Dataset Information

Structure elucidation for tunable hetero-assembly of a plant PDX1.2/PDX1.3 pseudoenzyme-enzyme pair

ABSTRACT: Mass spectrometry raw data including peptide mapping, and top down liquid chromatography mass spectrometry for Arabidopsis PDX1.2/PDX1.3 homo- and hetero-complexes produced using cell-free expression. Purified proteins from cell-free expression were digested using trifluoroethanol protocol for peptide mapping. Proteins were directly analyzed for top down without additional treatment. Peptide data were analyzed using MS-GF+ and Byonic. The Byonic results were reported in the associated manuscript. Top down data were processed with ProMex for intact mass deconvolution.

INSTRUMENT(S): LTQ Orbitrap Velos, Q Exactive Plus

ORGANISM(S): Arabidopsis Thaliana (ncbitaxon:3702)

SUBMITTER: Mowei Zhou

PROVIDER: MSV000085233 | MassIVE | Mon Apr 06 08:29:00 BST 2020

REPOSITORIES: MassIVE

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Publications

Tunable Heteroassembly of a Plant Pseudoenzyme-Enzyme Complex.

Novikova Irina V IV Zhou Mowei M Du Chen C Parra Marcelina M Kim Doo Nam DN VanAernum Zachary L ZL Shaw Jared B JB Hellmann Hanjo H Wysocki Vicki H VH Evans James E JE

ACS chemical biology 20210914 11

Pseudoenzymes have emerged as key regulatory elements in all kingdoms of life despite being catalytically nonactive. Yet many factors defining why one protein is active while its homologue is inactive remain uncertain. For pseudoenzyme-enzyme pairs, the similarity of both subunits can often hinder conventional characterization approaches. In plants, a pseudoenzyme, PDX1.2, positively regulates vitamin B<sub>6</sub> production by association with its active catalytic homologues such as PDX1.3 thr ...[more]

PMID: 34520180

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