Zobrazeno 1 - 10
of 34
pro vyhledávání: '"Carlo A. Raia"'
Publikováno v:
Applied Biochemistry and Biotechnology. 170:1482-1490
The synthesis of the aroma chemical cinnamyl alcohol (CMO) by means of enzymatic reduction of cinnamaldehyde (CMA) was investigated using NADH-dependent alcohol dehydrogenase from Bacillus stearothermophilus both as an isolated enzyme, and in recombi
Publikováno v:
Extremophiles (Tokyo, Print) 14 (2010): 193–204. doi:10.1007/s00792-009-0298-3
info:cnr-pdr/source/autori:Pennacchio A; Giordano A; Pucci B; Rossi M; Raia CA./titolo:Biochemical characterization of a recombinant short-chain NAD(H)-dependent dehydrogenase%2Freductase from Sulfolobus acidocaldarius./doi:10.1007%2Fs00792-009-0298-3/rivista:Extremophiles (Tokyo, Print)/anno:2010/pagina_da:193/pagina_a:204/intervallo_pagine:193–204/volume:14
info:cnr-pdr/source/autori:Pennacchio A; Giordano A; Pucci B; Rossi M; Raia CA./titolo:Biochemical characterization of a recombinant short-chain NAD(H)-dependent dehydrogenase%2Freductase from Sulfolobus acidocaldarius./doi:10.1007%2Fs00792-009-0298-3/rivista:Extremophiles (Tokyo, Print)/anno:2010/pagina_da:193/pagina_a:204/intervallo_pagine:193–204/volume:14
The gene encoding a novel alcohol dehydrogenase that belongs to the short-chain dehydrogenases/reductases (SDRs) superfamily was identified in the aerobic thermoacidophilic crenarchaeon Sulfolobus acidocaldarius strain DSM 639. The saadh gene was het
Publikováno v:
Extremophiles. 13:751-761
A mutant of the thermostable NAD(+)-dependent (S)-stereospecific alcohol dehydrogenase from Sulfolobus solfataricus (SsADH) which has a single substitution, Trp95Leu, located at the substrate binding pocket, was fully characterized to ascertain the r
Publikováno v:
Biopolymers. 83:595-613
Increasing attention is being paid to the role of selenium, both as an essential component required for the activity of many enzymes and in the context of selenium-based pharmaceutical agents. A wide range of therapeutics that include selenium are on
Autor:
Mosè Rossi, Ilaria Bruno, Carlo A. Raia, Luciana Esposito, Adriana Zagari, Antonietta Giordano, Filomena Sica, Lelio Mazzarella
Publikováno v:
FEBS letters
539 (2003): 14–18.
info:cnr-pdr/source/autori:Esposito L., Bruno I., Sica F., Raia C.A., Giordano A., Rossi M., Mazzarella L., Zagari A./titolo:Structural study of a single-point mutant of Sulfolobus solfataricus alcohol dehydrogenase with enhanced activity./doi:/rivista:FEBS letters (Print)/anno:2003/pagina_da:14/pagina_a:18/intervallo_pagine:14–18/volume:539
539 (2003): 14–18.
info:cnr-pdr/source/autori:Esposito L., Bruno I., Sica F., Raia C.A., Giordano A., Rossi M., Mazzarella L., Zagari A./titolo:Structural study of a single-point mutant of Sulfolobus solfataricus alcohol dehydrogenase with enhanced activity./doi:/rivista:FEBS letters (Print)/anno:2003/pagina_da:14/pagina_a:18/intervallo_pagine:14–18/volume:539
Alcohol dehydrogenase from Sulfolobus solfataricus (SsADH) is the only enzyme from Archaea among the structurally studied members of the medium-chain ADH family described so far. Here, we present the three-dimensional structure of the apo form of the
Autor:
Carlo A. Raia, Antonietta Giordano
Publikováno v:
Journal of Fluorescence. 13:17-24
Alcohol dehydrogenase from the thermoacidophilic Sulfolobus solfataricus (SsADH) is a thermophilic NAD+-dependent homotetrameric zinc enzyme whose crystal structure has been recently determined at 1.85 A resolution by using a selenomethionine-substit
Publikováno v:
Scopus-Elsevier
Protein engineering
15 (2002): 215–223.
info:cnr-pdr/source/autori:Casadio R., Martelli P. L., Giordano A., Rossi M., Raia C. A./titolo:A low-resolution 3D model of the tetrameric alcohol dehydrogenase from Sulfolobus solfataricus/doi:/rivista:Protein engineering (Print)/anno:2002/pagina_da:215/pagina_a:223/intervallo_pagine:215–223/volume:15
Protein engineering
15 (2002): 215–223.
info:cnr-pdr/source/autori:Casadio R., Martelli P. L., Giordano A., Rossi M., Raia C. A./titolo:A low-resolution 3D model of the tetrameric alcohol dehydrogenase from Sulfolobus solfataricus/doi:/rivista:Protein engineering (Print)/anno:2002/pagina_da:215/pagina_a:223/intervallo_pagine:215–223/volume:15
We describe the computation of a model of the thermophilic NAD-dependent homotetrameric alcohol dehydrogenase from the archaeon Sulfolobus solfataricus (SsADH). Modeling is based on the knowledge that each monomer contains two Zn ions with catalytic
Publikováno v:
Biochemistry. 35:638-647
Reaction of thermostable NAD(+)-dependent alcohol dehydrogenase from Sulfolobus solfataricus with iodoacetate at pH 9.0 and 37 degrees C significantly increases the oxidation rate of aliphatic and aromatic alcohols and decreases the reduction rate of
Autor:
Luciana Esposito, Antonietta Giordano, Adriana Zagari, Mosè Rossi, Carlo A. Raia, Filomena Sica, Lelio Mazzarella
Publikováno v:
Journal of Molecular Biology 318 (2002): 463–477.
info:cnr-pdr/source/autori:Esposito L., Sica F., Raia C. A., Giordano A., Rossi M., Mazzarella L., Zagari A./titolo:Crystal structure of the alcohol dehydrogenase from the hyperthermophilic Archaeon Sulfolobus solfataricus at 1.85 A resolution/doi:/rivista:Journal of Molecular Biology/anno:2002/pagina_da:463/pagina_a:477/intervallo_pagine:463–477/volume:318
info:cnr-pdr/source/autori:Esposito L., Sica F., Raia C. A., Giordano A., Rossi M., Mazzarella L., Zagari A./titolo:Crystal structure of the alcohol dehydrogenase from the hyperthermophilic Archaeon Sulfolobus solfataricus at 1.85 A resolution/doi:/rivista:Journal of Molecular Biology/anno:2002/pagina_da:463/pagina_a:477/intervallo_pagine:463–477/volume:318
The crystal structure of a medium-chain NAD(H)-dependent alcohol dehydrogenase (ADH) from an archaeon has been solved by multiwavelength anomalous diffraction, using a selenomethionine-substituted enzyme. The protein (SsADH), extracted from the hyper
Autor:
Vincenzo Sannino, Luciana Esposito, Mosè Rossi, Carlo A. Raia, Giosué Sorrentino, Angela Pennacchio
Publikováno v:
Applied microbiology and biotechnology. 97(9)
The gene encoding a novel alcohol dehydrogenase that belongs to the short-chain dehydrogenases/reductases superfamily was identified in the aerobic thermoacidophilic crenarchaeon Sulfolobus acidocaldarius strain DSM 639. The saadh2 gene was heterolog