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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
2.5.1.30
759075
Structure, function, and inhibition of Staphylococcus aureus heptaprenyl diphosphate synthase
ChemMedChem
11
1915-1923
2016
Staphylococcus aureus
27457559
2.5.1.30
759075
Structure, function, and inhibition of Staphylococcus aureus heptaprenyl diphosphate synthase
ChemMedChem
11
1915-1923
2016
Staphylococcus aureus NCTC 8325
27457559
2.5.1.30
637631
Artificial substrates of medium-chain elongating enzymes, hexaprenyl- and heptaprenyl diphosphate synthases
Bioorg. Med. Chem. Lett.
11
2157-2159
2001
Bacillus subtilis
11514159
2.5.1.30
702201
Chain length determination of prenyltransferases: both heteromeric subunits of medium-chain (E)-prenyl diphosphate synthase are involved in the product chain length determination
Biochemistry
39
12717-12722
2000
Bacillus subtilis
11027152
2.5.1.30
674185
Direct observation of substrate-enzyme complexation by surface forces measurement
J. Am. Chem. Soc.
128
15209-15214
2006
Bacillus subtilis
17117872
2.5.1.30
637623
Heptaprenyl pyrophosphate synthetase from Bacillus subtilis
J. Biol. Chem.
255
4539-4543
1980
Bacillus subtilis
6768722
2.5.1.30
637624
Heptaprenylpyrophosphate synthetase from Bacillus subtilis
Methods Enzymol.
110
199-205
1985
Bacillus subtilis
3927112
2.5.1.30
637624
Heptaprenylpyrophosphate synthetase from Bacillus subtilis
Methods Enzymol.
110
199-205
1985
Bacillus subtilis PCI-219
3927112
2.5.1.30
637628
Intersubunit structure within heterodimers of medium-chain prenyl diphosphate synthases. Formation of a hybrid-type heptaprenyl diphosphate synthase
J. Biochem.
124
790-797
1998
Geobacillus stearothermophilus
9756625
2.5.1.30
637630
Mechanism of product chain length determination for heptaprenyl diphosphate synthase from Bacillus stearothermophilus
Eur. J. Biochem.
267
4520-4528
2000
Bacillus subtilis
10880976
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