Zobrazeno 1 - 10
of 38
pro vyhledávání: '"M. Kanteev"'
Publikováno v:
Applied and environmental microbiology. 84(23)
An enhanced stability of enzymes in organic solvents is desirable under industrial conditions. The potential of lipases as biocatalysts is mainly limited by their denaturation in polar alcohols. In this study, we focused on selected solvent tunnels i
Publikováno v:
Applied Microbiology and Biotechnology. 99:9449-9461
Enzymatic production of biodiesel by transesterification of triglycerides and alcohol, catalyzed by lipases, offers an environmentally friendly and efficient alternative to the chemically catalyzed process while using low-grade feedstocks. Methanol i
Autor:
Ayelet Fishman, Laura De Luca, Rosaria Gitto, Giovanna Certo, M. Kanteev, Antonio Rapisarda, Maria Rosa Buemi, Stefania Ferro, Laura Ielo, Maria Paola Germanò
Tyrosinase is involved in the production of melanin through the hydroxylation of monophenols to o -diphenols. The role of this enzyme was extensively studied in order to identify new therapeutics preventing skin pigmentation and melanoma. In this wor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c200c875742b706b47f781f0311517d8
http://hdl.handle.net/2318/1835451
http://hdl.handle.net/2318/1835451
Autor:
Ayelet Fishman, M. Kanteev, Daniel Lecina, Victor Guallar, Mor Goldfeder, Batel Deri, Noam Adir
Publikováno v:
Scientific Reports
'Scientific Reports ', vol: 6, pages: 34993-1-34993-10 (2016)
Recercat. Dipósit de la Recerca de Catalunya
instname
UPCommons. Portal del coneixement obert de la UPC
Universitat Politècnica de Catalunya (UPC)
'Scientific Reports ', vol: 6, pages: 34993-1-34993-10 (2016)
Recercat. Dipósit de la Recerca de Catalunya
instname
UPCommons. Portal del coneixement obert de la UPC
Universitat Politècnica de Catalunya (UPC)
Tyrosinases are responsible for melanin formation in all life domains. Tyrosinase inhibitors are used for the prevention of severe skin diseases, in skin-whitening creams and to avoid fruit browning, however continued use of many such inhibitors is c
Publikováno v:
Journal of Molecular Biology. 405:227-237
Tyrosinase is a member of the type 3 copper enzyme family that is involved in the production of melanin in a wide range of organisms. The crystal structures of a tyrosinase from Bacillus megaterium were determined at a resolution of 2.0–2.3 A. The
Publikováno v:
Protein science : a publication of the Protein Society. 24(9)
Tyrosinases are metalloenzymes belonging to the type-3 copper protein family which contain two copper ions in the active site. They are found in various prokaryotes as well as in plants, fungi, arthropods, and mammals and are responsible for pigmenta
Publikováno v:
Biochimica et biophysica acta. 1854(12)
2-Hydroxybiphenyl 3-monooxygenase (HbpA) is an FAD dependent monooxygenase which catalyzes the ortho-hydroxylation of a broad range of 2-substituted phenols in the presence of NADH and molecular oxygen. We have determined the structure of HbpA from t
Publikováno v:
Nature Communications. 5
Tyrosinase is responsible for the two initial enzymatic steps in the conversion of tyrosine to melanin. Many tyrosinase mutations are the leading cause of albinism in humans, and it is a prominent biotechnology and pharmaceutical industry target. Her
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66:1101-1103
Tyrosinases are type 3 copper enzymes that are involved in the production of melanin and have two copper ions in the active site. Here, the crystallization and primary analysis of a tyrosinase fromBacillus megateriumis reported. The purified protein
Publikováno v:
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry. 18(8)
Tyrosinase belongs to the type 3 copper enzyme family, containing a dinuclear copper center, CuA and CuB. It is mainly responsible for melanin production in a wide range of organisms. Although copper ions are essential for the activity of tyrosinase,