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Literature summary extracted from
- Structural basis for the bi-functionality of human oxaloacetate decarboxylase FAHD1 (2018), Biochem. J., 475, 3561-3576 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.7.1.5 | expression in BL21(DE3) Escherichia coli LysS cells | Homo sapiens |
| 4.1.1.112 | expression in BL21(DE3) Escherichia coli LysS cells | Homo sapiens |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.7.1.5 | hanging drop vapor diffusion method at 18°C, crystal structure of the enzyme (FAHD1) protein in complex with its cofactor Mg2+, cocrystallization with oxalate and high resolution for the enzyme (FAHD1) in complex with oxalate | Homo sapiens |
| 4.1.1.112 | hanging drop vapor diffusion method at 18°C, crystal structure of the enzyme (FAHD1) protein in complex with its cofactor Mg2+, cocrystallization with oxalate and high resolution for the enzyme (FAHD1) in complex with oxalate | Homo sapiens |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.7.1.5 | E33A | significant reduction in oxaloacetate decarboxylase activity and complete abrogation of the acylpyruvate hydrolase activity | Homo sapiens |
| 3.7.1.5 | H30A | significant reduction in oxaloacetate decarboxylase activity and complete abrogation of the acylpyruvate hydrolase activity | Homo sapiens |
| 3.7.1.5 | K123A | oxaloacetate decarboxylase activity and acylpyruvate hydrolase activity are abolished | Homo sapiens |
| 3.7.1.5 | additional information | mutation of amino acids H30, E33 and K123 each had discernible influence on the acylpyruvate hydrolase and/or oxaloacetate decarboxylase activity of FAHD1, suggesting distinct catalytic mechanisms for both activities | Homo sapiens |
| 4.1.1.112 | E33A | significant reduction in oxaloacetate decarboxylase activity and complete abrogation of the acylpyruvate hydrolase activity | Homo sapiens |
| 4.1.1.112 | H30A | significant reduction in oxaloacetate decarboxylase activity and complete abrogation of the acylpyruvate hydrolase activity | Homo sapiens |
| 4.1.1.112 | K123A | oxaloacetate decarboxylase activity and acylpyruvate hydrolase activity are abolished | Homo sapiens |
| 4.1.1.112 | additional information | mutation of amino acids H30, E33 and K123 each had discernible influence on the acylpyruvate hydrolase and/or oxaloacetate decarboxylase activity of FAHD1, suggesting distinct catalytic mechanisms for both activities | Homo sapiens |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.7.1.5 | oxalate | competitive inhibitor | Homo sapiens |  |
| 4.1.1.112 | oxalate | competitive inhibitor | Homo sapiens | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.7.1.5 | 0.0405 | - |
Acetylpyruvate | pH 7.4, 25°C, wild-type enzyme | Homo sapiens | |
| 3.7.1.5 | 0.0421 | - |
Acetylpyruvate | pH 7.4, 25°C, mutant enzyme E33A | Homo sapiens | |
| 3.7.1.5 | 0.0819 | - |
Acetylpyruvate | pH 7.4, 25°C, mutant enzyme H30A | Homo sapiens | |
| 4.1.1.112 | 20.7 | - |
oxaloacetate | pH 7.4, 25°C, wild-type enzyme | Homo sapiens | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.7.1.5 | mitochondrion | - |
Homo sapiens | 5739 | - |
| 4.1.1.112 | mitochondrion | - |
Homo sapiens | 5739 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.7.1.5 | Mg2+ | - |
Homo sapiens | |
| 4.1.1.112 | Mg2+ | - |
Homo sapiens | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.7.1.5 | Homo sapiens | Q6P587 | - |
- |
| 4.1.1.112 | Homo sapiens | Q6P587 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.7.1.5 | - |
Homo sapiens |
| 4.1.1.112 | - |
Homo sapiens |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.7.1.5 | acetylpyruvate + H2O | bi-functional enzyme displaying both acylpyruvate hydrolase and oxaloacetate decarboxylase activity | Homo sapiens | acetate + pyruvate | - |
? | |
| 4.1.1.112 | Oxaloacetate | bi-functional enzyme displaying both acylpyruvate hydrolase and oxaloacetate decarboxylase activity | Homo sapiens | Pyruvate + CO2 | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.7.1.5 | FAH domain-containing protein 1 | - |
Homo sapiens |
| 3.7.1.5 | FAHD1 | - |
Homo sapiens |
| 4.1.1.112 | FAH domain-containing protein 1 | - |
Homo sapiens |
| 4.1.1.112 | FAHD1 | - |
Homo sapiens |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.7.1.5 | metabolism | the enzyme is important for mitochondrial function. It acts antagonistically to pyruvate carboxylase, a key metabolic enzyme | Homo sapiens |
| 4.1.1.112 | metabolism | the enzyme is important for mitochondrial function. It acts antagonistically to pyruvate carboxylase, a key metabolic enzyme | Homo sapiens |
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Release 2023.1 (January 2023)
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