Chorismic acidMethylmalonyl-CoATumor hypoxia: Tumor hypoxia is the situation where tumor cells have been deprived of oxygen. As a tumor grows, it rapidly outgrows its blood supply, leaving portions of the tumor with regions where the oxygen concentration is significantly lower than in healthy tissues.Shikimic acidDAHP synthaseCyclohexeneDicycloverineDiguanylate cyclasePhenylalanine N-monooxygenase: Phenylalanine N-monooxygenase (, phenylalanine N-hydroxylase, CYP79A2) is an enzyme with system name L-phenylalanine,NADPH:oxygen oxidoreductase (N-hydroxylating). This enzyme catalyses the following chemical reactionNitrile hydratase: In enzymology, nitrile hydratases (NHases; ) are mononuclear iron or non-corrinoid cobalt enzymes that catalyse the hydration of diverse nitriles to their corresponding amidesIvar Asbjørn Følling: Ivar Asbjørn Følling (23 August 1888 – 24 January 1973) was a Norwegian physician and biochemist who first described the disease named after him—Følling's disease—which is better known outside of Norway as phenylketonuria or, for short, PKU. He was born in Kvam, Steinkjer.Biopterin-dependent aromatic amino acid hydroxylase: In molecular biology, the biopterin-dependent aromatic amino acid hydroxylases (abbreviated AAAH) constitute a family of aromatic amino acid hydroxylases, including phenylalanine 4-hydroxylase (), tyrosine 3-hydroxylase (), and tryptophan 5-hydroxylase (). These enzymes primarily hydroxylate phenylalanine, tyrosine, and tryptophan, respectively.Allosteric regulationCyanohydrinGlutamate-1-semialdehydeProtein-ribulosamine 3-kinase: Protein-ribulosamine 3-kinase (, FN3KRP, FN3K-related protein, FN3K-RP, ketosamine 3-kinase 2, fructosamine-3-kinase-related protein, ribulosamine/erythrulosamine 3-kinase, ribulosamine 3-kinase) is an enzyme with system name ATP:(protein)-N6-D-ribulosyl-L-lysine 3-phosphotransferase. This enzyme catalyses the following chemical reactionStreptomyces aureofaciens: Streptomyces aureofaciens is a species of Streptomyces, and the source of many tetracycline antibiotics. The organism was first isolated at Sanborn Field on the University of Missouri campus in Columbia, Missouri, US; the site became a National Historic Landmark.Brevibacterium iodinum: Brevibacterium iodinum is a Gram-positive soil bacterium. It can often be found among the normal cutaneous flora of healthy people, particularly in humid environments, and is only very rarely involved in opportunistic infections.Tryptophan operon leaderNon-receptor tyrosine kinase: Non-receptor tyrosine kinases (nRTKs) are cytoplasmic enzymes that are responsible for catalysing the transfer of a phosphate group from a nucleoside triphosphate donor, such as ATP, to tyrosine residues in proteins. Non-receptor tyrosine kinases are a subgroup of protein family tyrosine kinases, enzymes that can transfer the phosphate group from ATP to a tyrosine residue of a protein (phosphorylation).DivinylbenzeneList of strains of Escherichia coli: Escherichia coli is a well studied bacterium that was first identified by Theodor Escherich, after whom it was later named.N-(p-amylcinnamoyl)anthranilic acidVitamin B12-binding domain: In molecular biology, the vitamin B12-binding domain is a protein domain which binds to cobalamin (vitamin B12). It can bind two different forms of the cobalamin cofactor, with cobalt bonded either to a methyl group (methylcobalamin) or to 5'-deoxyadenosine (adenosylcobalamin).Phosphoserine transaminase: Phosphoserine transaminase (, PSAT, phosphoserine aminotransferase, 3-phosphoserine aminotransferase, hydroxypyruvic phosphate-glutamic transaminase, L-phosphoserine aminotransferase, phosphohydroxypyruvate transaminase, phosphohydroxypyruvic-glutamic transaminase, 3-O-phospho-L-serine:2-oxoglutarate aminotransferase, SerC, PdxC, 3PHP transaminase) is an enzyme with system name O-phospho-L-serine:2-oxoglutarate aminotransferase. This enzyme catalyses the following chemical reactionCyclohexaneAcid catalysis: In acid catalysis and base catalysis a chemical reaction is catalyzed by an acid or a base. The acid is the proton donor and the base is the proton acceptor.Phosphotransferase: Phosphotransferases are a category of enzymes (EC number 2.7) that catalyze phosphorylation reactions.Coles PhillipsProtein primary structure: The primary structure of a peptide or protein is the linear sequence of its amino acid structural units, and partly comprises its overall biomolecular structure. By convention, the primary structure of a protein is reported starting from the amino-terminal (N) end to the carboxyl-terminal (C) end.Glutamine amidotransferase: In molecular biology, glutamine amidotransferases (GATase) are enzymes which catalyse the removal of the ammonia group from a glutamine molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. This activity is found in a range of biosynthetic enzymes, including glutamine amidotransferase, anthranilate synthase component II, p-aminobenzoate, and glutamine-dependent carbamoyl-transferase (CPSase).Glucose-methanol-choline oxidoreductase family: In molecular biology, the glucose-methanol-choline oxidoreductase family (GMC oxidoreductase) is a family of enzymes with oxidoreductase activity.Burst kinetics: Burst kinetics is a form of enzyme kinetics that refers to an initial high velocity of enzymatic turnover when adding enzyme to substrate. This initial period of high velocity product formation is referred to as the "Burst Phase".Reaction coordinateLigation-independent cloning: Ligation-independent cloning (LIC) is a form of molecular cloning that is able to be performed without the use of restriction endonucleases or DNA ligase. This allows genes that have restriction sites to be cloned without worry of chopping up the insert.Temporal feedback