Soybeans structure

Many recent stndies of NMR spectroscopy have been reported for structure elucidation of anthocyanins from many plant materials such as carrot, tart berries, boysenberries, " flowers, black soybeans, and anthocyanin and flavonol derivatives in red wine. Ginsti et al. (1998) structurally elucidated two novel diacylated anthocyanins and two monoacylated anthocyanins from radish Raphanus sativus) by one- and two-dimensional NMR. Anderson et al. (2006) applied two-dimensional NMR to characterize carboxypyranoanthocyanins. Two 3-deoxyantho-cyanins, lnteolinidin-5-glncoside, and apigeninidin-5-glucoside were identified by Swinny et al. nsing H and C NMR. 

Phenol, the simplest and industrially more important phenolic compound, is a multifunctional monomer when considered as a substrate for oxidative polymerizations, and hence conventional polymerization catalysts afford insoluble macromolecular products with non-controlled structure. Phenol was subjected to oxidative polymerization using HRP or soybean peroxidase (SBP) as catalyst in an aqueous-dioxane mixture, yielding a polymer consisting of phenylene and oxyphenylene units (Scheme 19). The polymer showed low solubility it was partly soluble in DMF and dimethyl sulfoxide (DMSO) and insoluble in other common organic solvents. 

Triantaphyllou, A.C. (1975) Genetic structure of races of Heterodera glycines and inheritance of ability to reproduce on resistant soybean. Journal of Nematology 7, 356. 

The purple speck disease of soybeans is caused by the fungus Cercospora kikuchii, and additional cash crops such as tobacco, com, sugar, and coffee are damaged by fungi from the genus Cercospora [3]. Cercosporin (3, Chart 7.1), initially isolated in 1957 from Cercospora kikuchii and subsequently from other Cercospora species, was found to be the phototoxin responsible for the destructive nature of the pathogen [4]. For these reasons, the natural product was extensively studied, yet its structure was not elucidated until the 1970s [5]. 

A. Dessen, D. Gupta, S. Sabesan, C. F. Brewer, and J. C. Sacchettini, X-ray crystal structure of the soybean agglutinin crosslinked with a biantennary analog of the blood group I carbohydrate antigen, Biochemistry, 34 (1995) 4933 1-942. 

Although LOX from soybean seed is the best characterized of plant LOXs, this enzyme is present in a wide variety of plant and animal tissues (Liavonchanka and Feussner, 2006). The enzyme occurs in a variety of isoenzymes, which often vary in their optimum pH and in product and substrate specificity. Given the occurrence of multiple LOX isoenzymes in soybean leaves and the proposed roles of these enzymes in the plant metabolism, it is possible that individual isoenzymes play specific functions (Feussner and Wasternack 2002). The molecular structure of soybean LOX is the most reported, and four isoenzymes have been isolated (Baysal and Demirdoven 2007). Soy isoenzyme 1 produces 9- and 13-hydroperoxides (1 9) when the enzyme acts on free PUFA at pH 9.0, its optimum pH (Lopez-Nicolas and others 1999). Soy isoenzyme 2 acts on triglycerides as well as free PUFA leading to 9- and 13-hydroperoxide... 

The peptide sequences obtained for codeinone reductase aligned well with the amino acid sequences for 6 -deoxychalcone synthase (chalcone reductase) from alfalfa, Glycerrhiza, and soybean. Knowledge of the relative positions of the peptides allowed for a quick RT-PCR based isolation of cDNAs encoding codeinone reductase from P. somniferum. The codeinone reductase isoforms are 53 % identical to chalcone reductase from soybean.25 By sequence comparison, both codeinone reductase and chalcone reductase belong to the aldo/keto reductase family, a group of structurally and functionally related NADPH-dependent oxidoreductases, and thereby possibly arise from primary metabolism. Six alleles encoding codeinone... 

Dr Bhushan has a research experience of 41 years. He received prestigious Alexander von Humboldt fellowship of Germany in the year 1988, and worked for research at the University of Oldenburg, and at the University of Giessen, Germany. He received European Economic Community Fellowship in 1992 and worked at University of Bristol, UK, on Rye protein. He is an elected Fellow of the Royal Society of Chemistry, London (including Chartered Chemist). He also worked on establishment of primary structures of proteins of Peanut, Brassica, and Soybean, and published several research papers from Univ of Roorkee. He also worked as post doc fellow at the Washington State University, USA. 

Tuteja JH, Vodkin LO (2008) Structural features of the endogenous CHS silencing and target loci in the soybean genome. Crop Sci 48 S49-S68... 

Zabala G, Vodkin L (2003) Cloning of the pleiotropic T locus in soybean and two recessive alleles that differentially affect structure and expression of the encoded flavonoid 3 hydroxylase. Genetics 163 295-309... 

Purple acid phosphatase (PAP) or tartrate-resistant phosphatase is not thought to be a protein phosphatase but it has a very similar dimetallic active site structure to that found in protein phosphatases. PAPs have been identified in bacteria, plants, mammals, and fungi. The molecular weights (animal 35 kDa, plant 55 kDa) are different and they exhibit low sequence homology between kingdoms but the residues involved in coordination of the metal ions are invariant. " There has been considerable debate as to the identity of the metal ions in PAPs in vivo. Sweet potato, Ipomoea batatas, has been shown to possess two different PAP enzymes and the active site of one of them has been shown to contain one Fe and one Zn " " ion. Another report has established that the active site of a PAP from sweet potato contains one Fe " and one Mn +. The well-characterized red kidney bean enzyme and the soybean enzyme contain Fe " and Zn. Claims that PAP from sweet potato has 2Fe ions or 2Mn ions have been discussed elsewhere. One explanation is that these are different forms of the enzyme, another is that because the metal ions are labile and are rapidly incorporated into the active site, the enzyme contains a mixture of metal ions in vivo and the form isolated depends on the conditions of isolation. 

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