Category:Team Samurai Rangers

Table 4

Based on table 1: for JadH, both UWM6 and 2,3-dehydro-UWM6 underwent 4a,12b-dehydration and C-12 monooxygenation and were converted to rabelomycin and dehydrorabelomycin, respectively. Rabelomycin remained unchanged. 3) In controls without supplemented enzymes, the substrates remained unchanged.

Based on table 1; for JadH, both UWM6 and 2,3-dehydro-UWM6 underwent 4a,12b-dehydration and C-12 monooxygenation and were converted to rabelomycin and dehydrorabelomycin, respectively. Rabelomycin remained unchanged. 3) In controls without supplemented enzymes, the substrates remained unchanged.

Based on Fig. 5 and 6; Total fatty acid and acyl-CoA measurements of 5-d-old aaBb (null for HAL3A and heterozygous for HAL3B) seedlings in medium lacking Suc revealed stalled storage lipid catabolism and impaired CoA biosynthesis; in particular, acetyl-CoA levels were reduced by approximately 80%. Taken together, these results provide in vivo evidence for the function of HAL3A and HAL3B, and they point out the critical role of CoA biosynthesis during early postgerminative growth.

Fig. 2 shows a liquid chromatography column of mutants. Fig. 2b specifically shows that the RH11 mutant cannot create the enzyme-intermediate needed to catalyze the reaction.

Table 4 and Fig. 4 shows that GluRS can bind both ATP and its tRNA substrate independently, but binding of glutamate requires the presence of tRNAGlu.

Fig. 5 shows geraniol oxidation by CAD1 or GEDH1 to produce geranial.

The amino acid sequence of limonene synthase was purified out of spearmint leaf and put into cDNA. Fig. 4 pLC 5.2 cDNA gave the highest specific activity of limonene synthase expression, which confirms the cDNA to represent this gene.

three types of cDNAs encoding N-methyltransferases were isolated from immature fruits of coffee (Coffea arabica) plants, and designated as CaXMT1, CaMXMT2, and CaDXMT1, respectively. The bacterially expressed encoded proteins were characterized for their catalytic properties. Using these recombinant proteins, catalytic specificity was determined with the following substrates: XMP, xanthosine, xanthine, 1-methylxanthine, 3-methylxanthine, 7-methylxanthine, paraxanthine, theobromine, and theophylline (Fig. ​(Fig.3B–D;3B–D; Table ​TableI).I). CaMXMT2 catalyzed conversion of 7-methylxanthine to theobromine (Fig. ​(Fig.3C,3C, lane 2).

three types of cDNAs encoding N-methyltransferases were isolated from immature fruits of coffee (Coffea arabica) plants, and designated as CaXMT1, CaMXMT2, and CaDXMT1, respectively. The bacterially expressed encoded proteins were characterized for their catalytic properties. Using these recombinant proteins, catalytic specificity was determined with the following substrates: XMP, xanthosine, xanthine, 1-methylxanthine, 3-methylxanthine, 7-methylxanthine, paraxanthine, theobromine, and theophylline (Fig. ​(Fig.3B–D;3B–D; Table ​TableI).I). Purified CaXMT1 solely catalyzed conversion of xanthosine to 7-methylxanthosine (Fig. ​(Fig.3B,3B, lane 2). In contrast, crude CaXMT1 catalyzed conversion of xanthosine to 7-methylxanthine, suggesting that conversion of xanthosine to 7-methylxanthosine and that of 7-methylxanthosine to 7-methylxanthine successively occurred (Fig. ​(Fig.3B,3B, lane 4). Although the former reaction was catalyzed by CaMXT1, the latter was found to be catalyzed by a nonspecific purine-nucleoside phosphorylase derived from E. coli (Fig. ​(Fig.3B,3B, lane 6).

Based on methods: three types of cDNAs encoding N-methyltransferases were isolated from immature fruits of coffee (Coffea arabica) plants, and designated as CaXMT1, CaMXMT2, and CaDXMT1, respectively. The bacterially expressed encoded proteins were characterized for their catalytic properties. Using these recombinant proteins, catalytic specificity was determined with the following substrates: XMP, xanthosine, xanthine, 1-methylxanthine, 3-methylxanthine, 7-methylxanthine, paraxanthine, theobromine, and theophylline (Fig. ​(Fig.3B–D;3B–D; Table ​TableI).I). Purified CaXMT1 solely catalyzed conversion of xanthosine to 7-methylxanthosine

Figure 1 (b) shows the enzyme AmnE, which is 4-oxalocrotonate decarboxylase, catalyzing the reaction from 4-oxalocrotinic acid to 2-oxopent-4-enoic acid. The enzyme was assayed spectrophotometrically using the substrates listed above.