The long chain fatty acids incorporated into plant lipids are derived from the iterative addition of C2 units which is provided by malonyl-CoA to an acyl-CoA after interactions with 3-ketoacyl-CoA synthase (KCS), found in several plants. This study provides functional characterization of three 3 ketoacyl CoA synthase like proteins in Vitis vinifera (one) and Oryza brachyantha (two proteins). Sequence analysis reveals that protein of Oryza brachyantha shows 96% similarity to a hypothetical protein in Sorghum bicolor; total 11 homologs were predicted in Sorghum bicolor. Conserved domain prediction confirm the presence of FAE1/Type III polyketide synthase-like protein, Thiolase-like, subgroup; Thiolase-like and 3-Oxoacyl-ACP synthase III, C-terminal and chalcone synthase like domain but very long chain 3-keto acyl CoA domain is absent. All three proteins were found to have Chalcone and stilbene synthases C terminal domain which is similar to domain of thiolase and β keto acyl synthase. Its N terminal domain is absent in J3M9Z7 protein of Oryza brachyantha and F6HH63 protein of Vitis vinifera. Differences in N-terminal domain is responsible for distinguish activity. The J3MF16 protein of Oryza brachyantha contains N terminal domain and C terminal domain and characterized using annotation of these domains. Domains Gcs (streptomyces coelicolor) and Chalcone-stilbene synthases (KAS) in 2-pyrone synthase (Gerbera hybrid) and chalcone synthase 2 (Medicago sativa) were found to be present in three proteins. This similarity points toward anthocyanin biosynthetic process. Similarity to chalcone synthase 2 reveals its possible role in Naringenine and Chalcone synthase like activity. In 3 keto acyl CoA synthase of Oryza brachyantha. Active site residues C-240, H-407, N-447 are present in J3MF16 protein that are common in these three protein at different positions. Structural variations among dimer interface, product binding site, malonyl-CoA binding sites, were predicted in localized combination of conserved residues.

Alzheimer's disease (AD) is a neurodegenerative disorder that is characterized by normal memory loss and cognitive impairment in humans. Many drug targets and disease-modulating therapies are available for treatment of AD, but none of these are effective enough in reducing problems associated with recognition and memory. Potential drug targets so far reported for AD are β-secretase, γ-secretase, amyloid beta (Aβ) and Aβ fibrils, glycogen synthase kinase-3 (GSK-3), acyl-coenzyme A: cholesterol acyl-transferase (ACAT) and acetylcholinesterase (AChE). Herbal remedies (antioxidants) and natural metal-chelators have shown a very significant role in reducing the risk of AD, as well as lowering the effect of Aβ in AD patients. Researchers are working in the direction of antisense and stem cell-based therapies for a cure for AD, which mainly depends on the clearance of misfolded protein deposits -including Aβ, tau, and alpha-synuclein. Computational approaches for inhibitor designing, interaction analysis, principal descriptors and an absorption, distribution, metabolism, excretion and toxicity (ADMET) study could speed up the process of drug development with higher efficacy and less chance of failure. This paper reviews the known drugs, drug targets, and existing and future therapies for the treatment of AD.

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Metabolic Control Analysis provides a quantitative description of concentration dynamics with the change in system parameters. A metabolic Control Analysis aids determination of the threshold value of metabolites involved in a reaction and also helps to understand the role of various parameters in a reaction. In this work, a metabolic model of a Naringenine chalcone biosynthetic reaction is defined and a time series simulation was carried out based on the law of Mass action. Initial concentration of p-Coumaroyl-CoA and Malonyl-CoA were taken 5.0*10-2 mM 2.2*10-3 mM respectively. This concentration was then simulated over time for 10 seconds to find the steady state. Final concentration of  Naringenine chalcone,CO2, and CoA becomes 8.593946e-004 mM after 5.00 second of simulation at reaction constant 6.587753e-005 mM*ml/s. Steady state solution shows that Initial concentration of Naringenine chalcone was 2.199777e-003 mM which is eventually converted into 2.785128e+013 seconds half-life concentration of product at 7.898e-017 mM/s rate and  0.000000e+000 mM*ml/s  rate constant. Phenylpropanoid pathway was analysed to predict all the enzymes that can maximise and minimise the concentration of  Malonyl-CoA and P-Coumaroyl-CoA which leads to flavonoid biosynthesis. In the Phenylpropanoid pathway four enzymes Phenylalanine/tyrosine ammonia lyase, trans-cinnamate 4-monooxygenase, Phenylalanine ammonia lyase, maximise the flavonoid biosynthesis. This analysis shows that other enzymes minimise the concentrations of  Malonyl-CoA and P-coumaroyl-CoA, these are Cinnamoyl Co A reductase, shikimate O hydroxyl transferase HCT), Oxidoreductase. Furthermore, Protein domain analysis of chalcone synthase mutants ( 1jwx Medicago sativa and 4yjy from Oryza sativa) was done to predict structural features to understand reaction mechanism and structure-based engineering to maximise flavonoid biosynthesis. Natural sequence variation CHS G256A, G256V, G256L, and G256F mutants of residue 256 reduce the size of the active site cavity but quick diversification of product specificity occurs. The threshold concentration of Malonyl-CoA and P-coumaroyl-CoA were predicted, maximisation of this concentration leads to enhanced flavonoid biosynthesis. Inhibition of few enzymes may also maximise the flavonoid biosynthesis if appropriate inhibitors are used and a constant supply of Malonyl-CoA and P-Coumaroyl-CoA is maintained using activator molecules. Chalcone synthase Mutants diversify product specificity that occurs without loss of catalytic activity and any conformational changes.