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Neoxanthin synthase (NXS) is an important enzyme in carotenoid biosynthesis. Here, the BoaNXS gene was cloned from yellow flower Chinese kale, and preformed for bioinformatics analysis. The BoaNXS gene contains an open reading frame of 699 bp that encodes a 232 - amino acid protein with a calculated molecular mass of 25.52 kD and an isoelectric point (pI) of 9.6. Subcellular localization predicted that the BoaNXS was in the chloroplast. The functional domain of the BoaNXS protein contains DUF4281 Super family. Homology analysis indicates that the NXS protein is apparently conserved during plant evolution, and BoaNXS is most closely related to Brassica napus, and B. oleracea var. oleracea. The findings of the present study provide a theoretical basis for the elucidation of NXS gene function in Chinese kale. [ABSTRACT FROM AUTHOR]

AOP3 is an important enzyme gene for secondary metabolism of glucosinolate side chain. In this study, the Brassica oleracea var. capitata AOP3 (BocAOP3) gene sequence was obtained from Brassica database (BRAD), and preformed for bioinformatics analysis. The analysis results indicated that BocAOP3 gene contains an open reading frame of 933 bp that encodes a 310 amino acid protein with a calculated molecular mass of 35.48 kD and an isoelectric point (pI) of 6.55. Secondary structure of protein indicated that BocAOP3 protein has 10 alpha helix, 13 beta sheet, and 25 beta turn and most amino acids are hydrophilic. Subcellular localization predicted BocAOP3 gene was in the cytoplasm. The conserved domain of the BocAOP3 protein is PLN02365. Homology analysis indicated that the BocAOP3 protein is apparently conserved during plant evolution. The results of this study provided a molecular basis for elucidating the BocAOP3 gene function in cabbage. [ABSTRACT FROM AUTHOR]

The AOP2.1 gene is an important gene affecting the side chain modification of aliphatic glucosinolate. Here, the Brassica oleracea var. capitata AOP2.1 (BocAOP2.1) gene sequence was obtained from the Brassica database (BRAD) and subjected to sequence analysis. It is indicated that the BocAOP2.1 gene contains a 1,320 bp open reading frame (ORF) encoding a protein of 439 amino acids with a calculated molecular weight of 48.28 kD, the isoelectric point (pI) is 5.36. The highest number of amino acids is Valine (Val), whereas the lowest number is Tryptophan (Trp). Its prediction formula is C2109H3347N589O682S13 Its total hydrophilicity index is -0.472, the solution instability index is 31.63, and the fat solubility index is 79.23. Sequence alignment indicated that the BocAOP2.1 protein is more closely related to Brassica napus and Brassica juncea, those all belonged to the Cruciferous genus. The results of this study provide a molecular basis for elucidating the function of BocAOP2.1 gene in cabbage. [ABSTRACT FROM AUTHOR]

In this study, we performed bioinformatics analysis toward genome sequence of Lysinibacillussphaericus (L. sphaericus) to determine gene encoded for gelatinase. L. sphaericus was isolated from soil and gelatinase species-specific bacterium to porcine and bovine gelatin. This bacterium offers the possibility of enzymes production which is specific to both species of meat, respectively. The main focus of this research is to identify the gelatinase encoded gene within the bacteria of L. Sphaericus using bioinformatics analysis of partially sequence genome. From the research study, three candidate gene were identified which was, gelatinase candidate gene 1 (P1), NODE_71_length_93919_cov_158.931839_21 which containing 1563 base pair (bp) in size with 520 amino acids sequence; Secondly, gelatinase candidate gene 2 (P2), NODE_23_length_52851_cov_190.061386_17 which containing 1776 bp in size with 591 amino acids sequence; and Thirdly, gelatinase candidate gene 3 (P3), NODE_106_length_32943_cov_169.147919_8 containing 1701 bp in size with 566 amino acids sequence. Three pairs of oligonucleotide primers were designed and namely as, F1, R1, F2, R2, F3 and R3 were targeted short sequences of cDNA by PCR. The amplicons were reliably results in 1563 bp in size for candidate gene P1 and 1701 bp in size for candidate gene P3. Therefore, the results of bioinformatics analysis of L. Sphaericus resulting in gene encoded gelatinase were identified. [ABSTRACT FROM AUTHOR]

The Duck Plague Virus (DPV) is the causative agent of Duck plague, which causes significant economic losses in the commercial duck industry all over the world. Our laboratory had identified and sequenced the DPV UL41 gene. Bioinformatics analysis of DPV UL41 gene were performed by some software and online tools. The results showed that GC content of duck plague virus UL41 gene was 42.42%, which encoded a protein with 498 amino acids in the peptide. The UL41 gene sequence didn't contain a rare codons string with more than two rare codons. The construction of phylogenetic tree suggested DPV had a close evolutionary relationship with the branch of the mardivirus genus, including MeHV-1, GaHV-2 and GaHV-3. [ABSTRACT FROM PUBLISHER]

This report showed some physico-chemical properties and structural features about UL41 protein predicted by some software and on-line tools. The analysis showed both the signal peptide and the trans membrance region are not found. Meanwhile, the protein has twenty-four potential phosphorylation sites. In addition, the protein has more hydrophilic amine acid districts than hydrophobic districts and subcellular localization mainly located at the cytoplasm with 56.5%. The prediction of secondary structure showed that random coils dominate among secondary structure elements followed by alpha helix and extended strand. The prediction of tertiary structure showed the structure of the UL41 protein had a certain level of similarity to the structure-specific nuclease FEN-1(flap endonuclease-1). The study will be a basis for the further functional study of the UL41 protein. [ABSTRACT FROM PUBLISHER]