CntA oxygenase substrate profile comparison and oxygen dependency of TMA production in Providencia rettgeri

CntA oxygenase is a Rieske 2S‐2Fe cluster‐containing protein that has been previously described as able to produce trimethylamine (TMA) from carnitine, gamma‐butyrobetaine, glycine betaine, and in one case, choline. TMA found in humans is exclusively of bacterial origin, and its metabolite, trimethy...

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Bibliographic Details
Published in:Journal of basic microbiology Vol. 58; no. 1; pp. 52 - 59
Main Authors: Kalnins, Gints, Sevostjanovs, Eduards, Hartmane, Dace, Grinberga, Solveiga, Tars, Kaspars
Format: Journal Article
Language:English
Published: Germany 01.01.2018
Subjects:
atherosclerosis
betaine
carnitine
Carnitine - metabolism
cell culture
choline
CntA
digestive system
heart
Humans
metabolites
Methylamines - metabolism
Microbiota
Oxidation-Reduction
oxygen
Oxygen - metabolism
Oxygen - pharmacology
oxygenases
Oxygenases - metabolism
Providencia - drug effects
Providencia - enzymology
Providencia - metabolism
Providencia rettgeri
renal failure
Rieske oxygenase
Substrate Specificity
trimethylamine
CntA
trimethylamine
carnitine
Rieske oxygenase
ISSN:0233-111X, 1521-4028, 1521-4028
Online Access:Get full text
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Summary:CntA oxygenase is a Rieske 2S‐2Fe cluster‐containing protein that has been previously described as able to produce trimethylamine (TMA) from carnitine, gamma‐butyrobetaine, glycine betaine, and in one case, choline. TMA found in humans is exclusively of bacterial origin, and its metabolite, trimethylamine oxide (TMAO), has been associated with atherosclerosis and heart and renal failure. We isolated four different Rieske oxygenases and determined that there are no significant differences in their substrate panels. All three had high activity toward carnitine/gamma‐butyrobetaine, medium activity toward glycine betaine, and very low activity toward choline. We tested the influence of low oxygen concentrations on TMA production in CntA‐containing Providencia rettgeri cell cultures and discovered that this process, although dependent on the amount of oxygen, is still feasible in environments with 1 and 0.2% oxygen, which is comparable to oxygen levels in some parts of the digestive system.
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ISSN:0233-111X
1521-4028
1521-4028
DOI:10.1002/jobm.201700428