Syntrophus aciditrophicus uses the same enzymes in a reversible manner to degrade and synthesize aromatic and alicyclic acids.
Acetates
/ metabolism
Acetyl Coenzyme A
/ metabolism
Acids
/ chemistry
Acyl Coenzyme A
/ metabolism
Bacterial Proteins
/ genetics
Benzoates
/ metabolism
Cyclohexanecarboxylic Acids
/ metabolism
Deltaproteobacteria
/ enzymology
Electron Transport
Methane
/ metabolism
Methanospirillum
/ metabolism
Proteomics
Journal
Environmental microbiology
ISSN: 1462-2920
Titre abrégé: Environ Microbiol
Pays: England
ID NLM: 100883692
Informations de publication
Date de publication:
05 2019
05 2019
Historique:
received:
23
01
2019
revised:
12
03
2019
accepted:
19
03
2019
pubmed:
22
3
2019
medline:
6
5
2020
entrez:
22
3
2019
Statut:
ppublish
Résumé
Syntrophy is essential for the efficient conversion of organic carbon to methane in natural and constructed environments, but little is known about the enzymes involved in syntrophic carbon and electron flow. Syntrophus aciditrophicus strain SB syntrophically degrades benzoate and cyclohexane-1-carboxylate and catalyses the novel synthesis of benzoate and cyclohexane-1-carboxylate from crotonate. We used proteomic, biochemical and metabolomic approaches to determine what enzymes are used for fatty, aromatic and alicyclic acid degradation versus for benzoate and cyclohexane-1-carboxylate synthesis. Enzymes involved in the metabolism of cyclohex-1,5-diene carboxyl-CoA to acetyl-CoA were in high abundance in S. aciditrophicus cells grown in pure culture on crotonate and in coculture with Methanospirillum hungatei on crotonate, benzoate or cyclohexane-1-carboxylate. Incorporation of
Identifiants
pubmed: 30895699
doi: 10.1111/1462-2920.14601
pmc: PMC6488403
mid: NIHMS1021024
doi:
Substances chimiques
Acetates
0
Acids
0
Acyl Coenzyme A
0
Bacterial Proteins
0
Benzoates
0
Cyclohexanecarboxylic Acids
0
Acetyl Coenzyme A
72-89-9
Methane
OP0UW79H66
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
1833-1846Subventions
Organisme : NIH HHS
ID : R01GM085402
Pays : United States
Organisme : UCLA-DOE Institute
Pays : International
Organisme : Department of Energy
ID : DE-FG02-96ER20214
Pays : International
Organisme : NIH HHS
ID : R01GM104610
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM104610
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM085402
Pays : United States
Organisme : Department of Energy Office of Science (BER)
ID : DE-FC-02-02ER63421
Pays : International
Organisme : Office of Basic Energy Sciences
Pays : International
Informations de copyright
© 2019 Society for Applied Microbiology and John Wiley & Sons Ltd.
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