Naslov
Investigating the possible evolution of isopentenyl diphosphate phosphohydrolase from isopentenyl diphosphate isomerase

Autori
Sučec, Iva ; Vlašić, Ana ; Sabljić, Igor ; Karačić, Zrinka

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
45th FEBS Congress, Molecules of Life: Towards New Horizons, FEBS Open Bio, Volume11, IssueS1 / - : John Wiley & Sons, 2021, 134-134

Skup
45th FEBS Congress, Molecules of Life: Towards New Horizons

Mjesto i datum
Online ; Ljubljana, Slovenija, 03.07.2021. - 08.07.2021

Vrsta sudjelovanja
Poster

Vrsta recenzije
Nije recenziran

Ključne riječi
Nudix hydrolase ; isopentenyl diphosphate ; protein structure

Sažetak
Isopentenyl diphosphate phosphohydrolase enzymatic activity was first identified in plants in proteins from the Nudix superfamily. The presence of this activity was postulated based on the presence of isopentenyl phosphate kinase in plants, previously published in Henry L et al. (2015) PNAS 112, 10050-10055, and was found in members of the Nudix hydrolase superfamily due to sequence similarity to isopentenyl diphosphate isomerase, previously published in: Karacic Z et al. (2017) Biol Chem 398, 101–112. This enzyme is presumed to be involved in the regulation of isoprenoid biosynthesis in plants. We found homologues of this protein in all land plants, but also in genomes of some eukaryotic and prokaryotic microorganisms. We solved the crystal structure of isopentenyl diphosphate phosphohydrolase from the amoeba Dictyostelium discoideum and found that the most similar structures are those of isopentenyl diphosphate isomerase type I, not other Nudix hydrolases. Additionally, we identified sequences from green algae that show characteristics of both isomerases and hydrolases – a conserved tryptophan residue that stabilizes the carbocation intermediate in isomerases, and the catalytic glutamate necessary for phosphohydrolase activity, however in an alternate position. We expressed one such protein from Parachlorella kessleri and confirmed that it is an isopentenyl diphosphate phosphohydrolase. Based on our results, we hypothesize that proteins with isopentenyl diphosphate phosphohydrolase activity evolved in green algae before the advent of Embryophyta, and spread to other microorganisms via horizontal gene transfer or endosymbiosis. *The authors marked with an asterisk equally contributed to the work.

Izvorni jezik
Engleski

Znanstvena područja
Kemija

POVEZANOST RADA