Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Gyu Hyun Nam"'
Autor:
Gyu Hyun Nam1,2, Do-Hyung Kim1,2, Nam-Chul Ha2,3, Do Soo Jang1,2, Young Sung Yun1,2, Bee Hak Hong1,2, Byung-Ha Oh2,3, Kwan Yong Choi1,2 kchoi@postech.ac.kr
Publikováno v:
Journal of Biochemistry. Jul2003, Vol. 134 Issue 1, p101-110. 10p. 4 Diagrams, 6 Charts, 3 Graphs.
Publikováno v:
FEBS Journal. 272:1999-2011
A structural motif called the small exterior hydrophobic cluster (SEHC) has been proposed to explain the stabilizing effect mediated by solvent-exposed hydrophobic residues; however, little is known about its biological roles. Unusually, in Δ5-3-ket
Autor:
Gyu Hyun Nam, Bee Hak Hong, Kwan Yong Choi, Sun Shin Cha, Young Sung Yun, Heung-Soo Lee, Yun Hee Oh
Publikováno v:
Biochemical Journal. 375:297-305
KSI (ketosteroid isomerase) from Comamonas testosteroni is a homodimeric enzyme that catalyses the allylic isomerization of Delta5-3-ketosteroids to their conjugated Delta4-isomers at a reaction rate equivalent to the diffusion-controlled limit. Base
Autor:
Kwan Yong Choi, Gyu Hyun Nam
Publikováno v:
European Journal of Biochemistry. 269:5280-5287
Tumor necrosis factor (TNF)-related apoptosis inducing ligand (TRAIL) has been known to induce tumor-specific apoptosis and to share the structural and functional characteristics with the proteins of TNF family. Recently, the crystal structure of hum
Autor:
Man K. Song, You Suk Suh, Gyu Hyun Nam, Sung H. Lee, Kwan Yong Choi, Gildon Choi, Won Bae Kim, Chu H. Lee, Sang J. Ha, Young Chul Sung, Hyun Tak Jin, Jun Chang
Publikováno v:
Nature Biotechnology. 20:381-386
Interleukin-12 (IL-12), consisting of p40 and p35 subunits, produces both p70 heterodimer and free p40. p70 is essential for the induction of T-helper 1 (Th1) and cytotoxic T-cell (CTL) immunity, whereas p40 inhibits p70-mediated function. Here, we f
Publikováno v:
Biochemistry. 40:5011-5017
Ketosteroid isomerase (KSI) from Comamonas testosteroni is a homodimeric enzyme with 125 amino acids in each monomer catalyzing the allylic isomerization reaction at rates comparable to the diffusion limit. Kinetic analysis of KSI refolding has been
Autor:
Jae-Hyun Cho, Sunggoo Yun, Kwan Yong Choi, Gyu Hyun Nam, Gildon Choi, Hee Cheon Lee, Do Hyung Kim, Do Soo Jang
Publikováno v:
Biochemistry. 39:13084-13092
Equilibrium and kinetic analyses have been carried out to elucidate the folding mechanism of homodimeric ketosteroid isomerase (KSI) from Comamonas testosteroni. The folding of KSI was reversible since the activity as well as the fluorescence and CD
Autor:
Byung-Ha Oh, Kwan Yong Choi, Jeong-Sun Kim, Do Hyung Kim, Gildon Choi, Min Sung Kim, Gyu Hyun Nam, Do Soo Jang, Nam-Chul Ha
Publikováno v:
Biochemistry. 39:4581-4589
Delta(5)-3-Ketosteroid isomerase from Pseudomonas putida biotype B is one of the most proficient enzymes catalyzing an allylic isomerization reaction at rates comparable to the diffusion limit. The hydrogen-bond network (Asp99... Wat504...Tyr14...Tyr
Autor:
Nam-Chul Ha, Bee Hak Hong, Kwan Yong Choi, Gyu Hyun Nam, Do Hyung Kim, Byung-Ha Oh, Young Sung Yun, Do Soo Jang
Publikováno v:
Journal of biochemistry. 134(1)
Ketosteroid isomerase (KSI) from Pseudomonas putida biotype B is a homodimeric enzyme catalyzing an allylic isomerization of Delta(5)-3-ketosteroids at a rate of the diffusion-controlled limit. The dimeric interactions mediated by Arg72, Glu118, and
Autor:
Sejeong Shin, Do Soo Jang, Kwan Yong Choi, Byung-Ha Oh, Gyu Hyun Nam, Tae-Hee Lee, Young Sung Yun
Publikováno v:
The Journal of biological chemistry. 278(30)
Two homologous Δ5-3-ketosteroid isomerases from Comamonas testosteroni (TI-WT) and Pseudomonas putida biotype B (PI-WT) exhibit different pH activity profiles. TI-WT loses activity below pH 5.0 due to the protonation of the conserved catalytic base,