Disease relevance of Xanthacridinum

• Irradiation with ultraviolet light (360 nm) of cell-free extracts, electron-transport particles, and soluble components from Mycobacterium phlei resulted in the loss of malate oxidation by the flavine adenine dinucleotide pathway both in cell-free extracts and reconstituted systems [1].
• Glutathione reductase deficiency in red cells in aplastic anemia. II. Effects of flavine compounds on red cell glutathione reductase [2].

High impact information on Xanthacridinum

• Mechanisms of isoalloxazine (flavine) hydrolysis [3].
• Furthermore, 8-anilino-1-naphthalene sulfonate (ANS) binding to cCSQ closely resembles ANS binding to flavine or nucleotide binding sites [4].
• The presence of flavine oxidases makes them an important intracellular source of H(2)O(2): an obligate product of peroxisomal redox reactions and a key reactive oxygen species [5].
• Third, the activity of flavine adenine dinucleotide-linked glycerophosphate dehydrogenase was found to be decreased to a greater relative extent than the B cell mass [6].
• The kinetics of flavine oxidation--reduction. I. Dismutation in nonaqueous solvent [7].

Biological context of Xanthacridinum

• At higher concentrations, state 4 and uncoupled respiration were inhibited by impairment of electron transfer from NAD- and flavine adenine dinucleotide-linked substrates to the respiratory chain [8].
• 2. The enzymes differ in their electrophoretic properties, tissue distribution, binding with flavine adenine denucleotide, heat stability, molecular size and possibly in subunit structure [9].
• Optimized amino acid sequence alignments of flavoprotein reductases revealed major similarities over protein length, in the binding domains for NAD(P)H, and the flavine centers of pro- and eukaryote systems [10].
• Flavipin and quadrilineatin are potent inhibitors (80% at a concentration of 25 microM) of site III phosphorylation [11].

Anatomical context of Xanthacridinum

• An endogenous inhibitor of amine oxidase (flavine-containing) in the carotid body of the cat [12].

Associations of Xanthacridinum with other chemical compounds

• Compared with luciferase, photoexcitable luciferase has a broader pH range for optimal activity, is more stable under acidic conditions, is less stable under alkaline conditions, and is more resistant at neutral pH to inactivation by heat, urea, and trypsin; A flavine-like chromophore, designated B, can be isolated from photoexcitable luciferase [13].
• Two new artificial photolyase models that recognize pyrimidine dimers in protic and aprotic organic solvents as well as in water through a combination of charge and hydrogen-bonding interactions and use a mimic of the flavine to achieve repair through reductive photoinduced electron transfer are presented [14].
• The mature AIF protein, a flavoprotein (prosthetic group: flavine adenine dinucleotide) with significant homology to plant ascorbate reductases and bacterial NADH oxidases, is normally confined to the mitochondrial intermembrane space [15].
• The other activity, isolated from Aspergillus sp. GE49752, was identified as flavipin, a substituted o-phthalaldehyde [16].
• With the former technic Diphenyl Brilliant Yellow 8G, Clayton Yellow, Thiazol Yellow, Thioflavine T and Seto Flavine T imparted strong to intense selective fluorescence to amyloid [17].

Gene context of Xanthacridinum

• CPR is a flavoprotein containing both flavine-adenine dinucleotide and flavine mononucleotide [18].
• These results suggest the potential participation of flavine monooxygenase and of lipooxygenase or of peroxidases/oxidases having similar characteristics but not of lactoperoxidase or cyclooxygenase [19].
• The results obtained with amidines are discussed in their relationship to other microsomal N-oxygenations both by cytochrome P-450 and flavine-containing monooxygenase [20].

Analytical, diagnostic and therapeutic context of Xanthacridinum

• This ratio was determined from spectroscopic analysis of the FMN in lyophilized samples of the enzyme and by titration of the coenzyme with the flavine specific enzyme inactivator 2-hydroxy-3-butynoate [21].
• The reduced flavine mononucleotide (FMNH2)-luciferase association constant, directly measured by equilibrium dialysis and gel filtration is the same for both luciferases, 3 times 10(-4) Mminus1 at romm temperature, and is significantly different from the kinetic reciprocal Michaelis-Menten constant [22].

References