EC Number |
BRENDA No. |
Title |
Journal |
Volume |
Pages |
Year |
Organism |
PubMed ID |
---|
2.5.1.59 | 636537 |
Protein prenyltransferases |
J. Biol. Chem. |
271 |
5289-5292 |
1996 |
Saccharomyces cerevisiae |
8621375 |
2.5.1.59 | 636538 |
Purification of a mammalian protein geranylgeranyltransferase. Formation and catalytic properties of an enzyme-geranylgeranyl pyrophosphate complex |
J. Biol. Chem. |
268 |
4055-4060 |
1993 |
Bos taurus |
8440698 |
2.5.1.59 | 636539 |
Mammalian protein geranylgeranyltransferase-I: Substrate specificity, kinetic mechanism, metal requirements, and affinity labeling |
Biochemistry |
34 |
1344-1354 |
1995 |
Bos taurus |
7827082 |
2.5.1.59 | 636540 |
Properties and kinetic mechanism of recombinant mammalian protein geranylgeranyltransferase type I |
J. Biol. Chem. |
269 |
23465-23470 |
1994 |
Rattus norvegicus |
8089111 |
2.5.1.59 | 636541 |
Influence of metal ions on substrate binding and catalytic activity of mammalian protein geranylgeranyltransferase type-I |
Biochem. J. |
320 |
925-932 |
1996 |
Rattus norvegicus |
- |
2.5.1.59 | 636542 |
Characterization of Ha-Ras, N-Ras, Ki-Ras4A, and Ki-Ras4B as in vitro substrates for farnesyl protein transferase and geranylgeranyl protein transferase type I |
J. Biol. Chem. |
272 |
10232-10239 |
1997 |
Homo sapiens |
9092572 |
2.5.1.59 | 636543 |
Yeast protein geranylgeranyltransferase type-I: overproduction, purification, and characterization |
Arch. Biochem. Biophys. |
321 |
182-190 |
1995 |
Saccharomyces cerevisiae |
7639519 |
2.5.1.59 | 636544 |
Yeast protein geranylgeranyltransferase type-I: steady-state kinetics and substrate binding |
Biochemistry |
36 |
4552-4557 |
1997 |
Saccharomyces cerevisiae |
9109664 |
2.5.1.59 | 636545 |
Characterization of yeast geranylgeranyl transferase type I expressed in Escherichia coli |
Mol. Cell |
6 |
602-608 |
1996 |
Bos taurus |
- |
2.5.1.59 | 636545 |
Characterization of yeast geranylgeranyl transferase type I expressed in Escherichia coli |
Mol. Cell |
6 |
602-608 |
1996 |
Saccharomyces cerevisiae |
- |