M
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.
Michael P. Torrens-Spence,Anastassia Bobokalonova,Valentina Carballo,Christopher M. Glinkerman,Tomáš Pluskal,Amber Shen,Jing-Ke Weng +6 more
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
Michael P. Torrens-Spence,Pingyang Liu,Haizhen Ding,Kim Harich,Glenda E. Gillaspy,Jianyong Li +5 more
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.
Tomáš Pluskal,Michael P. Torrens-Spence,Timothy R. Fallon,Andrea De Abreu,Cindy H. Shi,Jing-Ke Weng +5 more
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.
Journal ArticleDOI
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.