Related Research Articles
In biochemistry, flavin adenine dinucleotide (FAD) is a redox-active coenzyme associated with various proteins, which is involved with several enzymatic reactions in metabolism. A flavoprotein is a protein that contains a flavin group, which may be in the form of FAD or flavin mononucleotide (FMN). Many flavoproteins are known: components of the succinate dehydrogenase complex, α-ketoglutarate dehydrogenase, and a component of the pyruvate dehydrogenase complex.
Flavoproteins are proteins that contain a nucleic acid derivative of riboflavin. These proteins are involved in a wide array of biological processes, including removal of radicals contributing to oxidative stress, photosynthesis, and DNA repair. The flavoproteins are some of the most-studied families of enzymes.
The branched-chain α-ketoacid dehydrogenase complex is a multi-subunit complex of enzymes that is found on the mitochondrial inner membrane. This enzyme complex catalyzes the oxidative decarboxylation of branched, short-chain alpha-ketoacids. BCKDC is a member of the mitochondrial α-ketoacid dehydrogenase complex family comprising pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase, key enzymes that function in the Krebs cycle.
Any enzyme system that includes cytochrome P450 protein or domain can be called a P450-containing system.
In enzymology, a 2-methyl-branched-chain-enoyl-CoA reductase (EC 1.3.8.5) is an enzyme that catalyzes the chemical reaction
In enzymology, a 3-hydroxyphenylacetate 6-hydroxylase (EC 1.14.13.63) is an enzyme that catalyzes the chemical reaction
In enzymology, a 4-hydroxyacetophenone monooxygenase (EC 1.14.13.84) is an enzyme that catalyzes the chemical reaction:
In enzymology, a 4-hydroxybenzoate 1-hydroxylase (EC 1.14.13.64) is an enzyme that catalyzes the chemical reaction
The enzyme 4-hydroxybenzoate 3-monooxygenase, also commonly referred to as para-hydroxybenzoate hydroxylase (PHBH), is a flavoprotein belonging to the family of oxidoreductases. Specifically, it is a hydroxylase, and is one of the most studied enzymes and catalyzes reactions involved in soil detoxification, metabolism, and other biosynthetic processes.
In enzymology, a 4-hydroxybenzoate 3-monooxygenase [NAD(P)H] (EC 1.14.13.33) is an enzyme that catalyzes the chemical reaction
4-hydroxyphenylacetate 3-monooxygenase (EC 1.14.14.9) is an enzyme that catalyzes the chemical reaction
In enzymology, an anthraniloyl-CoA monooxygenase (EC 1.14.13.40) is an enzyme that catalyzes the chemical reaction
In enzymology, an unspecific monooxygenase (EC 1.14.14.1) is an enzyme that catalyzes the chemical reaction
In enzymology, a D-lactate dehydrogenase (cytochrome) is an enzyme that catalyzes the chemical reaction
In enzymology, a styrene-oxide isomerase is an enzyme that catalyzes the chemical reaction
2,6-Dihydroxypyridine is an alkaloid with the molecular formula C5H3N(OH)2. It is a colorless solid. 2,6-Dihyroxypyridine is an intermediate in the degradation of nicotine.
6-Hydroxynicotinate 3-monooxygenase (EC 1.14.13.114, NicC, 6HNA monooxygenase, HNA-3-monooxygenase) is an enzyme with systematic name 6-hydroxynicotinate,NADH:oxygen oxidoreductase (3-hydroxylating, decarboxylating). This enzyme catalyses the following chemical reaction
4-nitrocatechol 4-monooxygenase (EC 1.14.13.166) is an enzyme with systematic name 4-nitrocatechol,NAD(P)H:oxygen 4-oxidoreductase (4-hydroxylating, nitrite-forming). This enzyme catalyses the following chemical reaction:
The flavin-containing monooxygenase (FMO) protein family specializes in the oxidation of xeno-substrates in order to facilitate the excretion of these compounds from living organisms. These enzymes can oxidize a wide array of heteroatoms, particularly soft nucleophiles, such as amines, sulfides, and phosphites. This reaction requires an oxygen, an NADPH cofactor, and an FAD prosthetic group. FMOs share several structural features, such as a NADPH binding domain, FAD binding domain, and a conserved arginine residue present in the active site. Recently, FMO enzymes have received a great deal of attention from the pharmaceutical industry both as a drug target for various diseases and as a means to metabolize pro-drug compounds into active pharmaceuticals. These monooxygenases are often misclassified because they share activity profiles similar to those of cytochrome P450 (CYP450), which is the major contributor to oxidative xenobiotic metabolism. However, a key difference between the two enzymes lies in how they proceed to oxidize their respective substrates; CYP enzymes make use of an oxygenated heme prosthetic group, while the FMO family utilizes FAD to oxidize its substrates.
L-ornithine N5 monooxygenase (EC 1.14.13.195 or EC 1.14.13.196) is an enzyme which catalyzes one of the following chemical reactions:
L-ornithine + NADPH + O2 N(5)-hydroxy-L-ornithine + NADP+ + H2O L-ornithine + NAD(P)H + O2 N(5)-hydroxy-L-ornithine + NAD(P)+ + H2O
References
- ↑ Mooney A, Ward PG, O'Connor KE (August 2006). "Microbial degradation of styrene: biochemistry, molecular genetics, and perspectives for biotechnological applications". Applied Microbiology and Biotechnology. 72 (1): 1–10. doi:10.1007/s00253-006-0443-1. PMID 16823552.
- 1 2 Montersino S, Tischler D, Gassner GT, van Berkel WJ (September 2011). "Catalytic and structural features of flavoprotein hydroxylases and epoxidases". Advanced Synthesis & Catalysis. 353 (13): 2301–19. doi:10.1002/adsc.201100384.
- ↑ van Berkel WJ, Kamerbeek NM, Fraaije MW (August 2006). "Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts" (PDF). Journal of Biotechnology. 124 (4): 670–89. doi:10.1016/j.jbiotec.2006.03.044. hdl: 11370/99a1ac5c-d4a4-4612-90a3-4fe1d4d03a11 . PMID 16712999.
