scholarly journals Anaerobic degradation of sorbic acid by sulfate-reducing and fermenting bacteria: pentanone-2 and isopentanone-2 as byproducts

1991 ◽  
Vol 2 (1) ◽  
pp. 33-41 ◽  
Author(s):  
Sylvia Schnell ◽  
Christine Wondrak ◽  
G�nther Wahl ◽  
Bernhard Schink
2010 ◽  
Vol 44 (5) ◽  
pp. 1670-1676 ◽  
Author(s):  
Pablo A. Lara-Martín ◽  
Abelardo Gómez-Parra ◽  
José Luis Sanz ◽  
Eduardo González-Mazo

2018 ◽  
Vol 20 (10) ◽  
pp. 3589-3600 ◽  
Author(s):  
Anne M. Himmelberg ◽  
Thomas Brüls ◽  
Zahra Farmani ◽  
Philip Weyrauch ◽  
Gabriele Barthel ◽  
...  

1990 ◽  
Vol 153 (5) ◽  
pp. 470-477 ◽  
Author(s):  
Regine Szewzyk ◽  
Norbert Pfennig

2020 ◽  
Vol 117 (27) ◽  
pp. 15599-15608 ◽  
Author(s):  
Jiayi Liu ◽  
Yifeng Wei ◽  
Lianyun Lin ◽  
Lin Teng ◽  
Jinyu Yin ◽  
...  

2(S)-dihydroxypropanesulfonate (DHPS) is a microbial degradation product of 6-deoxy-6-sulfo-d-glucopyranose (sulfoquinovose), a component of plant sulfolipid with an estimated annual production of 1010tons. DHPS is also at millimolar levels in highly abundant marine phytoplankton. Its degradation and sulfur recycling by microbes, thus, play important roles in the biogeochemical sulfur cycle. However, DHPS degradative pathways in the anaerobic biosphere are not well understood. Here, we report the discovery and characterization of two O2-sensitive glycyl radical enzymes that use distinct mechanisms for DHPS degradation. DHPS-sulfolyase (HpsG) in sulfate- and sulfite-reducing bacteria catalyzes C–S cleavage to release sulfite for use as a terminal electron acceptor in respiration, producing H2S. DHPS-dehydratase (HpfG), in fermenting bacteria, catalyzes C–O cleavage to generate 3-sulfopropionaldehyde, subsequently reduced by the NADH-dependent sulfopropionaldehyde reductase (HpfD). Both enzymes are present in bacteria from diverse environments including human gut, suggesting the contribution of enzymatic radical chemistry to sulfur flux in various anaerobic niches.


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