Aerobic degradation of choline by Proteus mirabilis: enzymatic requirements and pathway
Abstract
Cleavage of choline to trimethylamine and acetaldehyde by extracts of Proteus mirabilis requires both particulate and soluble protein fractions, K+, and a bound divalent metal cation. The reaction shows a long lag period, abolished only by preincubation of the particulate fraction in the complete reaction system. The two-carbon fragment produced is acetaldehyde; choline cleavage appears to be tightly coupled to dismutation of the acetaldehyde to ethanol and acetate, as indicated by stimulation by NAD+, ADP. and Fe 2+ and inhibition by reagents reacting with acetaldehyde. The system is thus similar to that previously described in anaerobes (Desulfovibrio, Clostridium). Attempts to demonstrate a cobamide coenzyme requirement (as in the similar ethanolamine ammonia-lyase reaction) were unsuccessful; the reaction was carried out by fractions devoid of vitamin B 12 activity (not supporting growth of Lactobacillus leichmannii) and insensitive to light.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Neither IMC nor FMC affected the growth rate of P. mirabilis, E. fergusonii, and P. penneri under conditions showing complete inhibition of choline TMA lyase activity.
“neither affected the growth rate of several known TMA-producing human commensals (P. mirabilis, E. fergusonii, and P. penneri)33,46 when cultured in nutrient-rich media under conditions showing complete inhibition in choline TMA lyase activity”
From Development of a gut microbe–targeted nonlethal therapeutic to inhibit thrombosis potential (2018) · cites this paper as [46]
Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 315,771 · see citing works
Microdiffusion Analysis and Volumetric Error
(1948) · Nature · doi:10.1038/161583a0 · Cited by 2,182 · see citing works
COENZYME A FUNCTION IN AND ACETYL TRANSFER BY THE PHOSPHOTRANSACETYLASE SYSTEM
Stadtman, E. R., Novelli, G. D., & Lipmann, F. A. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)50986-8 · Cited by 505 · see citing works
ENZYMATIC PHOSPHORYLATION OF ACETATE
Rose, I. A., GRUNBERG‐MANAGO, M., Korey, S. R., & Ochoa, S. (1954) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)71161-7 · Cited by 387 · see citing works
Amines in Fish Muscle: I. Colorimetric Determination of Trimethylamine as the Picrate Salt
Dyer, W. J. (1945) · Journal of the Fisheries Research Board of Canada · doi:10.1139/f42-042 · Cited by 193 · see citing works
de la Huerga, J., & Popper, H. (1951) · Journal of Clinical Investigation · doi:10.1172/jci102463 · Cited by 129 · see citing works
MAMMALIAN METHYLMALONYL ISOMERASE AND VITAMIN B 12 COENZYMES
Lengyel, P., Mazumder, R., & Ochoa, S. (1960) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.46.10.1312 · Cited by 119 · see citing works
The Clostridial Fermentations of Choline and Ethanolamine
Bradbeer, C. (1965) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)97007-9 · Cited by 116 · see citing works
The formation of ethanol in Escherichia coli
DAWES, E. A., & Foster, S. M. (1956) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(56)90148-2 · Cited by 101 · see citing works
THE NON-SPECIFICITY OF THYMIDINE AS A GROWTH FACTOR FOR LACTIC ACID BACTERIA
Kitay, E., McNutt, W. S., & Snell, E. E. (1949) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)57047-2 · Cited by 70 · see citing works
ANAEROBIC DEGRADATION OF CHOLINE I. , Vibrio cholinicus n. sp
Hayward, H. R., & Stadtman, T. C. (1959) · Journal of Bacteriology · doi:10.1128/jb.78.4.557-561.1959 · Cited by 68 · see citing works
Trimethylaminuria: Fishy Odors in Children
Lee, C. W. G., Yu, J. S., Turner, B. B., & Murray, K. E. (1976) · New England Journal of Medicine · doi:10.1056/nejm197610212951706 · Cited by 51 · see citing works
[45] Enzymatic determination of ethanol
Kaplan, N. O., & Ciotti, M. M. (1957) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(57)03385-6 · Cited by 43 · see citing works
Anaerobic Degradation of Choline
Hayward, H. R. (1960) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64514-4 · Cited by 40 · see citing works
Microbiological Assay of Vitamin B 12
Hoff‐Jørgensen, E. (1954) · Methods of biochemical analysis · doi:10.1002/9780470110171.ch4 · Cited by 39 · see citing works
THE METABOLISM OF CHOLINE AND ITS CONVERSION TO GLYCINE IN THE RAT
Soloway, S., & Stetten, D. (1953) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)66129-0 · Cited by 34 · see citing works
Anaerobic Degradation of Choline
Hayward, H. R., & Stadtman, T. C. (1960) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)69563-8 · Cited by 34 · see citing works
Action of Enterobacteriaceae on Choline and Related Compounds
Dyer, F. E., & Wood, A. J. (1947) · Journal of the Fisheries Research Board of Canada · doi:10.1139/f47-002 · Cited by 29 · see citing works
[46] Chemical procedures for separation and determination of alcohols
Neish, A. C. (1957) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(57)03386-8 · Cited by 18 · see citing works
Graves, S. W., Fox, J. A., & BABIOR, B. M. (1980) · Biochemistry · doi:10.1021/bi00556a032 · Cited by 14 · see citing works
Über den Cholinstoffwechsel. 2. Mitteilung
Müller, H. (1940) · Hoppe-Seyler´s Zeitschrift für physiologische Chemie · doi:10.1515/bchm2.1940.266.4-6.205 · Cited by 13 · see citing works
THE ACTION OF MEMBERS OF THE GENUS ACHROMOBACTER ON TRIMETHYLAMINE OXIDE AND RELATED COMPOUNDS
Campbell, L. L., & Williams, O. B. (1951) · Journal of Bacteriology · doi:10.1128/jb.62.2.249-251.1951 · Cited by 9 · see citing works
Über den bakteriellen Abbau des Cholins.
Poller, K. (1933) · Hoppe-Seyler´s Zeitschrift für physiologische Chemie · doi:10.1515/bchm2.1933.217.1-2.79 · Cited by 3 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Wang, Z., Roberts, A. B., Buffa, J. A., Levison, B. S., Zhu, W., Org, E., Gu, X., Huang, Y., Zamanian-Daryoush, M., Culley, M. K., et al. (2015) · Cell · doi:10.1016/j.cell.2015.11.055 · Cited by 1,317 · see citing works
Development of a gut microbe–targeted nonlethal therapeutic to inhibit thrombosis potential
Roberts, A. B., Gu, X., Buffa, J. A., Hurd, A. G., Wang, Z., Zhu, W., Gupta, N., Skye, S. M., Cody, D. B., Levison, B. S., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0128-1 · Cited by 552 · see citing works
Martínez-del Campo, A., Bodea, S., Hamer, H. A., Marks, J. A., Haiser, H. J., Turnbaugh, P. J., & Balskus, E. P. (2015) · mBio · doi:10.1128/mbio.00042-15 · Cited by 224 · see citing works
Expanding role of gut microbiota in lipid metabolism
Ghazalpour, A., Cespedes, I., Bennett, B. J., & Allayee, H. (2016) · Current Opinion in Lipidology · doi:10.1097/mol.0000000000000278 · Cited by 171 · see citing works
Bekhit, A. E. A., Giteru, S. G., Holman, B. W. B., & Hopkins, D. L. (2021) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12764 · Cited by 169 · see citing works
Characterization of Choline Trimethylamine-Lyase Expands the Chemistry of Glycyl Radical Enzymes
Craciun, S., Marks, J. A., & Balskus, E. P. (2014) · ACS Chemical Biology · doi:10.1021/cb500113p · Cited by 139 · see citing works
Structure and Function of CutC Choline Lyase from Human Microbiota Bacterium Klebsiella pneumoniae
Kalnins, G., Kuka, J., Grı̄nberga, S., Makrecka‐Kuka, M., Liepinsh, E., Dambrova, M., & Tārs, K. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.670471 · Cited by 101 · see citing works
Wang, Q., Guo, M., Liu, Y., Xu, M., Shi, L., Li, X., Zhao, J., Zhang, H., Wang, G., & Chen, W. (2022) · Nutrients · doi:10.3390/nu14061222 · Cited by 95 · see citing works
Anaerobic choline metabolism in microcompartments promotes growth and swarming of P roteus mirabilis
Jameson, E., Fu, T., Brown, I. R., Paszkiewicz, K. H., Purdy, K. J., Frank, S., & Chen, Y. (2015) · Environmental Microbiology · doi:10.1111/1462-2920.13059 · Cited by 46 · see citing works
The Genetic Architecture of Coronary Artery Disease: Current Knowledge and Future Opportunities
Hartiala, J., Schwartzman, W. S., Gabbay, J., Ghazalpour, A., Bennett, B. J., & Allayee, H. (2017) · Current Atherosclerosis Reports · doi:10.1007/s11883-017-0641-6 · Cited by 43 · see citing works
Contribution of the commensal microbiota to atherosclerosis and arterial thrombosis
Kiouptsi, K., & Reinhardt, C. (2018) · British Journal of Pharmacology · doi:10.1111/bph.14483 · Cited by 39 · see citing works
Chao, C.-K., & Zeisel, S. H. (1990) · The Journal of Nutritional Biochemistry · doi:10.1016/0955-2863(90)90055-p · Cited by 23 · see citing works
Role of gut microbe-derived metabolites in cardiometabolic diseases: Systems based approach
Cao, Y., Aquino-Martínez, R., Hutchison, E. R., Allayee, H., Lusis, A. J., & Rey, F. E. (2022) · Molecular Metabolism · doi:10.1016/j.molmet.2022.101557 · Cited by 23 · see citing works
Zeisel, S. H., Gettner, S., & Youssef, M. (1989) · Food and Chemical Toxicology · doi:10.1016/0278-6915(89)90089-6 · Cited by 22 · see citing works
Gut microbiota: a novel strategy affecting atherosclerosis
Yang, L., Yang, J., Zhang, T., Xie, X., & Wu, Q. (2025) · Microbiology Spectrum · doi:10.1128/spectrum.00482-24 · Cited by 14 · see citing works
Proteomic analysis of homocholine catabolic pathway in Pseudomonas sp. strain A9
Ahmed, I. A. M., Eltayeb, M. M., Mori, N., Arima, J., TANAKA, H. K. M., Taniguchi, T., & Yamanaka, N. (2015) · Process Biochemistry · doi:10.1016/j.procbio.2015.07.001 · Cited by 4 · see citing works
Ahmed, I. A. M., Eltayeb, M. M., Habora, M. E. E., Eltayeb, A. E., Arima, J., Mori, N., Taniguchi, T., & Yamanaka, N. (2016) · Process Biochemistry · doi:10.1016/j.procbio.2016.10.009 · Cited by 2 · see citing works
Gut microbiota and lipid metabolism and metabolic syndrome
Duttaroy, A. K. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822405-2.00029-3 · Cited by 1 · see citing works
- Authors
- Sandhu, S. S., & Chase Jr., T.
- Venue
- Canadian Journal of Microbiology
- Publisher
- Canadian Science Publishing
- Published
- 1986-09-01
- Volume
- 32
- Issue
- 9
- Pages
- 743-750
- ISSN
- 0008-4166 (ISSN-L)
- 1480-3275
- OpenAlex
- W2080619691
- Cited by
- 18
- References
- 23
- Citations by year
- 2025: 1 · 2022: 2 · 2021: 2 · 2018: 2 · 2017: 1 · 2016: 2 · 2015: 5 · 2014: 1
- FWCI
- 0.14
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Canadian Journal of Microbiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- New Jersey Agricultural Experiment Station
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial metabolism and enzyme function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Polyamine Metabolism and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Steroid Chemistry and Biochemistry
- Keywords
- Proteus mirabilis, trimethylamine, acetaldehyde, ethanolamine ammonia-lyase, cobamide coenzyme, vitamin B12, lag phase, NAD+, ADP, iron, aerobic biodegradation
- MeSH terms
- Acetaldehyde, Aerobiosis, Cell-Free System, Choline, Kinetics, Methylamines, Proteus mirabilis
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
