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- W2367053595 abstract "Pyruvate dehydrogenase (PDH) is the former enzyme in pyruvate dehydrogenase complex and participates in generating acetyl coenzyme A,the initiator of tricarboxylic acid (TCA) cycle.It also plays a decisive role in the distribution of nutrition composition.By means of in silico cloning,RT-PCR and rapid amplification of cDNA ends (RACE) technology,a full-length cDNA which was similar to Drosophila melanogaster lethal(1) G0344 gene with pyruvate dehydrogenase function was cloned from silkworm (Bombyx mori) and designated as Bm-l(1) .It is 1 630 bp long,contains a complete ORF of 1 200 bp,186 bp of 5'-UTR and 207 bp of 3'-UTR.Bm-l(1) gene contains 8 exons and 7 introns.It encodes 399 amino acids,with predicted molecular mass of 43.93 kD and isoelectric point of 8.07.The deduced amino acids showed that an E1-dh domain was located between the 69th and the 365th amino acid residues.This structural domain is uniquely owned by thiamine pyrophosphate dependent dehydrogenases.Protein seconda-ry structure prediction showed that 28.8% of the protein is composed of α helix and 12.0% of β sheet.Multiple sequence alignment with Clustal W program revealed that Bm-l(1) coded protein has over 63% sequence identity with PDHs from Tribolium castaneum and other insect species.Nevertheless,their conservative regions are in high consensus.Bm-l(1) mRNA had high transcriptional levels during the whole egg,larval,and pupal stages,and in emerging adults,head,silk gland,gonad,fat body,midgut and hemolymph of 3-day-old larvae of the 5th instar,and the difference between tissues was relatively low." @default.
- W2367053595 created "2016-06-24" @default.
- W2367053595 creator A5083830696 @default.
- W2367053595 date "2010-01-01" @default.
- W2367053595 modified "2023-09-23" @default.
- W2367053595 title "Molecular Cloning,Sequence Structure and Expression Analysis of Bm-l (1) Gene with Pyruvate Dehydrogenase Function in the Silkworm,Bombyx mori" @default.
- W2367053595 hasPublicationYear "2010" @default.
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