Search results for "Flavin group"
showing 8 items of 8 documents
Biochemical Properties of Human D-Amino Acid Oxidase
2017
D-amino acid oxidase catalyzes the oxidative deamination of D-amino acids. In the brain, the NMDA receptor coagonist D-serine has been proposed as its physiological substrate. In order to shed light on the mechanisms regulating D-serine concentration at the cellular level, we biochemically characterized human DAAO (hDAAO) in greater depth. In addition to clarify the physical-chemical properties of the enzyme, we demonstrated that divalent ions and nucleotides do not affect flavoenzyme function. Moreover, the definition of hDAAO substrate specificity demonstrated that D-cysteine is the best substrate, which made it possible to propose it as a putative physiological substrate in selected tiss…
Human D-Amino Acid Oxidase: Structure, Function, and Regulation
2018
D-Amino acid oxidase (DAAO) is an FAD-containing flavoenzyme that catalyzes with absolute stereoselectivity the oxidative deamination of all natural D-amino acids, the only exception being the acidic ones. This flavoenzyme plays different roles during evolution and in different tissues in humans. Its three-dimensional structure is well conserved during evolution: minute changes are responsible for the functional differences between enzymes from microorganism sources and those from humans. In recent years several investigations focused on human DAAO, mainly because of its role in degrading the neuromodulator D-serine in the central nervous system. D-Serine is the main coagonist of N-methyl D…
ON THE OCCURRENCE OF RESPIRATORY COMPONENTS IN RAT-LIVER NUCLEI.
1965
Summary 1. Low-temperature spectrophotometric studies have been carried out on rat-liver nuclei isolated by two different procedures. Comparison of nuclei prepared in non-aqueous media with those prepared in high-density sucrose reveals only small quantitative differences. 2. The presence of hemoglobin, cytochrome b 5 , and cytochrome c was detected in both types of nuclei. No cytochrome b , or cytochrome oxidase could be found. Studies on the possible origin of the hemoproteins suggest that hemoglobin and cytochrome b 5 are of extra-nuclear origin. The presence of cytochrome c as a nuclear component could not be ruled out completely although leakage from mitochondria was also considered a …
[26] Isoforms of nitric-oxide synthase: Purification and regulation
1994
Publisher Summary Nitric-oxide synthase (NOS) catalyzes the five-electron oxidation of L-arginine to the nitric oxide radical (.NO) and L-citrulline. Molecular oxygen is the cosubstrate of the enzyme. NO synthase activity has been found in a large variety of cells and tissues. The enzyme exists in several isoforms, three of which have been purified, characterized, and cloned. The activities of all three isoforms are found distributed between the soluble and particulate fractions of cells. Isoform I (from brain) and isoform II (from cytokine-induced macrophages) are mostly soluble proteins. Isoform III from endothelial cells is myristoylated and found predominantly in the particulate fractio…
Study of a medium-size biological molecular association by means of a pair potential semiempirical approach: β-carboline-lumiflavin
1985
The molecular association between some substituted β-carbolines and a model flavin, lumiflavin, has been studied by means of a semiempirical approach proposed by Fraga based on a 1/R expansion of atom-atom pair potentials. Only stacked minima have been considered because of their possible biological interest. The calculations characterize 15 different minimum stacked conformations, most of them occurring in the complexes considered. The structural and energetic effects of 1–Me, 6–OH and 7–OH substituents of β-carboline are discussed. An equilibrium conformation involving geometric overlap between the pteridinic portion of flavin and the indole group of β-carboline is predicted to be the mos…
Theoretical Insight into the Spectroscopy and Photochemistry of Isoalloxazine, the Flavin Core Ring
2006
The electronic singlet-singlet and singlet-triplet electronic transitions of the isoalloxazine ring of the flavin core are studied using second-order perturbation theory within the framework of the CASPT2//CASSCF protocol. The main features of the absorption spectrum are computed at 3.09, 4.28, 4.69, 5.00, and 5.37 eV. The lowest singlet (S1) and triplet (T1) excited states are found to be both of pi character with a singlet-triplet splitting of 0.57 eV. On the basis of the analysis of the computed spin-orbit couplings and the potential energy hypersurfaces built for the relevant excited states, the intrinsic mechanism for photoinduced population of T1 is discussed. Upon light absorption, e…
Facile access to foldable redox-active flavin-peptide conjugates
2021
A convenient approach for the synthesis of foldable redox-active flavin peptide conjugates was established. A model β-hairpin oligopeptide motif was utilized to demonstrate that azidolysine side-chains are readily functionalised with an alkyne-bearing flavine derivative. The folding equilibrium of the peptide backbone as well as the redox behaviour of the flavin moieties remains intact after the conjugation.
Die Glucose-Oxydasen aus Penicillium notatum (Notatin) und Aspergillus niger (Nigerin) I. Isolierung und einige molekulare eigenschaften
1965
Summary By chromatography on carboxymethyl- and diethylaminoethyl-Sephadex pure preparations of the glucose oxidases ( β - d -glucose: oxygen oxidoreductase, EC 1.1.3.4) notatin from Penicillium notatum and nigerin from Aspergillus niger could be obtained. Differences in the binding to the cation- and anion-exchangers indicate that these two glucose oxidases differ markedly with respect to the structures of the respective apoenzymes. A mixture of notatin and nigerin can easily be separated by chromatography. Moreover, there are also structural differences in the neighbourhood of the prosthetic flavin-adenine dinucleotide groups. The flavin-adenine dinucleotide spectrum of notatin is shifted…