Combinatorial biosynthesis of ..
generated through combinatorial biosynthesis, ..
metabolic changes into six hallmarks: (1) deregulated uptake of glucose and amino acids, (2) use of opportunistic modes of nutrient acquisition, (3) use of glycolysis/TCA cycle intermediates for biosynthesis and NADPH prodn., (4) increased demand for nitrogen, (5) alterations in metabolite-driven gene regulation, and (6) metabolic interactions with the microenvironment.
FD-CF Combinatorial Small-Molecule Biosynthesis (A) Schematic of …
Some between the amino acids will yield easily under these forces; rigid bonds will resist.
is an amber, watery fluid, rich in , that separates out when coagulates.
is the serum or watery part of that is separated from the in making .
is an ambiguous term describing either several different forms of protein coded from the same gene, or proteins with amino acid sequence and functional similarities, even when they are products of different genes.
are proteins that bind (oil-soluble substances such as and ) to form lipoproteins.
bifunctionalization - Wiktionary
Many mechanisms have been discovered for how altered glycolytic metabolism fuels tumorigenesis, including the use of glycolytic carbons for synthesis of macromolecular precursors such as amino acids, nucleic acids, and fatty acids for generating proteins, DNA, and membranes for rapid cell proliferation, but there are likely yet unexplored pathways that link the Warburg effect to cancer pathogenicity.
Novobiocin is an aminocoumarin antibiotic ..
Acetyl-CoA carboxylase (ACC) and propionyl-CoA carboxylase (PCC) catalyze the carboxylation of acetyl- and propionyl-CoA to generate malonyl- and methylmalonyl-CoA, respectively. Understanding the substrate specificity of ACC and PCC will (1) help in the development of novel structure-based inhibitors that are potential therapeutics against obesity, cancer, and infectious disease and (2) facilitate bioengineering to provide novel extender units for polyketide biosynthesis. ACC and PCC in Streptomyces coelicolor are multisubunit complexes. The core catalytic beta-subunits, PccB and AccB, are 360 kDa homohexamers, catalyzing the transcarboxylation between biotin and acyl-CoAs. Apo and substrate-bound crystal structures of PccB hexamers were determined to 2.0-2.8 A. The hexamer assembly forms a ring-shaped complex. The hydrophobic, highly conserved biotin-binding pocket was identified for the first time. Biotin and propionyl-CoA bind perpendicular to each other in the active site, where two oxyanion holes were identified. N1 of biotin is proposed to be the active site base. Structure-based mutagenesis at a single residue of PccB and AccB allowed interconversion of the substrate specificity of ACC and PCC. The di-domain, dimeric interaction is crucial for enzyme catalysis, stability, and substrate specificity; these features are also highly conserved among biotin-dependent carboxyltransferases. Our findings enable bioengineering of the acyl-CoA carboxylase (ACCase) substrate specificity to provide novel extender units for the combinatorial biosynthesis of polyketides.