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Literature summary for 3.5.2.2 extracted from
- Simultaneous purification and immobilization of D-hydantoinase on the immobilized metal affinity membrane via coordination bonds (2012), Biochem. Eng. J., 61, 20-27.
No PubMed abstract available
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | the D-hydantoinase is an important enzyme capable of a reversible enantioselective ring-opening hydrolysis of hydantoins being applied for the efficient production of D-form amino acids which are key compounds applicable for the production of antibiotics, peptide hormones, pyrethroids, and pesticides in industry | Brevibacillus agri |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene pydB, recombinant expression of poly-His tagged enzyme in Escherichia coli | Brevibacillus agri |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | immobilization of the purified recombinant enzyme on N-carbamoyl-D-4-hydroxyphenylglycine in batch reactions, method optimization: 0.155 mM enzyme/disc, in 0.1 M Tris-HCl, pH 8, and 0.8 M sodium chloride, 14 h, overview. 99% enzyme activity remains after 15 reaction cycles. The immobilized DHTase membrane can achieve a larger pH and thermal tolerant range than that of free enzyme | Brevibacillus agri |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | eight Zn ions are located in DHTase tetramer active sites, the enzyme is highly dependent on metal ions for activity | Brevibacillus agri |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 57000 | - |
about | Brevibacillus agri |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5-(4-hydroxyphenyl) hydantoin + H2O | Brevibacillus agri | - |
N-carbamoyl-D-4-hydroxyphenylglycine | - |
? | |
| 5-(4-hydroxyphenyl) hydantoin + H2O | Brevibacillus agri NCHU1002 | - |
N-carbamoyl-D-4-hydroxyphenylglycine | - |
? | |
| additional information | Brevibacillus agri | the Brevibacillus agri strain NCHU1002 can perform the ring opening reaction of D,L-5-monosubstituted hydantoins stereoselectively to N-carbamoyl-D-amino acids. No L-form amino acid are formed in the reaction, analysis via the chiral HPLC | ? | - |
? | |
| additional information | Brevibacillus agri NCHU1002 | the Brevibacillus agri strain NCHU1002 can perform the ring opening reaction of D,L-5-monosubstituted hydantoins stereoselectively to N-carbamoyl-D-amino acids. No L-form amino acid are formed in the reaction, analysis via the chiral HPLC | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Brevibacillus agri | Q846U5 | gene pydB | - |
| Brevibacillus agri NCHU1002 | Q846U5 | gene pydB | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His tagged enzyme 28.94fold from Escherichia coli by nickel affinity chromatography | Brevibacillus agri |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 5.79 | - |
purified recombinant His-tagged enzyme, pH 8.0, 50°C | Brevibacillus agri |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5-(4-hydroxyphenyl) hydantoin + H2O | - |
Brevibacillus agri | N-carbamoyl-D-4-hydroxyphenylglycine | - |
? | |
| 5-(4-hydroxyphenyl) hydantoin + H2O | - |
Brevibacillus agri NCHU1002 | N-carbamoyl-D-4-hydroxyphenylglycine | - |
? | |
| additional information | the Brevibacillus agri strain NCHU1002 can perform the ring opening reaction of D,L-5-monosubstituted hydantoins stereoselectively to N-carbamoyl-D-amino acids. No L-form amino acid are formed in the reaction, analysis via the chiral HPLC | Brevibacillus agri | ? | - |
? | |
| additional information | the Brevibacillus agri strain NCHU1002 can perform the ring opening reaction of D,L-5-monosubstituted hydantoins stereoselectively to N-carbamoyl-D-amino acids. No L-form amino acid are formed in the reaction, analysis via the chiral HPLC | Brevibacillus agri NCHU1002 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| tetramer | - |
Brevibacillus agri |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| D-hydantoin-hydrolyzing enzyme | - |
Brevibacillus agri |
| D-hydantoinase | - |
Brevibacillus agri |
| DHTase | - |
Brevibacillus agri |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
free recombinant enzyme | Brevibacillus agri |
| 70 | - |
immobilized recombinant enzyme | Brevibacillus agri |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 10 | 80 | activity range, profile overview | Brevibacillus agri |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
free recombinant enzyme | Brevibacillus agri |
| 9 | - |
immobilized recombinant enzyme | Brevibacillus agri |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 10 | activity range, profile overview | Brevibacillus agri |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | te enzyme belongs to the urease family | Brevibacillus agri |
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