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  Indian J Med Microbiol
 

Figure 1: Nucleotide and deduced amino acid sequence of E. oleifera ƒÒ-ketoacyl-[ACP] synthase II (EoKAS-II) cDNA clone. An open reading frame and non-coding regions are shown in capital and small letters, respectively. The deduced amino acid sequence is given below the nucleotide sequence, which is numbered at the both ends of each sequence line. The open reading frame encodes for a protein of 562 amino acid residues. Amino acid residues are numbered beginning with the initial Methionine (m) till last Lysine (k) residue. Initiation and termination codons are shown in bold. The 'ƒÒ-ketoacyl-[ACP] synthase (KAS) (type I and II)', 'Elongating' condensing enzymes and 'Condensing enzymes super-family conserved domain (multi-domain) residues (170 to 543) are highlighted in green color. Residues (1 to 562) underlined with pink color line are part of the '3-oxoacyl-[ACP] synthase II' domain (region ame="PLN02787"). *represent the termination codon. This cDNA clone was isolated by random method of gene isolation from E. oleifera 17-week-old fruit-mesocarp tissue cDNA library

Figure 1: Nucleotide and deduced amino acid sequence of E. oleifera ƒÒ-ketoacyl-[ACP] synthase II (EoKAS-II) cDNA clone. An open reading frame and non-coding regions are shown in capital and small letters, respectively. The deduced amino acid sequence is given below the nucleotide sequence, which is numbered at the both ends of each sequence line. The open reading frame encodes for a protein of 562 amino acid residues. Amino acid residues are numbered beginning with the initial Methionine (m) till last Lysine (k) residue. Initiation and termination codons are shown in bold. The 'ƒÒ-ketoacyl-[ACP] synthase (KAS) (type I and II)', 'Elongating' condensing enzymes and 'Condensing enzymes super-family
conserved domain (multi-domain) residues (170 to 543) are highlighted in green color. Residues (1 to 562) underlined with pink color line are part of the '3-oxoacyl-[ACP] synthase II' domain (region  ame=