wei, R.; Then, J.; Schmidt, J.; Zimmermann, W.; Biochem. Eng. J. 93, 222-228 (2015)
No PubMed abstract available

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
bis(2-hydroxyethyl) terephthalic acid
competitive inhibition of the hydrolytic activity against PET nanoparticles
Thermobifida fusca
ethylene terephthalate
competitive inhibition of the hydrolytic activity against PET nanoparticles
Thermobifida fusca
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.9
-
bis(2-hydroxyethyl) terephthalic acid
pH 8.5, 60C
Thermobifida fusca
7.3
-
ethylene terephthalate
pH 8.5, 60C
Thermobifida fusca
Organism
Organism
UniProt
Commentary
Textmining
Thermobifida fusca
E5BBQ3
cf. EC 3.1.1.74
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
bis(2-hydroxyethyl) terephthalic acid + 2 H2O
-
737630
Thermobifida fusca
terephthalic acid + 2 ethylene glycol
-
-
-
?
ethylene terephthalate + H2O
-
737630
Thermobifida fusca
terephthalate + ethylene glycol
-
-
-
?
additional information
enzyme additionally catalyzes hydrolysis of poly(ethylene terephthalate), reaction of EC 3.1.1.101
737630
Thermobifida fusca
?
-
-
-
-
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.31
-
ethylene terephthalate
pH 8.5, 60C
Thermobifida fusca
26.8
-
bis(2-hydroxyethyl) terephthalic acid
pH 8.5, 60C
Thermobifida fusca
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
bis(2-hydroxyethyl) terephthalic acid
competitive inhibition of the hydrolytic activity against PET nanoparticles
Thermobifida fusca
ethylene terephthalate
competitive inhibition of the hydrolytic activity against PET nanoparticles
Thermobifida fusca
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.9
-
bis(2-hydroxyethyl) terephthalic acid
pH 8.5, 60C
Thermobifida fusca
7.3
-
ethylene terephthalate
pH 8.5, 60C
Thermobifida fusca
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
bis(2-hydroxyethyl) terephthalic acid + 2 H2O
-
737630
Thermobifida fusca
terephthalic acid + 2 ethylene glycol
-
-
-
?
ethylene terephthalate + H2O
-
737630
Thermobifida fusca
terephthalate + ethylene glycol
-
-
-
?
additional information
enzyme additionally catalyzes hydrolysis of poly(ethylene terephthalate), reaction of EC 3.1.1.101
737630
Thermobifida fusca
?
-
-
-
-
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.31
-
ethylene terephthalate
pH 8.5, 60C
Thermobifida fusca
26.8
-
bis(2-hydroxyethyl) terephthalic acid
pH 8.5, 60C
Thermobifida fusca
Other publictions for EC 3.1.1.102
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
739707
Yoshida
A bacterium that degrades and ...
Ideonella sakaiensis 201-F6, Ideonella sakaiensis
Science
351
1196-1199
2016
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737630
Barth
-
Effect of hydrolysis products ...
Thermobifida fusca
Biochem. Eng. J.
93
222-228
2015
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