کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8290648 | 1536362 | 2013 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Identification, characterization, and crystal structure of an aldo-keto reductase (AKR2E4) from the silkworm Bombyx mori
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کلمات کلیدی
3-dehydroecdysoneDL-glyceraldehydeAKR3DETIMNADPHGSTRT-PCRDLGReverse transcriptase PCR - PCR معکوس رونویسیSDS–PAGE - SDS-PAGEaldo–keto reductase - آلدو کتو ردوکتازsodium dodecyl sulfate–polyacrylamide gel electrophoresis - الکتروفورز ژل دوده سولفات سدیم پلی آکریل آمیدEnzyme specificity - خاصیت آنزیمXylose reductase - ریدکتاز کایسوزCrystal structure - ساختار کریستالیTriose phosphate isomerase - سه فسفات ایزومرازNADH - نادانpolymerase chain reaction - واکنش زنجیره ای پلیمرازPCR - واکنش زنجیرهٔ پلیمرازLepidoptera - پروانه سانانGlutathione transferase - گلوتاتیون ترانسفراز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله

چکیده انگلیسی
A new member of the aldo-keto reductase (AKR) superfamily with 3-dehydroecdysone reductase activity was found in the silkworm Bombyx mori upon induction by the insecticide diazinon. The amino acid sequence showed that this enzyme belongs to the AKR2 family, and the protein was assigned the systematic name AKR2E4. In this study, recombinant AKR2E4 was expressed, purified to near homogeneity, and kinetically characterized. Additionally, its ternary structure in complex with NADP+ and citrate was refined at 1.3Â Ã
resolution to elucidate substrate binding and catalysis. The enzyme is a 33-kDa monomer and reduces dicarbonyl compounds such as isatin and 17α-hydroxy progesterone using NADPH as a cosubstrate. No NADH-dependent activity was detected. Robust activity toward the substrate inhibitor 3-dehydroecdysone was observed, which suggests that this enzyme plays a role in regulation of the important molting hormone ecdysone. This structure constitutes the first insect AKR structure determined. Bound NADPH is located at the center of the TIM- or (β/α)8-barrel, and residues involved in catalysis are conserved.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Archives of Biochemistry and Biophysics - Volume 538, Issue 2, 15 October 2013, Pages 156-163
Journal: Archives of Biochemistry and Biophysics - Volume 538, Issue 2, 15 October 2013, Pages 156-163
نویسندگان
Kohji Yamamoto, David K. Wilson,