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Literature summary for 2.5.1.59 extracted from
- Structure of protein geranylgeranyltransferase-I from the human pathogen Candida albicans complexed with a lipid substrate (2008), J. Biol. Chem., 283, 31933-31940.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Candida albicans |
| PCR-amplification and expression in Escherichia coli | Candida albicans |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| enzyme in complex with its substrate geranylgeranylpyrophosphate, hanging drop method, PCB buffer, pH 7.0 and 25% PEG 1500, cryoprotection in PCB vuffer, pH 7.0, 30% PEG 1500, and 10% ethylene glycol, flash frozen in liquid nitrogen, diffraction data collection at -173°C | Candida albicans |
| hanging-drop method, crystal structure of GGTase-I in complex with its cognate lipid substrate, geranylgeranylpyrophosphate | Candida albicans |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | for maximum reaction rate | Candida albicans |  |
| Zn2+ | activating the cysteine thiolate of the substrate | Candida albicans | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 37000 | - |
alpha-subunit | Candida albicans |
| 45000 | - |
beta-subunit | Candida albicans |
| 82000 | - |
heterodimer of the alpha and beta subunits | Candida albicans |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| geranylgeranyl diphosphate + protein-cysteine | Candida albicans | - |
S-geranylgeranyl-protein + diphosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Candida albicans | Q9Y765 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Candida albicans |
| centrifugation of cells, frozen paste resuspended in 20 mM Tris, pH 7.7 with 5 mM dithiothreitol, and 5 microM ZnCls, and protease inhibitor tablet, cells lysed with pressure homogenization, crude lysate clarified by centrifugation, applied to DEAE Sepharose column, fractionation with buffer and varying NaCl concentrations, pooling of fractions, addition of substrate geranylgeranylpyrophosphate to displace nonspecifically bound lipids, phenyl-Sepharose column fractionation with gradient of buffer with (NH4)2SO4, pooled fractions applied to Q-Sepharose column, fractionated with gradient of buffer and NaCl, concentration of active fractions, application to a 120-ml Superdex 16/10 gel filtration column, concentration of enzyme | Candida albicans |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| geranylgeranyl diphosphate + protein-cysteine | - |
Candida albicans | S-geranylgeranyl-protein + diphosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heterodimer | 1 * 37000 + 1 * 45000 | Candida albicans |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CaGGTase-I | - |
Candida albicans |
| geranylgeranyltransferase-I | - |
Candida albicans |
| GGTase-I | - |
Candida albicans |
| protein geranylgeranyltransferase type I | - |
Candida albicans |
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