| http://purl.uniprot.org/citations/3022798 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/3022798 | http://www.w3.org/2000/01/rdf-schema#comment | "Isopentenyl pyrophosphate isomerase catalyzes the interconversion of isopentenyl pyrophosphate and dimethylallyl pyrophosphate. The isomerase from yeast has been purified to near homogeneity (purity greater than 90%). The substrate analogue (Z)-3-(trifluoromethyl)-2-butenyl pyrophosphate reacts at less than 1.8 X 10(-6) times the rate of dimethylallyl pyrophosphate. The enzyme is irreversibly inactivated by 2-(dimethyl-amino)ethyl pyrophosphate (I). These observations are consistent with a carbonium ion mechanism for the isomerization. Compound I is an analogue of the intermediate carbonium ion and probably acts as a transition state analogue. For I, kon' = 2.1 X 10(6) M-1 min-1. No off-rate was detected and, therefore, Ki less than 1.4 X 10(-11) M. Upon denaturation of the inactivated enzyme, I is released unchanged. 2-(Trimethylammonio)ethyl pyrophosphate also inhibits with Ki' = 7 X 10(-7) M, kon' = 4.4 X 10(4) M-1 min-1, and koff = 0.03 min-1. Substrate analogues without a positively charged nitrogen were relatively poor inhibitors. The best inhibitor of these is ethyl pyrophosphate, Ki = 10(-4) M. The enzyme is inactivated by sulfhydryl-selective reagents. These reagents also prevent binding of I to the enzyme. The inactivation by iodoacetamide is dependent upon one ionizable group (pK = 9.3). The pH dependence of V and V/K for the isomerase-catalyzed reaction also depends upon a group with pK = 9.3."xsd:string |
| http://purl.uniprot.org/citations/3022798 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi00367a040"xsd:string |
| http://purl.uniprot.org/citations/3022798 | http://purl.uniprot.org/core/author | "Abeles R.H."xsd:string |
| http://purl.uniprot.org/citations/3022798 | http://purl.uniprot.org/core/author | "Reardon J.E."xsd:string |
| http://purl.uniprot.org/citations/3022798 | http://purl.uniprot.org/core/date | "1986"xsd:gYear |
| http://purl.uniprot.org/citations/3022798 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/3022798 | http://purl.uniprot.org/core/pages | "5609-5616"xsd:string |
| http://purl.uniprot.org/citations/3022798 | http://purl.uniprot.org/core/title | "Mechanism of action of isopentenyl pyrophosphate isomerase: evidence for a carbonium ion intermediate."xsd:string |
| http://purl.uniprot.org/citations/3022798 | http://purl.uniprot.org/core/volume | "25"xsd:string |
| http://purl.uniprot.org/citations/3022798 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/3022798 |
| http://purl.uniprot.org/citations/3022798 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/3022798 |
| http://purl.uniprot.org/uniprot/#_P15496-mappedCitation-3022798 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/3022798 |
| http://purl.uniprot.org/uniprot/P15496 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/3022798 |