Reference - Detail
| RRC ID | 29350 |
|---|---|
| Author | Mori T, Ogawa T, Yoshimura T, Hemmi H. |
| Title | Substrate specificity of undecaprenyl diphosphate synthase from the hyperthermophilic archaeon Aeropyrum pernix. |
| Journal | Biochem Biophys Res Commun |
| Abstract |
Cis-prenyltransferase from a hyperthermophilic archaeon Aeropyrum pernix was expressed in Escherichia coli and purified for characterization. Properties such as substrate specificity, product chain-length, thermal stability and cofactor requirement were investigated using the recombinant enzyme. In particular, the substrate specificity of the enzyme attracts interest because only dimethylallyl diphosphate and geranylfarnesyl diphosphate, both of which are unusual substrates for known cis-prenyltransferases, are likely available as an allylic primer substrate in A. pernix. From the enzymatic study, the archaeal enzyme was shown to be undecaprenyl diphosphate synthase that has anomalous substrate specificity, which results in a preference for geranylfarnesyl diphosphate. This means that the product of the enzyme, which is probably used as the precursor of the glycosyl carrier lipid, would have an undiscovered structure. |
| Volume | 436(2) |
| Pages | 230-4 |
| Published | 2013-6-28 |
| DOI | 10.1016/j.bbrc.2013.05.081 |
| PII | S0006-291X(13)00888-7 |
| PMID | 23726912 |
| MeSH | Aeropyrum / enzymology* Aeropyrum / genetics Alkyl and Aryl Transferases / genetics Alkyl and Aryl Transferases / metabolism* Archaeal Proteins / genetics Archaeal Proteins / metabolism* Electrophoresis, Polyacrylamide Gel Enzyme Stability Escherichia coli / genetics Gefarnate / analogs & derivatives Gefarnate / metabolism Hot Temperature* Organophosphates / metabolism Recombinant Proteins / metabolism Substrate Specificity |
| IF | 2.985 |
| Times Cited | 7 |
| WOS Category | BIOPHYSICS BIOCHEMISTRY & MOLECULAR BIOLOGY |
| Resource | |
| General Microbes | JCM 9820 |