Enzymes
| UniProtKB help_outline | 1,668 proteins |
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- Name help_outline isopentenyl diphosphate Identifier CHEBI:128769 Charge -3 Formula C5H9O7P2 InChIKeyhelp_outline NUHSROFQTUXZQQ-UHFFFAOYSA-K SMILEShelp_outline CC(=C)CCOP([O-])(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 38 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline dimethylallyl diphosphate Identifier CHEBI:57623 (CAS: 22679-02-3) help_outline Charge -3 Formula C5H9O7P2 InChIKeyhelp_outline CBIDRCWHNCKSTO-UHFFFAOYSA-K SMILEShelp_outline CC(C)=CCOP([O-])(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 79 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:23284 | RHEA:23285 | RHEA:23286 | RHEA:23287 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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An unusual isopentenyl diphosphate isomerase found in the mevalonate pathway gene cluster from Streptomyces sp. strain CL190.
Kaneda K., Kuzuyama T., Takagi M., Hayakawa Y., Seto H.
A gene cluster encoding five enzymes of the mevalonate pathway had been cloned from Streptomyces sp. strain CL190. This gene cluster contained an additional ORF, orfD, encoding an unknown protein that was detected in some archaebacteria and some Gram-positive bacteria including Staphylococcus aure ... >> More
A gene cluster encoding five enzymes of the mevalonate pathway had been cloned from Streptomyces sp. strain CL190. This gene cluster contained an additional ORF, orfD, encoding an unknown protein that was detected in some archaebacteria and some Gram-positive bacteria including Staphylococcus aureus. The recombinant product of orfD was purified as a soluble protein and characterized. The molecular mass of the enzyme was estimated to be 37 kDa by SDS-polyacrylamide gel electrophoresis and 155 kDa by gel filtration chromatography, suggesting that the enzyme is most likely to be a tetramer. The purified enzyme contained flavin mononucleotide (FMN) with the amount per tetramer being 1.4 to 1.6 mol/mol. The enzyme catalyzed the isomerization of isopentenyl diphosphate (IPP) to produce dimethylallyl diphosphate (DMAPP) in the presence of both FMN and NADPH. The Escherichia coli plasmid expressing orfD could complement the disrupted IPP isomerase gene in E. coli. These results indicate that orfD encodes an unusual IPP isomerase showing no sequence similarity to those of IPP isomerases identified to date. Based on the difference in enzymatic properties, we classify the IPP isomerases into two types: Type 2 for FMN- and NAD(P)H-dependent enzymes, and type 1 for the others. In view of the critical role of this isomerase in S. aureus and of the different enzymatic properties of mammalian (type 1) and S. aureus (type 2) isomerases, this unusual enzyme is considered to be a suitable molecular target for the screening of antibacterial drugs specific to S. aureus. << Less
Proc. Natl. Acad. Sci. U.S.A. 98:932-937(2001) [PubMed] [EuropePMC]
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Cellular oncogenes and retroviruses.
Bishop J.M.
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Biosynthesis of terpenes. VII. Isopentenyl pyrophosphate isomerase.
AGRANOFF B.W., EGGERER H., HENNING U., LYNEN F.