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Michael P. Torrens-Spence

Researcher at Massachusetts Institute of Technology

Publications -  22
Citations -  560

Michael P. Torrens-Spence is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Amino acid & Aromatic amino acids. The author has an hindex of 11, co-authored 22 publications receiving 350 citations. Previous affiliations of Michael P. Torrens-Spence include Virginia Tech.

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Journal ArticleDOI

PBS3 and EPS1 Complete Salicylic Acid Biosynthesis from Isochorismate in Arabidopsis.

TL;DR: Together, PBS3 and EPS1 form a two-step metabolic pathway to produce SA from isochorismate in Arabidopsis, which is distinct from how SA is biosynthesized in bacteria.
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Complete Pathway Elucidation and Heterologous Reconstitution of Rhodiola Salidroside Biosynthesis

TL;DR: It is shown that heterologous production of salidroside can be achieved in the yeast Saccharomyces cerevisiae as well as the plant Nicotiana benthamiana through transgenic expression of Rhodiola salid roside biosynthetic genes.
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Biochemical Evaluation of the Decarboxylation and Decarboxylation-Deamination Activities of Plant Aromatic Amino Acid Decarboxylases

TL;DR: The data indicates that the tyrosine and phenylalanine in the catalytic loop region could serve as a signature residue to reliably distinguish plant arylalkylamine and aldehyde synthesizing AAADs and enables further insights into the mechanistic roles of active site residues.
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The biosynthetic origin of psychoactive kavalactones in kava.

TL;DR: The structural basis for the evolutionary development of a pair of paralogous styrylpyrone synthases that establish the kavalactone scaffold and the catalytic mechanism of a regio- and stereo-specific kvalactone reductase that produces a subset of chiral kavalACTones are presented.
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Investigation of a substrate-specifying residue within Papaver somniferum and Catharanthus roseus aromatic amino acid decarboxylases.

TL;DR: In this study, bioinformatic approaches were utilized to identify several active site residues within plant AAAD enzymes that may impact substrate specificity and produce a primary sequence identifier that may help differentiate the indolic and phenolic substrate specificities of individual plant AAads.