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Literature summary extracted from
- Biochemical analysis and kinetic modeling of the thermal inactivation of MBP-fused heparinase I: implications for a comprehensive thermostabilization strategy (2011), Biotechnol. Bioeng., 108, 1841-1851.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.2.2.8 | expression of maltose-binding protein fusion HepI, MBP-HepI, in Escherichia coli | Pedobacter heparinus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 4.2.2.8 | C297S | site-directed mutagenesis, the mutant suppresses the dimerization and shows 70% reduced activity compared to the wild-type enzyme | Pedobacter heparinus |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 4.2.2.8 | after freeze-thawing, 97% of maximal activity remains | Pedobacter heparinus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.2.8 | alpha-lactose | - |
Pedobacter heparinus |  |
| 4.2.2.8 | Ca2+ | - |
Pedobacter heparinus | |
| 4.2.2.8 | Dextran | - |
Pedobacter heparinus | |
| 4.2.2.8 | DTT | suppresses the dimerization | Pedobacter heparinus | |
| 4.2.2.8 | glycerol | - |
Pedobacter heparinus | |
| 4.2.2.8 | PEG 20000 | - |
Pedobacter heparinus | |
| 4.2.2.8 | PEG 8000 | - |
Pedobacter heparinus | |
| 4.2.2.8 | sucrose | - |
Pedobacter heparinus | |
| 4.2.2.8 | trehalose | - |
Pedobacter heparinus | |
| 4.2.2.8 | Triton X-100 | - |
Pedobacter heparinus | |
| 4.2.2.8 | Tween 80 | - |
Pedobacter heparinus | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.2.2.8 | additional information | - |
additional information | kinetic modeling based on inactivation data, overview | Pedobacter heparinus |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.2.8 | Ca2+ | activates | Pedobacter heparinus | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.2.2.8 | Pedobacter heparinus | - |
formerly Flavobacterium heparinum | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.2.2.8 | recombinant maltose-binding protein fusion HepI, MBP-HepI, from Escherichia coli by affinity and anion exchange chromatography, followed by gel filtration to apparent homogeneity | Pedobacter heparinus |
Renatured (Commentary)
| EC Number | Renatured (Comment) | Organism |
|---|---|---|
| 4.2.2.8 | temperature-induced reactivation of MBP-HepI, when the temperature is lowered from 35°C to 4°C, the rate constant of unfolding decreases by 6000times while that of refolding decreases by only 600times, MBP-HepI undergoes reactivation during the cooling treatment at 4°C after incubation at 35°C | Pedobacter heparinus |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 4.2.2.8 | 149 | - |
purified recombinant HepI, pH 7.5, 30°C | Pedobacter heparinus |
Storage Stability
| EC Number | Storage Stability | Organism |
|---|---|---|
| 4.2.2.8 | 4°C, purified recombinant MBP-HEPI, 1 week, 95% remaining activity | Pedobacter heparinus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.2.8 | additional information | cleavage/degradation of heparin forming unsaturated uronic acid | Pedobacter heparinus | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.2.2.8 | More | three-dimensional model structure, modelling based on the known crystal structure of Bacteroides thetaiotaomicron HepI, overview | Pedobacter heparinus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.2.2.8 | heparinase I | - |
Pedobacter heparinus |
| 4.2.2.8 | HepI | - |
Pedobacter heparinus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.2.2.8 | 30 | - |
- |
Pedobacter heparinus |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.2.2.8 | additional information | - |
the inactivation shows strong concentration dependence. Acceleration of the inactivation with the increase of enzyme concentration implies multi-molecular interactions in the thermal inactivation. Strong reversibility of the unfolding of MBP-HepI, overview | Pedobacter heparinus |
| 4.2.2.8 | 30 | - |
purified recombinant enzyme, half-life is 160 min | Pedobacter heparinus |
| 4.2.2.8 | 70 | - |
purified recombinant enzyme, loss of 97% activity within 1 min | Pedobacter heparinus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.2.2.8 | 7.5 | - |
assay at | Pedobacter heparinus |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 4.2.2.8 | additional information | intermolecular disulfide bond formation in HepI important for catalysis, overview | Pedobacter heparinus |
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