Proteomics

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Mass spectrometry study of the adduct formed by F-ALDH with thiram

ABSTRACT: F-ALDH is a recently characterized psychrophilic aldehyde dehydrogenase from Flavobacterium PL002. Thiram was shown to inhibit its enzymatic activity, yet the mechanism of inhibition is unknown. We have used low flow liquid chromatography (nanoLC) coupled to tandem mass spectrometry (MS/MS) to study the mechanism behind thiram inhibition, as we assumed a Cys-covalent adduct could be formed between F-ALDH and thiram. For this, purified F-ALDH was incubated with thiram and the sample was subjected to Cys reduction or not along a control sample of non-treated F-ALDH.

INSTRUMENT(S):

ORGANISM(S): Flavobacterium Sp. Pl002

SUBMITTER: Cristian Munteanu  

LAB HEAD: Alina Vasilescu

PROVIDER: PXD066425 | Pride | 2025-10-24

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
250503_GeoP_FALDH-THIRAM_NR_run01.raw Raw
250503_GeoP_FALDH-THIRAM_NR_run02.raw Raw
250503_GeoP_FALDH-THIRAM_NRtestinj.raw Raw
250504_GeoP_FALDH-THIRAM_R_run01B.raw Raw
250504_GeoP_FALDH-THIRAM_R_run02.raw Raw
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Publications

The selective detection of dithiocarbamate fungicides in food and agricultural products presents significant analytical challenges. While Surface-enhanced Raman spectroscopy (SERS) has been extensively investigated to address this, detection systems based on enzymatic inhibition remain underexplored. Using thiram as a model dithiocarbamate, the present work explores the potential application of a cold-active aldehyde dehydrogenase from Flavobacterium PL002 for the development of specific, inhibi  ...[more]

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