Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Susanna Haapanen"'
Autor:
Susanna Haapanen, Andrea Angeli, Martti Tolvanen, Reza Zolfaghari Emameh, Claudiu T. Supuran, Seppo Parkkila
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 38, Iss 1 (2023)
Schistosoma mansoni is an intestinal parasite with one β-class carbonic anhydrase, SmaBCA. We report the sequence enhancing, production, catalytic activity, and inhibition results of the recombinant SmaBCA. It showed significant catalytic activity o
Externí odkaz:
https://doaj.org/article/3790dc0dd24242b7a7f439f695ddde5a
Publikováno v:
Metabolites, Vol 9, Iss 2, p 26 (2019)
The β-carbonic anhydrase (CA, EC 4.2.1.1) from the pathogenic protozoan Entamoeba histolytica, EhiCA, was investigated for its activation with a panel of natural and non-natural amino acids and amines. EhiCA was potently activated by D-His, D-Phe, D
Externí odkaz:
https://doaj.org/article/295cc9a16a82423083847f8afbecadb8
Publikováno v:
International Journal of Molecular Sciences, Vol 19, Iss 12, p 3946 (2018)
A newly described β-carbonic anhydrase (CA, EC 4.2.1.1) from the pathogenic protozoan Entamoeba histolytica, EhiCA, was recently shown to possess a significant catalytic activity for the physiologic CO2 hydration reaction (kcat of 6.7 × 105 s−1 a
Externí odkaz:
https://doaj.org/article/485ab127403d4684a69ae30b1c6a6069
Publikováno v:
Molecules, Vol 23, Iss 12, p 3112 (2018)
We report the cloning and catalytic activity of a β-carbonic anhydrase (CA, EC 4.2.1.1), isolated from the pathogenic protozoan Entamoeba histolytica, EhiCA. This enzyme has a high catalytic activity for the physiologic CO2 hydration reaction, with
Externí odkaz:
https://doaj.org/article/41785ea81f3d4050aa8caf490b164921
Publikováno v:
Metabolites, Vol 8, Iss 1, p 22 (2018)
Carbonic anhydrases (CAs) are metalloenzymes that are omnipresent in nature. CAs catalyze the basic reaction of the reversible hydration of CO2 to HCO3− and H+ in all living organisms. Photosynthetic organisms contain six evolutionarily different c
Externí odkaz:
https://doaj.org/article/c15e88becba042e296bd9614ad601bbf
Autor:
Susanna Haapanen, Seppo Parkkila
Publikováno v:
Topics in Medicinal Chemistry ISBN: 9783031068492
Entamoeba histolytica infection, amoebiasis, is a major cause of morbidity and mortality in developing countries. It is also a significant causative agent of traveler’s diarrhea. It has been estimated that amoebiasis may affect 10% of the global po
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b42619a96af570be8a218d7fbe8d2e38
https://doi.org/10.1007/7355_2021_127
https://doi.org/10.1007/7355_2021_127
Publikováno v:
Metabolites
Volume 9
Issue 2
Metabolites, Vol 9, Iss 2, p 26 (2019)
Volume 9
Issue 2
Metabolites, Vol 9, Iss 2, p 26 (2019)
The &beta
carbonic anhydrase (CA, EC 4.2.1.1) from the pathogenic protozoan Entamoeba histolytica, EhiCA, was investigated for its activation with a panel of natural and non-natural amino acids and amines. EhiCA was potently activated by D-His,
carbonic anhydrase (CA, EC 4.2.1.1) from the pathogenic protozoan Entamoeba histolytica, EhiCA, was investigated for its activation with a panel of natural and non-natural amino acids and amines. EhiCA was potently activated by D-His,
Publikováno v:
International Journal of Molecular Sciences
Volume 19
Issue 12
International Journal of Molecular Sciences, Vol 19, Iss 12, p 3946 (2018)
Volume 19
Issue 12
International Journal of Molecular Sciences, Vol 19, Iss 12, p 3946 (2018)
A newly described &beta
carbonic anhydrase (CA, EC 4.2.1.1) from the pathogenic protozoan Entamoeba histolytica, EhiCA, was recently shown to possess a significant catalytic activity for the physiologic CO2 hydration reaction (kcat of 6.7 ×
carbonic anhydrase (CA, EC 4.2.1.1) from the pathogenic protozoan Entamoeba histolytica, EhiCA, was recently shown to possess a significant catalytic activity for the physiologic CO2 hydration reaction (kcat of 6.7 ×
Publikováno v:
Molecules
Volume 23
Issue 12
Molecules, Vol 23, Iss 12, p 3112 (2018)
Volume 23
Issue 12
Molecules, Vol 23, Iss 12, p 3112 (2018)
We report the cloning and catalytic activity of a β-carbonic anhydrase (CA, EC 4.2.1.1), isolated from the pathogenic protozoan Entamoeba histolytica, EhiCA. This enzyme has a high catalytic activity for the physiologic CO2 hydration reaction, with
Carbonic anhydrases (CAs) are metalloenzymes that are omnipresent in nature. The CAs catalyze the basic reaction of reversible hydration of CO2 to HCO3− and H+ in all living organisms. Photosynthetic organisms contain six evolutionarily different c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9090df253541b19fb9e0bd0581ff6933
https://doi.org/10.20944/preprints201801.0110.v1
https://doi.org/10.20944/preprints201801.0110.v1