Publications and Presentations



19. Kelkar, D. S., Ravikumar, G., Mehendale, N., Singh, S., Joshi, A., Sharma, A. K., Mhetre, A., Rajendran, A., Chakrapani, H., Kamat, S. S.* (2019) A chemical genetic screen identifies ABHD12 as an oxidized phosphatidylserine lipase, Nature Chemical Biology 15, 169-178. (*corresponding author)[Youtube video on this paper]

18. Chaplot, K., Pimpale, L., Ramalingam, B., Deivasigamani, S., Kamat, S. S., Ratnaparkhi, G. S. (2019) SOD1 activity thresholds and TOR signaling modulate VAP(P58S) aggregation via ROS-induced proteasomal degradation in a Drosophila model of Amylotrophic Lateral Sclerosis, Disease Models & Mechanisms 12(2), dmm033803, 1-15. (This article featured on the cover of the February 2019 issue).

17. Joshi, A., Shaikh, M., Singh, S., Rajndran, A., Mhetre, A., Kamat, S. S.* (2018) Biochemical characterization of the PHARC associated serine hydrolase ABHD12 reveals its preference for very long chain lipids, Journal of Biological Chemistry 293 (44), 16953-16963. (This article featured on the cover of the 2nd November 2018 issue). (*corresponding author)

16. Abhyankar, V., Kaduskar, B., Kamat, S. S., Deobagkar, D., Ratnaparkhi, G. S. (2018) Drosophila DNA/RNA methyltransferase contributes to robust host defense in ageing animals by regulating sphingolipid metabolism, Journal of Experimental Biology 221 (22), 1-10

15. Pathak, D., Mehendale, N., Singh, S., Mallik, R., Kamat, S. S.* (2018) Lipidomics suggests a new role for ceramide synthase in phagocytosis, ACS Chemical Biology 13 (8), 2280-2287. (This article featured on the cover of the August 2018 issue). (*corresponding author)

14. Rai, P., Kumar, M., Sharma, G., Barak, P., Das, S., Kamat, S. S., Mallik, R. M. (2017) Kinesin-dependent mechanism for controlling triglyceride secretion from the liver, PNAS 114 (49), 12958-12963.


From Ph.D. & Postdoc

13. Kory, N., Grond, S., Kamat, S. S., Li, Z., Krahmer, N., Chitraju, C., Zhou, P., Fronlich, F., Semova, I., Ejsing, C., Zechner, R., Cravatt, B. F., Farese, R. V., Walther, T. C. (2017) Mice lacking lipid droplet-associated hydrolase, a gene linked to human prostate cancer, have normal cholesterol ester metabolism, J. Lipid Research 58, 226-235.

12. Kolar, M. J., Kamat, S. S., Parsons, W. H., Homan, E., Maher, T., Peroni, O., Syed, I., Molven, A., Kahn, B. B., Cravatt, B. F., Saghatelian, A. (2016) Branched fatty acid esters of hydroxyl fatty acids are preferred substrates of the MODY8 gene carboxyl ester lipase, Biochemistry 55, 4636-4641.

11. Ogura, Y., Parsons, W. H., Kamat, S. S., Cravatt, B. F. (2016) A calcium-dependent acyltransferase that produces N-acyl phosphatidylethanolamines. Nature Chemical Biology 12, 669-671.

10. Parsons, W. H., Kolar, M. J., Kamat, S. S., Cognetta, A. B. III, Hulce, J. J., Saez, E., Kahn, B., Saghatelian, A. S., Cravatt, B. F. (2016) AIG1 and ADTRP are atypical membrane hydrolase that degrade bioactive FAHFAs, Nature Chemical Biology 12, 367-372.

9. Kamat, S. S., Camara, K., Parsons, W. H., Chen, D. H., Dix, M. M., Bird, T. D., Howell, A. R., Cravatt, B. F. (2015) Immunomodulatory lysophosphatidylserines are regulated by ABHD16A and ABHD12 interplay, Nature Chemical Biology 11,164-171.

8. Camara, K., Kamat, S. S., Lasota, C. C., Cravatt, B. F., Howell, A. R. (2015) Combining cross-metathesis and activity based protein profiling: new β-lactone motifs for targeting serine hydrolases, Bio. Org. Med. Chem. Let. 25, 317-321.

7. Korczynska, M., Xiang, D. F., Zhang, Z., Xu, C., Narindoshvili, T., Kamat, S. S., Williams, H. J., Chang, S. S., Kolb, P., Hillerich, B. S., Sauder, J. M., Burley, S. K., Almo, S. C., Swaminathan, S., Shoichet, B. K., Raushel, F. M. (2014) Functional annotation and structural characterization of a novel lactonase D-xylono-1,4-lactone-5-phosphate and L-arabino-1,4-lactone-5-phosphate, Biochemistry 53, 4727-4738.

6. Kamat, S. S., Burgos, E. S., Raushel, F. M. (2013) Potent inhibition of the C-P lyase nucleosidase PhnI by immucillinA-triphosphate, Biochemistry 52, 7366-7368.

5. Kamat, S. S., Williams, H. J., Dangott L. J., Chakrabarti, M., Raushel, F. M. (2013) The catalytic mechanism for the aerobic formation of methane by bacteria, Nature 497, 132-36. 

4. Kamat, S. S., Williams, H. J., Raushel, F. M. (2011) Intermediates in the transformation of phosphonates to phosphate by bacteria, Nature 480, 570-73. 

3. Kamat, S. S., Holmes-Hampton, G. P., Bagaria, A., Kumran, D., Tichy, S. E., Gheyi, T., Zheng, X., Bain, K., Groshong, C., Emtage, S., Sauder, J. M., Burley, S. K., Swaminathan, S., Lindahl, P. A., Raushel, F. M. (2011) The catalase activity of diiron adenine deaminase, Protein Science 20, 2080-94.

2. Kamat, S. S., Fan, H., Sauder, J. M., Burley, S. K., Shoichet, B. K., Sali, A., Raushel, F. M. (2011): Enzymatic deamination of the epigenetic base N-6-methyladenine, JACS 133, 2080-83. 

1. Kamat, S. S., Bagaria, A., Kumaran, D., Holmes-Hampton, G. P., Fan, H., Sali, A., Sauder, J. M., Burley, S. K., Lindahl, P. A., Swaminathan, S., Raushel, F. M. (2011): Catalytic mechanism and three dimensional structure of adenine deaminase, Biochemistry 50, 1917-27. 




6. Kamat, S. S.*, Singh, S., Rajendran, A., Gama, S., Zechel, D. L.* (2018) Enzymatic strategies for the catabolism of organophosphonates, Comprehensive Natural Products III: Enzymes and Enzyme Mechanisms, Book 4. (* co-corresponding authors) (Accepted, In Press).

5. Ulrich, E., Kamat, S. S.*, Hove-Jensen, B.*, Zechel, D. L.* (2018) Chapter 13: Methylphosphonic acid biosynthesis and catabolism in pelagic bacteria, Methods in Enzymology Vol. 605, 351-426 (* co-corresponding authors)


From Ph.D. & Postdoc

4. Kamat, S. S., Raushel, F. M. (2015) PhnJ – A novel radical SAM enzyme from the C-P lyase complex, Perspectives in Science 4, 32-37.

3. Kamat, S. S., Raushel, F. M. (2013) Adenine Deaminase, Encyclopedia of Inorganic and Bioinorganic Chemistry, 1-9.

2. Kamat, S. S., Raushel F. M. (2013) The enzymatic conversion of phosphonates to phosphate by bacteria, Current Opinions in Chemical Biology 17, 589-596.

1. Kamat, S. S., Williams, H. J., Raushel, F. M. (2013) Phosphonates to phosphate: A functional annotation of the essential genes of the phn operon in Escherichia coli, Beilstein Institut Proceedings, 5th International Symposium on Experimental Standard Conditions of Enzyme Characterizations (ESCEC), 1-18