ABSTRACT
Isoprenoids are a highly diverse and important group of natural compounds. The enzyme 1-deoxy-D-xylulose-5-phosphate reductoisomerase (DXR) catalyzes a key regulatory step in the non-mevalonate isoprenoid biosynthetic pathway in eubacteria and in plant plastids. For example, in Artemisia annua DXR participates in regulation of the biosynthesis of artemisinin, an important antimalarial drug. We performed phylogenetic analysis using DXR protein sequences from a model prokaryote, Escherichia coli, a picoplanktonic alga, Ostreococcus lucimarinus, and higher plants. The functional domain of DXR was conserved, allowing molecular evolutionary comparisons of both prokaryotic and eukaryotic sequences of DXR. Despite this conservation, for some plant species such as Campthoteca acuminata and Arabidopsis thaliana, phylogenetic relationships of their lineages were consistently violated. Our analysis revealed that plant DXR has an N-terminal transit domain that is likely bipartite, consisting of a chloroplast transit peptide (cTP) and a lumen transit peptide (lTP). Several features observed in the lTP suggest that, while DXR is targeted to the chloroplast, it is localized to the thylakoid lumen. These features include a twin arginine motif, a hydrophobic region, and a proline-rich region. The transit peptide also showed putative motifs for a 14-3-3 binding site with a chaperone phosphorylation site at Thr.
Subject(s)
Aldose-Ketose Isomerases/genetics , Evolution, Molecular , Multienzyme Complexes/genetics , Oxidoreductases/genetics , Plant Proteins/genetics , Terpenes/metabolism , 14-3-3 Proteins/chemistry , Aldose-Ketose Isomerases/chemistry , Aldose-Ketose Isomerases/classification , Amino Acid Sequence , Arabidopsis/enzymology , Binding Sites , Computational Biology , Molecular Sequence Data , Multienzyme Complexes/chemistry , Multienzyme Complexes/classification , Oxidoreductases/chemistry , Oxidoreductases/classification , Phylogeny , Plant Proteins/chemistry , Plant Proteins/classification , Sequence Homology, Amino AcidABSTRACT
Volatile components of three commercial plain sufus or fermented soybean (Glycine max) curds (A-C) were extracted by a supercritical fluid extraction apparatus and analyzed by gas chromatography-mass spectrometry. A total of 83 compounds were found, of which 68 compounds were common among the three samples. Samples A, B, and C had 76, 75, and 74 components, respectively. Alcohols (17), acids (15), and esters (16) were the major classes. The rest of the classes were miscellaneous compounds (9), aldehydes (7), alkanes (5), aromatic compounds (5), ketones (3), furans (2), S-containing compounds (2), and other N-containing compounds (2). Gas chromatography-flame ionization detection-olfactometry analyses identified 17 potent odorants with different odor descriptions such as sour, sweet, fruity, coconut-like, and meaty. Fourteen odorants were further pinpointed by omission experiments among the 17 to be critical to the odor of commercial plain sufu. Acetic acid, methional, ethyl (Z,Z)-9,12-octadecadienoate, ethyl (Z)-9-ocatadecenoate, and 3-methylbutanoic acid were some of the potent odorants found.
