Investigating the reaction and substrate preference of indole-3-acetaldehyde dehydrogenase from the plant pathogen Pseudomonas syringae PtoDC3000.

doi:10.1042/BSR20202959

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Article

Investigating the reaction and substrate preference of indole-3-acetaldehyde dehydrogenase from the plant pathogen Pseudomonas syringae PtoDC3000.

Bioscience reports - 23 Dec 2020

Zhang Kaleena, Lee Josephine S, Liu Regina, Chan Zita T, Dawson Trenton J, De Togni Elisa S, Edwards Chris T, Eng Isabel K, Gao Ashley R, Goicouria Luis A, Hall Erin M, Hu Kelly A, Huang Katherine, Kizhner Alexander, Kodama Kelsie C, Lin Andrew Z, Liu Jennifer Y, Lu Alan Y, Peng Owen W, Ryu Erica P, Shi Sophia, Sorkin Maria L, Walker Patricia L, Wang Grace J, Xu Mark C, Yang Rebecca S, Cascella Barrie, Cruz Wilhelm, Holland Cynthia K, McClerkin Sheri A, Kunkel Barbara N, Lee Soon Goo, Jez Joseph M

Abstract excerpt

Aldehyde dehydrogenases (ALDHs) catalyze the conversion of various aliphatic and aromatic aldehydes into corresponding carboxylic acids. Traditionally considered as housekeeping enzymes, new biochemical roles are being identified for members of ALDH family. Recent work showed that AldA from the plant pathogen Pseudomonas syringae strain PtoDC3000 (PtoDC3000) functions as an indole-3-acetaldehyde dehydrogenase for...

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PMID: 33325526
DOI: 10.1042/BSR20202959
PMCID: PMC7745063

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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