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Literature summary for 3.1.8.1 extracted from
- Engineering and introduction of de novo disulphide bridges in organophosphorus hydrolase enzyme for thermostability improvement (2016), J. Biosci., 41, 577-588 .
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| A204C/T234C | site-directed mutagenesis, Ala204 and Thr234 are located on the alpha-helices and gamma turn, respectively, thermostability of the mutant enzyme is increased compared to the wild-type, due to increased rigidity | Brevundimonas diminuta |
| G74C/A78C | site-directed mutagenesis, Gly74 and Ala78 are located on the gamma turn and beta-turn, respectively, which link gamma turn and beta-turn adjacent together, thermostability of the mutant enzyme is decreased compared to the wild-type, due to increased flexibility | Brevundimonas diminuta |
| additional information | appropriate amino acid pairs for the introduction of disulfide bridge to improve protein thermostability are selected, engineering of de novo disulfide bridges is explored as a means to increase the thermal stability of enzymes in the rational method of protein engineering. Circular dichroism (CD) spectrometry and intrinsic fluorescence experiments are applied to evaluate the structural changes of mutants compared to the wild-type after introducing disulfide bridge | Brevundimonas diminuta |
| T128C/ E124C | site-directed mutagenesis, thermostability and kcat of the mutant enzyme are increased compared to the wild-type | Brevundimonas diminuta |
| T128C/ E153C | site-directed mutagenesis, Thr128 and Glu153 are located on the beta-sheet and alpha-helices, respectively, thermostability of the mutant enzyme is increased compared to the wild-type, due to increased rigidity | Brevundimonas diminuta |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | required, a metalloenzyme, the active site contains two divalent metal ions essential for its catalytic activity and also 6 amino acids, including four histidine, one aspartic acid and one lysine | Brevundimonas diminuta |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 72000 | - |
- |
Brevundimonas diminuta |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Brevundimonas diminuta | P0A434 | - |
- |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | each monomer includes eight strands of parallel beta-pleated sheets in a beta-barrel structure. Secondary structure analysis of wild-type and mutant enzymes, overview | Brevundimonas diminuta |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| OPH | - |
Brevundimonas diminuta |
| organophosphorus hydrolase | - |
Brevundimonas diminuta |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 65 | - |
60 min, the wild-type enzyme had a residual activity of 31%, the residual activities of enzyme mutants G74C/A78C, A204C/T234C, and T128C/E153C are 28%, 33%, and 46.36%, respectively | Brevundimonas diminuta |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | enzyme homology modeling and molecular dynamics simulations, overview. The active site contains two divalent metal ions essential for its catalytic activity and also 6 amino acids, including four histidine, one aspartic acid and one lysine. Disulfide bridge confirmation in the enzyme structure | Brevundimonas diminuta |
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Release 2023.1 (January 2023)
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