Recombinant Thermotoga petrophila S-adenosylmethionine decarboxylase proenzyme (SpeH) is a pyruvoyl-dependent enzyme critical for polyamine biosynthesis, catalyzing the decarboxylation of S-adenosylmethionine (AdoMet) to produce dcAdoMet, a precursor for spermidine synthesis . Derived from the hyperthermophilic bacterium Thermotoga petrophila, this enzyme exhibits thermostability and functional robustness, making it valuable for industrial and research applications . Its recombinant form, expressed in Escherichia coli, is widely used to study polyamine metabolism and enzyme mechanisms .
Converts AdoMet to dcAdoMet via pyruvoyl-mediated decarboxylation, enabling spermidine biosynthesis .
Inhibition by substrate analogs like 5′-deoxy-5′-dimethylthioadenosine (MMTA) via competitive binding .
Inherits thermostability from T. petrophila, retaining activity at high temperatures (optimal growth: 80°C) .
Polyamine Research: Essential for studying spermidine/spermine biosynthesis pathways .
Enzyme Engineering: Serves as a model for thermostable decarboxylases in synthetic biology .
KEGG: tpt:Tpet_0276
STRING: 390874.Tpet_0276