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Literature summary extracted from

  • Hast, M.A.; Beese, L.S.
    Structure of protein geranylgeranyltransferase-I from the human pathogen Candida albicans complexed with a lipid substrate (2008), J. Biol. Chem., 283, 31933-31940.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.59
-
 Candida albicans
2.5.1.59 PCR-amplification and expression in Escherichia coli Candida albicans

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.5.1.59 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
2.5.1.59 hanging-drop method, crystal structure of GGTase-I in complex with its cognate lipid substrate, geranylgeranylpyrophosphate Candida albicans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.59 Mg2+ for maximum reaction rate Candida albicans
2.5.1.59 Zn2+ activating the cysteine thiolate of the substrate Candida albicans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.5.1.59 37000
-
 alpha-subunit Candida albicans
2.5.1.59 45000
-
 beta-subunit Candida albicans
2.5.1.59 82000
-
 heterodimer of the alpha and beta subunits Candida albicans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.59 geranylgeranyl diphosphate + protein-cysteine Candida albicans
-
 S-geranylgeranyl-protein + diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.59 Candida albicans Q9Y765
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.59
-
 Candida albicans
2.5.1.59 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.59 geranylgeranyl diphosphate + protein-cysteine
-
 Candida albicans S-geranylgeranyl-protein + diphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.59 heterodimer 1 * 37000 + 1 * 45000 Candida albicans

Synonyms

EC Number Synonyms Comment Organism
2.5.1.59 CaGGTase-I
-
 Candida albicans
2.5.1.59 geranylgeranyltransferase-I
-
 Candida albicans
2.5.1.59 GGTase-I
-
 Candida albicans
2.5.1.59 protein geranylgeranyltransferase type I
-
 Candida albicans