Potter Kevin, Criswell Jared, Zi Jiachen, Stubbs Alisha, Peters Reuben J
Dept. Biochemistry, Biophysics & Molecular Biology, Iowa State University, Ames, IA 50011 (USA).
Angew Chem Int Ed Engl. 2014 Jul 7;53(28):7198-202. doi: 10.1002/anie.201402911. Epub 2014 May 23.
An active-site water molecule coordinated by conserved histidine and asparagine residues seems to serve as the catalytic base in all ent-copalyl diphosphate synthases (CPSs). When these residues are substituted by alanine, the mutant CPSs produce stereochemically novel ent-8-hydroxy-CPP. Given the requisite presence of CPSs in all land plants for gibberellin phytohormone biosynthesis, such plasticity presumably underlies the observed extensive diversification of the resulting labdane-related diterpenoids.
由保守的组氨酸和天冬酰胺残基配位的活性位点水分子似乎在所有内贝壳杉烯二磷酸合酶(CPS)中充当催化碱。当这些残基被丙氨酸取代时,突变的CPS会产生立体化学上新颖的内-8-羟基-CPP。鉴于所有陆地植物中CPS对于赤霉素植物激素生物合成的必要存在,这种可塑性大概是所观察到的由此产生的与半日花烷型二萜广泛多样化的基础。