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Literature summary for 2.5.1.29 extracted from

  • Chang, C.K.; Teng, K.H.; Lin, S.W.; Chang, T.H.; Liang, P.H.
    Control activity of yeast geranylgeranyl diphosphate synthase from dimer interface through H-bonds and hydrophobic interaction (2013), Biochemistry, 52, 2783-2792.
    View publication on PubMed
Search for more literature for 2.5.1.29

Cloned(Commentary)

Cloned (Comment) Organism
gene GGPPS, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain JM109 Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
H139A site-directed mutagenesis, the dimeric mutant shows altered kinetics compared to the wild-type enzyme Saccharomyces cerevisiae
H139A/R140A site-directed mutagenesis, inactive monomeric mutant Saccharomyces cerevisiae
M111A site-directed mutagenesis, the dimeric mutant shows altered kinetics compared to the wild-type enzyme Saccharomyces cerevisiae
M111E site-directed mutagenesis, the dimeric/monomeric mutant shows altered kinetics compared to the wild-type enzyme Saccharomyces cerevisiae
M111F site-directed mutagenesis, the dimeric mutant shows altered kinetics compared to the wild-type enzyme Saccharomyces cerevisiae
N101A site-directed mutagenesis, the dimeric mutant shows altered kinetics compared to the wild-type enzyme Saccharomyces cerevisiae
N101A/N104A site-directed mutagenesis, the dimeric mutant shows reduced kcat compared to the wild-type Saccharomyces cerevisiae
N101A/N104A/Y105A site-directed mutagenesis, inactive dimeric mutant Saccharomyces cerevisiae
N101A/Y105A site-directed mutagenesis, the dimeric mutant shows reduced kcat compared to the wild-type Saccharomyces cerevisiae
N104A site-directed mutagenesis, the dimeric mutant shows altered kinetics compared to the wild-type enzyme Saccharomyces cerevisiae
N104A/Y105A site-directed mutagenesis, the dimeric mutant shows slightly reduced activity compared to the wild-type Saccharomyces cerevisiae
R140A site-directed mutagenesis, the dimeric mutant shows altered kinetics compared to the wild-type enzyme Saccharomyces cerevisiae
Y105A site-directed mutagenesis, the dimeric mutant shows altered kinetics compared to the wild-type enzyme Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00061
-
 (2E,6E)-farnesyl diphosphate mutant N101A/Y105A, pH 7.5, 25°C Saccharomyces cerevisiae
0.00061
-
 isopentenyl diphosphate mutant N101A/Y105A, pH 7.5, 25°C Saccharomyces cerevisiae
0.0017
-
 isopentenyl diphosphate wild-type enzyme, pH 7.5, 25°C Saccharomyces cerevisiae
0.0025
-
 (2E,6E)-farnesyl diphosphate mutant H139A, pH 7.5, 25°C Saccharomyces cerevisiae
0.0025
-
 isopentenyl diphosphate mutant M111A, pH 7.5, 25°C Saccharomyces cerevisiae
0.0026
-
 isopentenyl diphosphate mutant Y105A, pH 7.5, 25°C Saccharomyces cerevisiae
0.0037
-
 (2E,6E)-farnesyl diphosphate wild-type enzyme, pH 7.5, 25°C Saccharomyces cerevisiae
0.0037
-
 (2E,6E)-farnesyl diphosphate mutant M111A, pH 7.5, 25°C Saccharomyces cerevisiae
0.0045
-
 isopentenyl diphosphate mutant R140A, pH 7.5, 25°C Saccharomyces cerevisiae
0.0051
-
 isopentenyl diphosphate mutant H139A, pH 7.5, 25°C Saccharomyces cerevisiae
0.0055
-
 (2E,6E)-farnesyl diphosphate mutant N104A, pH 7.5, 25°C Saccharomyces cerevisiae
0.0055
-
 isopentenyl diphosphate mutant N104A, pH 7.5, 25°C Saccharomyces cerevisiae
0.0063
-
 (2E,6E)-farnesyl diphosphate mutant N101A, pH 7.5, 25°C Saccharomyces cerevisiae
0.0066
-
 isopentenyl diphosphate mutant M111E, pH 7.5, 25°C Saccharomyces cerevisiae
0.0077
-
 (2E,6E)-farnesyl diphosphate mutant Y105A, pH 7.5, 25°C Saccharomyces cerevisiae
0.0081
-
 isopentenyl diphosphate mutant N104A/Y105A, pH 7.5, 25°C Saccharomyces cerevisiae
0.0089
-
 (2E,6E)-farnesyl diphosphate mutant R140A, pH 7.5, 25°C Saccharomyces cerevisiae
0.009
-
 (2E,6E)-farnesyl diphosphate mutant M111E, pH 7.5, 25°C Saccharomyces cerevisiae
0.0113
-
 isopentenyl diphosphate mutant M111F, pH 7.5, 25°C Saccharomyces cerevisiae
0.0146
-
 (2E,6E)-farnesyl diphosphate mutant M111F, pH 7.5, 25°C Saccharomyces cerevisiae
0.0153
-
 (2E,6E)-farnesyl diphosphate mutant N101A/N104A, pH 7.5, 25°C Saccharomyces cerevisiae
0.0292
-
 isopentenyl diphosphate mutant N101A/N104A, pH 7.5, 25°C Saccharomyces cerevisiae
0.0467
-
 (2E,6E)-farnesyl diphosphate mutant N104A/Y105A, pH 7.5, 25°C Saccharomyces cerevisiae
0.048
-
 isopentenyl diphosphate mutant N101A, pH 7.5, 25°C Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
44790
-
 recombinant mutant H139A/R140A, gel filtration Saccharomyces cerevisiae
47820
-
 recombinant monomeric mutant M111E, gel filtration Saccharomyces cerevisiae
72070
-
 recombinant mutant N101A/Y105A, gel filtration Saccharomyces cerevisiae
74740
-
 recombinant mutant Y105A, gel filtration Saccharomyces cerevisiae
75950
-
 recombinant mutant N101A, gel filtration Saccharomyces cerevisiae
76730
-
 recombinant mutant N104A/Y105A, gel filtration Saccharomyces cerevisiae
76990
-
 recombinant mutant R140A, gel filtration Saccharomyces cerevisiae
78690
-
 recombinant mutant H139A, gel filtration Saccharomyces cerevisiae
80350
-
 recombinant mutant N104A, gel filtration Saccharomyces cerevisiae
82300
-
 recombinant wild-type enzyme, gel filtration Saccharomyces cerevisiae
83880
-
 recombinant mutant N101A/N104A/Y105A, gel filtration Saccharomyces cerevisiae
84980
-
 recombinant mutant N101A/N104A, gel filtration Saccharomyces cerevisiae
85920
-
 recombinant dimeric mutant M111E, gel filtration Saccharomyces cerevisiae
88080
-
 recombinant mutant M111F, gel filtration Saccharomyces cerevisiae
92340
-
 recombinant mutant M111A, gel filtration Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate Saccharomyces cerevisiae
-
 diphosphate + geranylgeranyl diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae Q12051 gene GGPPS
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes by nickel affinity chromatography from Escherichia coli strain JM109, removal of the tag by cleavage with Factor Xa Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate
-
 Saccharomyces cerevisiae diphosphate + geranylgeranyl diphosphate
-
 ?

Subunits

Subunits Comment Organism
dimer dimerization is required for GGPPS activity, resdieus N101 and Y105 form H-bonds with H139 and R140 in the other subunit, and the H-bonds, mainly through N101 for maintaining substrate binding stability and the hydrophobic interaction of M111 in dimer interface, are essential for activity of yeast GGPPS Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
GGPPS
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.00013
-
 (2E,6E)-farnesyl diphosphate mutant N101A/Y105A, pH 7.5, 25°C Saccharomyces cerevisiae
0.00013
-
 isopentenyl diphosphate mutant N101A/Y105A, pH 7.5, 25°C Saccharomyces cerevisiae
0.0002
-
 (2E,6E)-farnesyl diphosphate mutant N101A/N104A, pH 7.5, 25°C Saccharomyces cerevisiae
0.0002
-
 isopentenyl diphosphate mutant N101A/N104A, pH 7.5, 25°C Saccharomyces cerevisiae
0.017
-
 (2E,6E)-farnesyl diphosphate mutant N104A/Y105A, pH 7.5, 25°C Saccharomyces cerevisiae
0.017
-
 isopentenyl diphosphate mutant N104A/Y105A, pH 7.5, 25°C Saccharomyces cerevisiae
0.02
-
 (2E,6E)-farnesyl diphosphate mutant M111E, pH 7.5, 25°C Saccharomyces cerevisiae
0.02
-
 isopentenyl diphosphate mutant M111E, pH 7.5, 25°C Saccharomyces cerevisiae
0.036
-
 (2E,6E)-farnesyl diphosphate mutant M111F, pH 7.5, 25°C Saccharomyces cerevisiae
0.036
-
 isopentenyl diphosphate mutant M111F, pH 7.5, 25°C Saccharomyces cerevisiae
0.037
-
 (2E,6E)-farnesyl diphosphate wild-type enzyme, pH 7.5, 25°C Saccharomyces cerevisiae
0.037
-
 isopentenyl diphosphate wild-type enzyme, pH 7.5, 25°C Saccharomyces cerevisiae
0.038
-
 (2E,6E)-farnesyl diphosphate mutant R140A, pH 7.5, 25°C Saccharomyces cerevisiae
0.038
-
 isopentenyl diphosphate mutant R140A, pH 7.5, 25°C Saccharomyces cerevisiae
0.04
-
 (2E,6E)-farnesyl diphosphate mutant M111A, pH 7.5, 25°C Saccharomyces cerevisiae
0.04
-
 isopentenyl diphosphate mutant M111A, pH 7.5, 25°C Saccharomyces cerevisiae
0.042
-
 (2E,6E)-farnesyl diphosphate mutant H139A, pH 7.5, 25°C Saccharomyces cerevisiae
0.042
-
 isopentenyl diphosphate mutant H139A, pH 7.5, 25°C Saccharomyces cerevisiae
0.06
-
 (2E,6E)-farnesyl diphosphate mutant Y105A, pH 7.5, 25°C Saccharomyces cerevisiae
0.06
-
 isopentenyl diphosphate mutant Y105A, pH 7.5, 25°C Saccharomyces cerevisiae
0.067
-
 (2E,6E)-farnesyl diphosphate mutant N101A, pH 7.5, 25°C Saccharomyces cerevisiae
0.067
-
 isopentenyl diphosphate mutant N101A, pH 7.5, 25°C Saccharomyces cerevisiae
0.11
-
 (2E,6E)-farnesyl diphosphate mutant N104A, pH 7.5, 25°C Saccharomyces cerevisiae
0.11
-
 isopentenyl diphosphate mutant N104A, pH 7.5, 25°C Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Saccharomyces cerevisiae

General Information

General Information Comment Organism
malfunction yeast geranylgeranyl diphosphate synthase becomes an inactive monomer when the first N-terminal helix involved in dimerization is deleted Saccharomyces cerevisiae