کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10748548 | 1050275 | 2016 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Structural characterization of an aldo-keto reductase (AKR2E5) from the silkworm Bombyx mori
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کلمات کلیدی
AKRNADPHRT-PCRDLGTIMDL-glyceraldehydeReverse transcriptase PCR - PCR معکوس رونویسیaldo-keto reductase - آلدو کتو ردوکتازSDS-PAGE - الکتروفورز ژل پلی آکریل آمیدSodium dodecyl sulfate polyacrylamide gel electrophoresis - الکتروفورز ژل پلی اتیل آمید سدیم دودسیل سولفاتEnzyme specificity - خاصیت آنزیمProtein crystal structure - ساختار بلوری بلورینTriose phosphate isomerase - سه فسفات ایزومرازpolymerase chain reaction - واکنش زنجیره ای پلیمرازPCR - واکنش زنجیرهٔ پلیمرازLepidoptera - پروانه سانان
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله

چکیده انگلیسی
We report a new member of the aldo-keto reductase (AKR) superfamily in the silkworm Bombyx mori. Based on its amino acid sequence, the new enzyme belongs to the AKR2 family and was previously assigned the systematic name AKR2E5. In the present study, recombinant AKR2E5 was expressed, purified to homogeneity, and characterized. The X-ray crystal structures were determined at 2.2Â Ã
for the apoenzyme and at 2.3Â Ã
resolution for the NADPH-AKR2E5 complex. Our results demonstrate that AKR2E5 is a 40-kDa monomer and includes the TIM- or (β/α)8-barrel typical for other AKRs. We found that AKR2E5 uses NADPH as a cosubstrate to reduce carbonyl compounds such as DL-glyceraldehyde, xylose, 3-hydroxy benzaldehyde, 17α-hydroxy progesterone, 11-hexadecenal, and bombykal. No NADH-dependent activity was detected. Site-directed mutagenesis of AKR2E5 indicates that amino acid residues Asp70, Tyr75, Lys104, and His137 contribute to catalytic activity, which is consistent with the data on other AKRs. To the best of our knowledge, AKR2E5 is only the second AKR characterized in silkworm. Our data should contribute to further understanding of the functional activity of insect AKRs.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 474, Issue 1, 20 May 2016, Pages 104-110
Journal: Biochemical and Biophysical Research Communications - Volume 474, Issue 1, 20 May 2016, Pages 104-110
نویسندگان
Kohji Yamamoto, Akifumi Higashiura, Mamoru Suzuki, Takahiro Shiotsuki, Ryohei Sugahara, Takeshi Fujii, Atsushi Nakagawa,