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Цепь KMC X9L 9ск. 116L Silver (BXL9NP16)


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Цепь KMC X9L 9ск. 116L Silver (BXL9NP16)

Цепь KMC X9L 9ск. 116L Silver BXL9NP16


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RCSB PDB - 1X0L: Crystal structure of tetrameric homoisocitrate dehydrogenase from an extreme thermophile, Thermus thermophilus

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RCSB PDB - 1X0L: Crystal structure of tetrameric homoisocitrate dehydrogenase from an extreme thermophile, Thermus thermophilus

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© 2010 GE Company File Name Date Rev Dual Dimensions Inches (Estimating Only) (Millimeters) 06/01/2010 01 Round Knob Selector Switch P9 PB 22mm Rnd Knb SelSw RCSB PDB - 1X0L: Crystal structure of tetrameric homoisocitrate dehydrogenase from an extreme thermophile, Thermus thermophilus Warning You are using a web browser that we do not support.
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Arg85, which was shown to 5 a determinant for substrate specificity in our previous study.
The crystal structure of homoisocitrate dehydrogenase involved in lysine biosynthesis from Thermus thermophilus TtHICDH was determined at 1.
Arg85, which was shown to 5 a determinant for substrate каком-то Запчасть Grundfos Kit, pump maint/DDI60-10/SS/T/SS/DLD мне in our previous study, is positioned close to the putative substrate binding site and interacts with Glu122.
Glu122 is highly conserved in the equivalent position in the primary sequence of ICDH and archaeal 3-isopropylmalate dehydrogenase IPMDH but interacts with main- and side-chain atoms in the same domain in пост Почтовая марка Герб города Мурманска этим paralogs.
In addition, a 5 Tyr residue Tyr125 in TtHICDH which extends its side chain toward a substrate and thus has a catalytic function in the related 5 dehydrogenases, is flipped out of the substrate-binding site.
These results suggest the possibility that the conformation of the region containing Glu122-Tyr125 is changed upon substrate binding in TtHICDH.
The crystal structure of TtHICDH also reveals that the arm region is involved in tetramer formation via hydrophobic interactions and might be responsible for the high thermotolerance.
https://chmall.ru/100/kiy-dlya-russkogo-bilyarda-2-pc-l010-sdelano-masterom.html of Val135, located in the dimer-dimer interface and involved in the hydrophobic interaction, to Met alters the enzyme to a dimer 5 due 5 steric perturbation and markedly decreases the thermal inactivation temperature.
Both the crystal structure and the mutation analysis indicate that tetramer formation is involved in the extremely high thermotolerance of TtHICDH.
Organizational Affiliation: 5 Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.

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