Temat: enzyme substrate interaction - Katalog OPAC zbiorów

Skocz do pozycji: 1.

Tytuł:: Light-triggered protochlorophyllide to chlorophyllide reduction – new insights into enzyme-substrate interactions
Autorzy:: Gabruk, M.
Kruk, J.
Mysliwa-Kurdziel, B.
Powiązania:: https://bibliotekanauki.pl/articles/79867.pdf
Data publikacji:: 2013
Wydawca:: Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:: biosynthesis
chlorophyll
photosynthetic pigment
protochlorophyllide
chlorophyllide
enzyme substrate interaction
fluorescence
Źródło:: BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2013, 94, 3
0860-7796
Pojawia się w:: BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:: Biblioteka Nauki

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Skocz do pozycji: 2.

Tytuł:: Influence of dipeptidyl peptidase IV on enzymatic properties of adenosine deaminase
Autorzy:: Sharoyan, Svetlana
Antonyan, Alvard
Mardanyan, Sona
Lupidi, Giulio
Cristalli, Gloria
Powiązania:: https://bibliotekanauki.pl/articles/1041210.pdf
Data publikacji:: 2006
Wydawca:: Polskie Towarzystwo Biochemiczne
Tematy:: protein-protein interaction
large and small adenosine deaminases
CD26-dipeptidyl peptidase IV
enzyme-substrate and enzyme-inhibitor interactions
Opis:: The importance of ADA (adenosine deaminase) in the immune system and the role of its interaction with an ADA-binding cell membrane protein dipeptidyl peptidase IV (DPPIV), identical to the activated immune cell antigen, CD26, has attracted the interest of researchers for many years. To investigate the specific properties in the structure - function relationship of the ADA/DPPIV-CD26 complex, its soluble form, identical to large ADA (LADA), was isolated from human blood serum, human pleural fluid and bovine kidney cortex. The kinetic constants (Km and Vmax) of LADA and of small ADA (SADA), purified from bovine lung and spleen, were compared using adenosine (Ado) and 2'-deoxyadenosine (2'-dAdo) as substrates. The Michaelis constant, Km, evidences a higher affinity of both substrates (in particular of more toxic 2'-dAdo) for LADA and proves the modulation of toxic nucleoside neutralization in the extracellular medium due to complex formation between ADA and DPPIV-CD26. The values of Vmax are significantly higher for SADA, but the efficiency, Vmax /Km, in LADA-catalyzed 2'-dAdo deamination is higher than that in Ado deamination. The interaction of all enzyme preparations with derivatives of adenosine and erythro-9-(2-hydroxy-3-nonyl)adenine (EHNA) was studied. 1-DeazaEHNA and 3-deazaEHNA demonstrate stronger inhibiting activity towards LADA, the DPPIV-CD26-bound form of ADA. The observed differences between the properties of the two ADA isoforms may be considered as a consequence of SADA binding with DPPIV-CD26. Both SADA and LADA indicated a similar pH-profile of adenosine deamination reaction with the optimum at pHs 6.5 - 7.5, while the pH-profile of dipeptidyl peptidase activity of the ADA/DPPIV-CD26 complex appeared in a more alkaline region.
Źródło:: Acta Biochimica Polonica; 2006, 53, 3; 539-546
0001-527X
Pojawia się w:: Acta Biochimica Polonica
Dostawca treści:: Biblioteka Nauki

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