Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Angelo Merli"'
Autor:
Anna Palló, Petr V. Konarev, Tamás Szimler, Julianna Oláh, Anita Garamszegi, Éva Gráczer, Mária Vas, Angelo Merli, Anikó Lábas, Manfred S. Weiss, Dmitri I. Svergun, Péter Závodszky
Publikováno v:
Biochemistry. 55:560-574
The key active site residues K185, Y139, D217, D241, D245, and N102 of Thermus thermophilus 3-isopropylmalate dehydrogenase (Tt-IPMDH) have been replaced, one by one, with Ala. A drastic decrease in the kcat value (0.06% compared to that of the wild-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7f899859a88bf69e6e590e9ac0b505a
https://doi.org/10.1021/acs.biochem.5b00839
https://doi.org/10.1021/acs.biochem.5b00839
Autor:
Manfred S. Weiss, Dmitri I. Svergun, Petr V. Konarev, Anna Palló, Mária Vas, Angelo Merli, Éva Gráczer, Julianna Oláh, Péter Závodszky, Tamás Szimler
Publikováno v:
FEBS Letters. 589:240-245
The mutant E270A of Thermus thermophilus 3-isopropylmalate dehydrogenase exhibits largely reduced (∼1%) catalytic activity and negligible activation by K(+) compared to the wild-type enzyme. A 3-4 kcal/mol increase in the activation energy of the c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42cfb772ea97d857ede84b04146faa06
https://doi.org/10.1016/j.febslet.2014.12.005
https://doi.org/10.1016/j.febslet.2014.12.005
Autor:
Anna Palló, Manfred S. Weiss, Éva Gráczer, Julianna Oláh, Angelo Merli, Mária Vas, Péter Závodszky
Publikováno v:
FEBS Journal. 281:5063-5076
The three-dimensional structure of the enzyme 3-isopropylmalate dehydrogenase from the bacterium Thermus thermophilus in complex with Mn2+, its substrate isopropylmalate and its co-factor product NADH at 2.0 A resolution features a fully closed confo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a5dc30beec54dd90186b34c70773c90
https://doi.org/10.1111/febs.13044
https://doi.org/10.1111/febs.13044
Autor:
F. S. Mathews, Bharati Mitra, Angelo Merli, Gian Luigi Rossi, A. Dewanti, Narayanasami Sukumar
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 65:543-552
(S)-Mandelate dehydrogenase (MDH) from Pseudomonas putida, a membrane-associated flavoenzyme, catalyzes the oxidation of (S)-mandelate to benzoylformate. Previously, the structure of a catalytically similar chimera, MDH-GOX2, rendered soluble by the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40e29b46998ccdf5eef73b0fec27a233
https://doi.org/10.1107/s0907444909010270
https://doi.org/10.1107/s0907444909010270
Autor:
Angelo Merli, Marcellus Ubbink, Monica D. Vlasie, Davide Ferrari, Gian Luigi Rossi, Chiara Cavalieri, Nikolai Biermann, Oliver Einsle
Publikováno v:
Biochemistry. 47:6560-6570
Methylamine can be used as the sole carbon source of certain methylotrophic bacteria. Methylamine dehydrogenase catalyzes the conversion of methylamine into formaldehyde and donates electrons to the electron transfer protein amicyanin. The crystal st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4049a76a71cda224024b76b86218b16c
https://doi.org/10.1021/bi7023749
https://doi.org/10.1021/bi7023749
Publikováno v:
Scientific Reports
In living organisms, the conversion of urate into allantoin requires three consecutive enzymes. The pathway was lost in hominid, predisposing humans to hyperuricemia and gout. Among other species, the genomic distribution of the two last enzymes of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14299ffbd6d529ce216fded5858586da
https://doi.org/10.1038/srep13798
https://doi.org/10.1038/srep13798
Autor:
Davide Ferrari, Marilena Di Valentin, Zhi-wei Chen, Angelo Merli, Gian Luigi Rossi, F. Scott Mathews, Victor L. Davidson, Donatella Carbonera
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 9:231-237
EPR studies of the methylamine dehydrogenase (MADH)-amicyanin and MADH-amicyanin-cytochrome c551i crystalline complexes have been performed on randomly oriented microcrystals before and after exposure to the substrate, methylamine, as a function of p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f72ce15b853bd59371693785f65ba6e
https://doi.org/10.1007/s00775-003-0513-0
https://doi.org/10.1007/s00775-003-0513-0
Publikováno v:
Biochemistry. 41:111-119
Binding constants for the nucleotide substrates were determined in two different crystalline forms of pig muscle 3-phosphoglycerate kinase (PGK): the binary complex with 3-phosphoglycerate (3-PG) in which the two domains are in an open conformation (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78c19dd4c5d78ad5ec09162c3bacf9d6
https://doi.org/10.1021/bi0115380
https://doi.org/10.1021/bi0115380
Autor:
Angelo Merlin, Andrea Sottani
Publikováno v:
Acque Sotterranee (2022)
This Technical Note, inspired by some recent international scientific contributions, focuses attention on the relationships existing between the diffusion of per- and polyfluoroalkyl substances and the drinking water environmental sector. Firstly, th
Externí odkaz:
https://doaj.org/article/927014f1603e42588b31ef7ed7e45e73
Autor:
F. Scott Mathews, Ditlev E. Brodersen, Zhi-wei Chen, Barbara Morini, R. C. E. Durley, Gian Luigi Rossi, Victor L. Davidson, Angelo Merli
Publikováno v:
Journal of Biological Chemistry. 271:9177-9180
Enzymatic and electron transfer activities have been studied by polarized absorption spectroscopy in single crystals of both binary and ternary complexes of methylamine dehydrogenase (MADH) with its redox partners. Within the crystals, MADH oxidizes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b814319d5e7a9b4df52db4bf7db5ccd
https://doi.org/10.1074/jbc.271.16.9177
https://doi.org/10.1074/jbc.271.16.9177