S
Shiva Bhowmik
Researcher at Scripps Research Institute
Publications - 10
Citations - 784
Shiva Bhowmik is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: CYP8B1 & Catalytic triad. The author has an hindex of 8, co-authored 10 publications receiving 512 citations. Previous affiliations of Shiva Bhowmik include Purdue University & Scripps Health.
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Journal ArticleDOI
Consequences of bile salt biotransformations by intestinal bacteria
TL;DR: Elucidating methods to control the gut microbiome and bile acid pool composition in humans may lead to a reduction in some of the major diseases of the liver, gall bladder and colon.
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The Tautomeric Half-reaction of BphD, a C-C Bond Hydrolase KINETIC AND STRUCTURAL EVIDENCE SUPPORTING A KEY ROLE FOR HISTIDINE 265 OF THE CATALYTIC TRIAD
Geoff P. Horsman,Shiva Bhowmik,Stephen Y. K. Seah,Pravindra Kumar,Jeffrey T. Bolin,Lindsay D. Eltis +5 more
TL;DR: This study identifies a keto intermediate, and demonstrates that the catalytic triad histidine catalyzes the tautomerization half-reaction, expanding the role of this residue from its purely hydrolytic function in other serine hydrolases.
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Structure and functional characterization of a bile acid 7α dehydratase BaiE in secondary bile acid synthesis
Shiva Bhowmik,Hsien-Po Chiu,David H. Jones,Hsiu-Ju Chiu,Mitchell D. Miller,Qingping Xu,Carol L. Farr,Jason M. Ridlon,Jason M. Ridlon,James E. Wells,Marc-André Elsliger,Ian A. Wilson,Phillip B. Hylemon,Phillip B. Hylemon,Scott A. Lesley,Scott A. Lesley +15 more
TL;DR: Site‐directed mutagenesis of BaiE from Clostridium scindens VPI 12708 confirm that these residues are essential for catalysis and also the importance of other conserved residues, Tyr54 and Arg146, which are involved in substrate binding and affect catalytic turnover.
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Structural and functional characterization of BaiA, an enzyme involved in secondary bile acid synthesis in human gut microbe
Shiva Bhowmik,David H. Jones,Hsien-Po Chiu,In-Hee Park,Hsiu-Ju Chiu,Herbert L. Axelrod,Carol L. Farr,Henry J Tien,Sanjay Agarwalla,Scott A. Lesley,Scott A. Lesley +10 more
TL;DR: The crystal structures of BaiA2, a short chain dehydrogenase/reductase from Clostridium scindens VPI 12708 that represent the first protein structure of this pathway, elucidated the basis of cofactor specificity and mechanism of proton relay and uncovered a novel nicotinamide‐hydroxyl ion (NAD+‐OH−) adduct contraposing previously reported adducts.
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The molecular basis for inhibition of BphD, a C-C bond hydrolase involved in polychlorinated biphenyls degradation: large 3-substituents prevent tautomerization.
TL;DR: It is reported that BphD preferentially hydrolyzed a series of 3-substituted HOPDAs in the order H > F > Cl > Me, suggesting that catalysis is affected by steric, not electronic, determinants.