scholarly journals 3-Hydroxy-3-Methylglutaryl-CoA Reductase (HMGR) Enzyme of the Sterol Biosynthetic Pathway: A Potential Target against Visceral Leishmaniasis

2018 ◽  
Author(s):  
Sushma Singh ◽  
N. Kishore Babu
Keyword(s):  
Visceral Leishmaniasis ◽  
Biosynthetic Pathway ◽  
Potential Target ◽  
Sterol Biosynthetic Pathway ◽  
Coa Reductase

scholarly journals Molecular Characterization of a Poly-β-Hydroxybutyrate-Producing Microbacterium Isolate

2015 ◽  
Vol 3 (2) ◽  
pp. 143-150 ◽  
Author(s):  
Yehia A. Osman ◽  
Ahmed Abd Elrazak ◽  
Wesam Khater ◽  
EL-Shahat Nashy ◽  
Attia Mohamadeen
Keyword(s):  
Biosynthetic Pathway ◽  
Nitrogen Deficiency ◽  
Rrna Gene ◽  
Excess Carbon ◽  
Controlling Elements ◽  
Tree Data ◽  
Microbacterium Paraoxydans ◽  
Coa Reductase ◽  
Beta Hydroxybutyrate

Bacterial poly-β-hydroxybutyrate (PHB) is a natural, biodegradable polymer, which is accumulated in the cells as an energy reserve materialdue to depletion of nitrogen or phosphorous in the presence of excess carbon source. This polymer is foreseen to possess high industrialpotentiality and excellent alternative to the non-degradable petroleum-based plastics. In this study, we isolated and characterized a localbacterial strain WA81 which accumulated 18mg/L PHB after 72 h growth in mineral salt medium under nitrogen deficiency. The PHB granuleswere detected in the cells using TEM and the genes encode for this polymer were detected by oligonucleotide primers using PCR technology.The 16S rRNA gene nucleotide sequence for this isolate was used to construct a phylogentic tree against all available sequences in the GenBank.The phylogenetic tree data suggested that the closest type strain to the local bacterium is the Microbacterium paraoxydans CF36T and hencewe named it Microbacterium sp. strain WA81. Moreover, the set of enzymes responsible for the PHB biosynthetic pathway and their controllingelements were detected in this local isolate using PCR. The genes encode for the biosynthesis enzymes are phbA (β-ketothiolase), phbB(acetoacetly CoA reductase), phbC (PHB polymerase), while the genes encode for the controlling elements are phbP (phasin), phbZ (PHBdepolymerase). The novelty of this local bacterium lies in its ability to accumulate huge amounts of PHB in its cytoplasm and the presence ofa whole set of genes encode for the PHB biosynthetic and catabolic pathways of this polymer.Int J Appl Sci Biotechnol, Vol 3(2): 143-150 DOI: http://dx.doi.org/10.3126/ijasbt.v3i2.12277 

Bacterial Lipoprotein Biosynthetic Pathway as a Potential Target for Structure-based Design of Antibacterial Agents

2020 ◽  
Vol 27 (7) ◽  
pp. 1132-1150 ◽  
Author(s):  
Jie Xia ◽  
Bo Feng ◽  
Gang Wen ◽  
Wenjie Xue ◽  
Guixing Ma ◽  
...  
Keyword(s):  
Drug Design ◽  
Active Sites ◽  
Biosynthetic Pathway ◽  
Antibacterial Agents ◽  
Biochemical Characterization ◽  
Global Public Health ◽  
Structure Based Drug Design ◽  
Key Enzymes ◽  
Potential Target ◽  
Bacterial Lipoprotein

Background: Antibiotic resistance is currently a serious problem for global public health. To this end, discovery of new antibacterial drugs that interact with novel targets is important. The biosynthesis of lipoproteins is vital to bacterial survival and its inhibitors have shown efficacy against a range of bacteria, thus bacterial lipoprotein biosynthetic pathway is a potential target. Methods: At first, the literature that covered the basic concept of bacterial lipoprotein biosynthetic pathway as well as biochemical characterization of three key enzymes was reviewed. Then, the recently resolved crystal structures of the three enzymes were retrieved from Protein Data Bank (PDB) and the essential residues in the active sites were analyzed. Lastly, all the available specific inhibitors targeting this pathway and their Structure-activity Relationship (SAR) were discussed. Results: We briefly introduce the bacterial lipoprotein biosynthetic pathway and describe the structures and functions of three key enzymes in detail. In addition, we present much knowledge on ligand recognition that may facilitate structure-based drug design. Moreover, we focus on the SAR of LspA inhibitors and discuss their potency and drug-likeness. Conclusion: This review presents a clear background of lipoprotein biosynthetic pathway and provides practical clues for structure-based drug design. In particular, the most up-to-date knowledge on the SAR of lead compounds targeting this pathway would be a good reference for discovery of a novel class of antibacterial agents.

scholarly journals Identification of the Polyhydroxyalkanoate (PHA)-Specific Acetoacetyl Coenzyme A Reductase among Multiple FabG Paralogs in Haloarcula hispanica and Reconstruction of the PHA Biosynthetic Pathway in Haloferax volcanii

2009 ◽  
Vol 75 (19) ◽  
pp. 6168-6175 ◽  
Author(s):  
Jing Han ◽  
Qiuhe Lu ◽  
Ligang Zhou ◽  
Hailong Liu ◽  
Hua Xiang
Keyword(s):  
Biosynthetic Pathway ◽  
Coenzyme A ◽  
Reductase Activity ◽  
Halophilic Archaea ◽  
Haloferax Volcanii ◽  
Pha Synthase ◽  
Haloarcula Marismortui ◽  
Coa Reductase ◽  
Haloarcula Hispanica ◽  
Acetoacetyl Coa Reductase

ABSTRACT Genome-wide analysis has revealed abundant FabG (β-ketoacyl-ACP reductase) paralogs, with uncharacterized biological functions, in several halophilic archaea. In this study, we identified for the first time that the fabG1 gene, but not the other five fabG paralogs, encodes the polyhydroxyalkanoate (PHA)-specific acetoacetyl coenzyme A (acetoacetyl-CoA) reductase in Haloarcula hispanica. Although all of the paralogous fabG genes were actively transcribed, only disruption or knockout of fabG1 abolished PHA synthesis, and complementation of the ΔfabG1 mutant with the fabG1 gene restored both PHA synthesis capability and the NADPH-dependent acetoacetyl-CoA reductase activity. In addition, heterologous coexpression of the PHA synthase genes (phaEC) together with fabG1, but not its five paralogs, reconstructed the PHA biosynthetic pathway in Haloferax volcanii, a PHA-defective haloarchaeon. Taken together, our results indicate that FabG1 in H. hispanica, and possibly its counterpart in Haloarcula marismortui, has evolved the distinct function of supplying precursors for PHA biosynthesis, like PhaB in bacteria. Hence, we suggest the renaming of FabG1 in both genomes as PhaB, the PHA-specific acetoacetyl-CoA reductase of halophilic archaea.

Induction of potato steroidal glycoalkaloid biosynthetic pathway by overexpression of cDNA encoding primary metabolism HMG-CoA reductase and squalene synthase

Planta ◽  
2011 ◽  
Vol 235 (6) ◽  
pp. 1341-1353 ◽  
Author(s):  
Idit Ginzberg ◽  
Muddarangappa Thippeswamy ◽  
Edna Fogelman ◽  
Ufuk Demirel ◽  
Alice M. Mweetwa ◽  
...  
Keyword(s):  
Biosynthetic Pathway ◽  
Squalene Synthase ◽  
Primary Metabolism ◽  
Hmg Coa Reductase ◽  
Coa Reductase ◽  
Steroidal Glycoalkaloid

scholarly journals 3-Hydroxy-3-methylglutaryl-coenzyme A reductase in normal and dystrophic hamsters

1982 ◽  
Vol 201 (3) ◽  
pp. 501-504 ◽  
Author(s):  
M C Greenough ◽  
R J Boegman
Keyword(s):  
Diurnal Variation ◽  
Biosynthetic Pathway ◽  
Dark Period ◽  
Normal Male ◽  
Hmg Coa Reductase ◽  
Cholesterol Biosynthetic Pathway ◽  
Normal Males ◽  
Coa Reductase ◽  
Rate Limiting ◽  
The Brain

The activity and diurnal variation of 3-hydroxy-3-methyglutaryl-CoA reductase (EC 1.1.1.34; HMG-CoA reductase), the rate-limiting enzyme in the cholesterol-biosynthetic pathway, of normal and dystrophic hamsters was determined. Liver enzyme activity showed a diurnal pattern in the normal male, but not in the dystrophic male. Enzyme values in normal males at the midpoint of the 12 h dark period were 10 times those in dystrophic males. No evidence for diurnal variation in the HMG-CoA reductase of the brain was observed, and similar activities were found for normal and dystrophic animals. The apparent Km for HMG-CoA reductase from the liver of normal or dystrophic hamsters was approx. 9 microM, and the Vmax. was 5.9 and 21.7 pmol/min per mg of protein for dystrophic and normal hamsters respectively.

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