7QUG

Crystal structure of carbon-sulfur lyase FnaPatB1 from Fusobacterium nucleatum subspecies animalis in complex with allyl-cysteine

Summary for 7QUG

• Entry DOI: 10.2210/pdb7qug/pdb
• Descriptor: carbon-sulfur lyase FnaPatB1, allyl-cysteine, ACETATE ION, ... (5 entities in total)
• Functional Keywords: carbon-sulfur lyase, plp-dependent aminotransferase, lyase
• Biological source: Fusobacterium nucleatum
• Total number of polymer chains: 2
• Total formula weight: 95612.11

Authors

Schwartz, M. (deposition date: 2022-01-18, release date: 2023-01-18, Last modification date: 2024-01-31)

Primary citation

Neiers, F.,Gourrat, K.,Canon, F.,Schwartz, M.
Metabolism of Cysteine Conjugates and Production of Flavor Sulfur Compounds by a Carbon-Sulfur Lyase from the Oral Anaerobe Fusobacterium nucleatum.
J.Agric.Food Chem., 70:9969-9979, 2022

PubMed Abstract: Flavor perception is a key factor in the acceptance or rejection of food. Aroma precursors such as cysteine conjugates are present in various plant-based foods and are metabolized into odorant thiols in the oral cavity. To date, the involved enzymes are unknown, despite previous studies pointing out the likely involvement of carbon-sulfur lyases (C-S lyases) from the oral microbiota. In this study, we show that saliva metabolizes allyl-cysteine into odorant thiol metabolites, with evidence suggesting that microbial pyridoxal phosphate-dependent C-S lyases are involved in the enzymatic process. A phylogenetic analysis of PatB C-S lyase sequences in four oral subspecies of was carried out and led to the identification of several putative targets. FnaPatB1 from subspecies , a putative C-S lyase, was characterized and showed high activity with a range of cysteine conjugates. Enzymatic and X-ray crystallographic data showed that FnaPatB1 metabolizes cysteine derivatives within a unique active site environment that enables the formation of flavor sulfur compounds. Using an enzymatic screen with a library of pure compounds, we identified several inhibitors able to reduce the C-S lyase activity of FnaPatB1 in vitro, which paves the way for controlling the release of odorant sulfur compounds from their cysteine precursors in the oral cavity.

PubMed: 35920882
DOI: 10.1021/acs.jafc.2c01727

Experimental method

X-RAY DIFFRACTION (2.6 Å)