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Literature summary for 3.1.1.47 extracted from
- The functional implications of the dimerization of the catalytic subunits of the mammalian brain platelet-activating factor acetylhydrolase (Ib) (2000), Protein Eng., 13, 865-871.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of the catalytic subunit alpha1-homodimer and alpha1-alpha2-heterodimer in Escherichia coli as GST-fusion protein, expression of wild-type and mutant enzymes as GST-fusion proteins in Escherichia coli | Bos taurus |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| purified recombinant R22K mutant, X-ray structure determination at 1.2 A resolution | Bos taurus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D20N | site-directed mutagenesis, mutant is not efficiently expressed | Bos taurus |
| D20R | site-directed mutagenesis, mutant is not efficiently expressed | Bos taurus |
| L194A | site-directed mutagenesis, decreased Km and Vmax compared to the wild-type enzyme | Bos taurus |
| L26A | site-directed mutagenesis, 60% reduced activity compared to the wild-type enzyme | Bos taurus |
| L48A | site-directed mutagenesis, decreased Km and Vmax compared to the wild-type enzyme | Bos taurus |
| R22E | site-directed mutagenesis, mutant is not efficiently expressed | Bos taurus |
| R22K | site-directed mutagenesis, inactive mutant | Bos taurus |
| R29K | site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme | Bos taurus |
| T103S | site-directed mutagenesis, decreased Km and Vmax compared to the wild-type enzyme | Bos taurus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics | Bos taurus | |
| 0.082 | - |
acetylated platelet-activation factor | mutant T103S, pH 7.4, 37°C | Bos taurus | |
| 0.092 | - |
acetylated platelet-activation factor | mutant L48A, pH 7.4, 37°C | Bos taurus | |
| 0.135 | - |
acetylated platelet-activation factor | mutant L194A, pH 7.4, 37°C | Bos taurus | |
| 0.206 | - |
acetylated platelet-activation factor | wild-type enzyme, pH 7.4, 37°C | Bos taurus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | influences the dimerization of the enzyme | Bos taurus |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 26000 | - |
isozyme Ib, 2 * 26000, subunits alpha1 and/or subunit alpha2, + 1 * 45000, beta-subunit | Bos taurus |
| 45000 | - |
isozyme Ib, 2 * 26000, subunits alpha1 and/or subunit alpha2, + 1 * 45000, beta-subunit | Bos taurus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
isoform Ib | - |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate | Arg29 and Arg22 in the one monomer contribute to the catalytic competence of the active site across the dimer interface, and complement the catalytic triad of Ser47, Asp192, and His195 in the second monomer | Bos taurus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| brain | isoform Ib | Bos taurus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine + H2O | i.e. platelet-activation factor | Bos taurus | 1-alkyl-sn-glycero-3-phosphocholine + acetate | - |
? | |
| acetylated platelet-activation factor + H2O | - |
Bos taurus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | determination of structure-function relationship, dimerization of the brain isozyme is essential for both catalytic activity and stability, the monomeric enzyme is unstable, the alpha1 and alpha2 are catalytic subunits, the beta-subunit is a regulatory one | Bos taurus |
| trimer | isozyme Ib, 2 * 26000, subunits alpha1 and/or subunit alpha2, + 1 * 45000, beta-subunit | Bos taurus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PAF-AH | - |
Bos taurus |
| platelet-activating factor acetylhydrolase | - |
Bos taurus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Bos taurus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 47.5 | - |
unfolding and irreversible denaturation at pH 9.5 | Bos taurus |
| 52.3 | - |
unfolding and irreversible denaturation at pH 6.5 | Bos taurus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Bos taurus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Bos taurus |
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Release 2023.1 (January 2023)
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