کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8328574 | 1540206 | 2018 | 36 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Kinetic characterization and structural modeling of an NADP+-dependent succinic semialdehyde dehydrogenase from Anabaena sp. PCC7120
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کلمات کلیدی
NADPN-(2-hydroxyethyl)piperazine-N'-2-ethanesulfonic acid2-(N-cyclohexylamino)ethanesulfonic acidCHESCAPSDTTα-KGHEPESα-ketoglutarate - α-کتوگلووتراتβ-mercaptoethanol - β-merkaptoethanolβ-Me - β-منEDTA - اتیلن دی آمین تترا استیک اسید ethylene diamine tetraacetic acid - اتیلن دیامین تتراستیک اسیدsodium dodecyl sulphate-polyacrylamide gel electrophoresis - الکتروفورز ژل دوده سولفات سدیم پلی آکریل آمیدSDS-PAGE - الکتروفورز ژل پلی آکریل آمیدBis-tris - بیس-تریسdithiothreitol - دیتیوتریتولNAD - نادانnicotinamide adenine dinucleotide - نیکوتین آمید adenine dinucleotidenicotinamide adenine dinucleotide phosphate - نیکوتین آمید adenine dinucleotide phosphate
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
Succinic semialdehyde dehydrogenases (SSADH) of cyanobacteria played a pivotal role in completing the cyanobacterial tricarboxylic acid cycle. The structural information of cofactor preference and catalysis for SSADH from cyanobacteria is currently available. However, the detailed kinetics of SSADH from cyanobacteria were not characterized yet. In this study, an all3556 gene encoding SSADH from Anabaena sp. PCC7120 (ApSSADH) was amplified and the recombinant ApSSADH was purified homogenously. Kinetic analysis showed that ApSSADH was an NADP+-dependent SSADH, which utilized NADP+ and succinic semialdehyde (SSA) as its preferred substrates and the activity of ApSSADH was inhibited by its substrate of SSA. At the same time, the Ser157 residue was found to function as the determinant of cofactor preference. Further study demonstrated that activity and substrate inhibition of ApSSADH would be greatly reduced by the mutation of the residues at the active site. Bioinformatic analysis indicated that those residues were highly conserved throughout the SSADHs. To our knowledge this is the first report exploring the detailed kinetics of SSADH from cyanobacteria.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 108, March 2018, Pages 615-624
Journal: International Journal of Biological Macromolecules - Volume 108, March 2018, Pages 615-624
نویسندگان
Xiaoqin Wang, Chongde Lai, Guofeng Lei, Fei Wang, Haozhi Long, Xiaoyu Wu, Jinyin Chen, Guanghua Huo, Zhimin Li,