Zobrazeno 1 - 10
of 11
pro vyhledávání: '"R. Siva Sai Kumar"'
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 33, Iss 1, Pp 31-36 (2018)
The β-carbonic anhydrases (CAs, EC 4.2.1.1) from the pathogenic bacterium Clostridium perfringens (CpeCA) was recently characterised kinetically and for its anion inhibition profile. In the search of effective CpeCA inhibitors, possibly useful to in
Externí odkaz:
https://doaj.org/article/ca69753cccaf48bfaaa7107ac45a591c
Autor:
James G. Ferry, R. Siva Sai Kumar, Adepu K. Kumar, Deepa Yenugudhati, Neela H. Yennawar, Divya Prakash, Hemant P. Yennawar
Publikováno v:
Biochemistry. 55:313-321
Glutaredoxins (GRXs) are thiol-disulfide oxidoreductases abundant in prokaryotes, although little is understood of these enzymes from the domain Archaea. The numerous characterized GRXs from the domain Bacteria utilize a diversity of low-molecular-we
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3875458abd38efc2f67a7d625206564
https://doi.org/10.1021/acs.biochem.5b00823
https://doi.org/10.1021/acs.biochem.5b00823
Autor:
Andrea Scozzafava, James G. Ferry, Daniela Vullo, Claudiu T. Supuran, Clemente Capasso, R. Siva Sai Kumar
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 23:6706-6710
A β-carbonic anhydrases (CAs, EC 4.2.1.1) was recently cloned, purified and characterized kinetically in the pathogen Clostridium perfringens . We report here the first inhibition study of this enzyme (CpeCA). CpeCA was poorly inhibited by iodide an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::73dd7767d6929c21ecab4878c6622ed2
https://doi.org/10.1016/j.bmcl.2013.10.037
https://doi.org/10.1016/j.bmcl.2013.10.037
Publikováno v:
Biochemistry. 54(19)
Bioinformatics analyses predict the distribution in nature of several classes of diverse disulfide reductases that evolved from an ancestral plant-type ferredoxin:thioredoxin reductase (FTR) catalytic subunit to meet a variety of ecological needs. Me
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dfeaf04c326738a8976f7193bdf52590
https://pubmed.ncbi.nlm.nih.gov/25915695
https://pubmed.ncbi.nlm.nih.gov/25915695
Publikováno v:
Process Biochemistry. 41:2282-2288
Purification of alpha-amylases using alginate as an affinity matrix is reported. This process involved affinity binding of the amylase to alginate, precipitation of amylase-alginate beads in the presence of CaCl2, and subsequent recovery of the enzym
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1f30a44275245629e8861fd5d3f8fcac
https://doi.org/10.1016/j.procbio.2006.05.028
https://doi.org/10.1016/j.procbio.2006.05.028
Autor:
R Siva Sai, Kumar, James G, Ferry
Publikováno v:
Sub-cellular biochemistry. 75
Carbonic anhydrase is a metalloenzyme catalyzing the reversible hydration of carbon dioxide to bicarbonate. Five independently evolved classes have been described for which one or more are found in nearly every cell type underscoring the general impo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::212c54ee5cfd49cd0078f82e7743fb72
https://pubmed.ncbi.nlm.nih.gov/24146375
https://pubmed.ncbi.nlm.nih.gov/24146375
Autor:
R. Siva Sai Kumar, James G. Ferry
Publikováno v:
Subcellular Biochemistry ISBN: 9789400773585
Carbonic anhydrase is a metalloenzyme catalyzing the reversible hydration of carbon dioxide to bicarbonate. Five independently evolved classes have been described for which one or more are found in nearly every cell type underscoring the general impo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4ddca494b3168352978a24c6f41f9073
https://doi.org/10.1007/978-94-007-7359-2_5
https://doi.org/10.1007/978-94-007-7359-2_5
Autor:
Andrew D. Patterson, Stephen B. Melville, James G. Ferry, Jared B. Correll, R. Siva Sai Kumar, William Hendrick
The carbonic anhydrase (Cpb) from Clostridium perfringens strain 13, the only carbonic anhydrase encoded in the genome, was characterized both biochemically and physiologically. Heterologously produced and purified Cpb was shown to belong to the type
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::736ee3870f0478cd51fdbd7c107528f1
https://europepmc.org/articles/PMC3650550/
https://europepmc.org/articles/PMC3650550/
Publikováno v:
Biochimie. 91(4)
Alpha-amylase from Sorghum bicolor, is reversibly unfolded by chemical denaturants at pH 7.0 in 50mM Hepes containing 13.6mM calcium and 15 mM DTT. The isothermal equilibrium unfolding at 27 degrees C is characterized by two state transition with Del
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ccabdb250017e2114806a042ddb07d4e
https://pubmed.ncbi.nlm.nih.gov/19278621
https://pubmed.ncbi.nlm.nih.gov/19278621
Publikováno v:
Journal of agricultural and food chemistry. 53(17)
Malted cereals are rich sources of alpha-amylase, which catalyzes the random hydrolysis of internal alpha-(1-4)-glycosidic bonds of starch, leading to liquefaction. Amylases play a role in the predigestion of starch, leading to a reduction in the wat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a5dbbf71a79fb4650237c0f125bfa07
https://pubmed.ncbi.nlm.nih.gov/16104815
https://pubmed.ncbi.nlm.nih.gov/16104815