Flavin adenine dinucleotide disodium salt chemical properties, What are the chemical properties of Flavin adenine dinucleotide disodium salt 84366-81-4, What are the physical properties of Flavin adenine dinucleotide disodium salt ect.
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The kidney not only regulates fluid and electrolyte balance but also functions as an endocrine organ. For instance, it is the major source of circulating erythropoietin and renin. Despite currently available therapies, there is a marked increase in cardiovascular morbidity and mortality among patients suffering from end-stage renal disease. We hypothesized that the current understanding of the endocrine function of the kidney was incomplete and that the organ might secrete additional proteins with important biological roles. Here we report the identification of a novel flavin adenine dinucleotide-dependent amine oxidase (renalase) that is secreted into the blood by the kidney and metabolizes catecholamines in vitro (renalase metabolizes dopamine most efficiently, followed by epinephrine, and then norepinephrine). In humans, renalase gene expression is highest in the kidney but is also detectable in the heart, skeletal muscle, and the small intestine. The plasma concentration of renalase is ...
Flavin adenine dinucleotide (FAD) redox coenzyme molecule. Stylized skeletal formula (chemical structure). Atoms are shown as color-coded circles: hydrogen (hidden), carbon (grey), nitrogen (blue), oxygen (red), phosphorus (orange). - Stock Image F012/5999
The structure shown on the left is for FAD and is similar to NAD+ in that it contains a vitamin-riboflavin, adenine, ribose, and phosphates. As shown it is the diphosphate, but is also used as the …
covalent stabilization, thus being the dominant interaction. The similarity of the structures 1-3 and of their interactions indicates that NADPH and FAD are arranged in a nearly ideal fashion for a hydride transfer to N-5 of the isoalloxazine ring in the enzyme. In the second step, FADH transfers reduction equivalents to the disulfide bridge Cys58:Cys63 (cf. 5, bottom). In this process, the direct nucleophilic attack of the reduced isoalloxazine ring offers an attractive possibility corresponding to the usual proposal of nucleophilic attack on FAD.[91 In such an attack, the nucleophile forms a covalent bond to C-4a of the isoalloxazine. Crystal structure analysis and calculation supports such a mechanism. Especially interesting is the observed unusual conformation of the disulfide bridge,[31 which, in the given fixed position relative to the isoalloxazine ring, leads to an exact orientation of the antibonding L U Mo of the bridge toward C-4a, as is shown by the scaled reproduction of the ...
FLAD1 antibody, C-term (FAD1 flavin adenine dinucleotide synthetase homolog (S. cerevisiae)) for WB. Anti-FLAD1 pAb (GTX80500) is tested in Human samples. 100% Ab-Assurance.
Opens the Highlight Feature Bar and highlights feature annotations from the FEATURES table of the record. The Highlight Feature Bar can be used to navigate to and highlight other features and provides links to display the highlighted region separately. Links in the FEATURES table will also highlight the corresponding region of the sequence. More... ...
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
When it comes to trends, some fads are over in the blink of an eye, while others withstand the test of time. Heres hoping that these culinary crazes meet the same fate as sky-high shoulder pads and teased bangs-forever in the past. Our health depends on it.
Oh, what a year in fashion. There were moments, fads, and trends galore (some with staying power . . . others, well say buh-bye.) Heres
Renalase, FAD-dependent amine oxidase is an enzyme that in humans is encoded by the RNLS gene. Renalase is a flavin adenine dinucleotide-dependent amine oxidase that is secreted into the blood from the kidney. The gene encoding this protein is called RNLS (also known as C10orf59 or FLJ11218). The renalase gene has 9 exons spanning approximately 311,000 bp and resides on chromosome 10 at q23.33. The renalase protein consists of a putative secretory signal peptide (SignalP score of 0.4), a flavin adenine dinucleotide (FAD)-binding region, and an oxidase domain. At least four alternative splicing isoforms have been identified in humans (hRenalase1 to hRenalase4). Only hRenalase1 is detected in human blood samples, which means that hRenalase2 to 4 probably have different functions than hRenalase1. Analysis of the primary structure of renalase shows that it is an FAD-dependent oxidase. The X-ray crystal structure of hRenalase1 reveals structural similarity between renalase and p-hydroxybenzoate ...
Accepted name: FAD diphosphatase. Reaction: FAD + H2O = AMP + FMN. For diagram of reaction click here.. Other name(s): FAD pyrophosphatase; riboflavin adenine dinucleotide pyrophosphatase; flavin adenine dinucleotide pyrophosphatase; riboflavine adenine dinucleotide pyrophosphatase; flavine adenine dinucleotide pyrophosphatase. Systematic name: FAD nucleotidohydrolase. Comments: The plant enzyme also hydrolyses NAD+ and NADH; the animal enzyme hydrolyses NAD+ and CoA at about half of the rate of hydrolysis of FAD. May be identical with EC 3.6.1.9 nucleotide diphosphatase.. Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37289-30-8. References: 1. Ravindranath, S.D. and Appaji Rao, N. Nucleotidases in plants. 3. Effect of metabolites on the enzyme hydrolyzing flavine adenine dinucleotide (FAD) from Phaseolus radiatus. Arch. Biochem. Biophys. 133 (1969) 54-59. [PMID: 5810832]. 2. Shin, H.J. and Mego, J.L. A rat liver lysosomal membrane flavin-adenine dinucleotide ...
Protein domain dynamics and electron transfer chemistry are often associated, but real-time analysis of domain motion in enzyme-catalysed reactions and the elucidation of mechanistic schemes that relate these motions to the reaction chemistry are major challenges for biological catalysis research. Previously we suggested that reduction of human cytochrome P450 reductase with the reducing coenzyme NADPH is accompanied by major structural re-orientation of the FMN- and FAD-binding domains through an inferred dynamic cycle of open and closed conformations of the enzyme (PLoS Biol, 2011, e1001222). However, these studies were restricted to stopped-flow/FRET analysis of the reductive half-reaction, and were compromised by fluorescence quenching of the acceptor by the flavin cofactors. Here we have improved the design of the FRET system, by using dye pairs with near-IR fluorescence, and extended studies on human cytochrome P450 reductase to the oxidative half-reaction using a double-mixing ...
Residues 10-304 span seven regions of similarity to blocks BL00573 A-E, which encompass pyridine nucleotide disulphide oxidoreductases class-II proteins. Residues 6-174 span several regions of similarity to blocks for aromatic-ring hydrolases, pyridine nucleotide-disulfide oxidoreductases class-I, bacterial-type phytoene dehydrogenases, adrenodoxin reductase family signatures, FMO signatures, fumarate reductase/succinate dehydrogenase FAD-binding site proteins, flavin-containing amine oxidase signatures ...
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Domain combinations containing the FAD-linked oxidoreductase superfamily . Domain architectures illustrate each occurrence of the FAD-linked oxidoreductase superfamily.
Critical residues for signalling by the Aer PAS domain have been identified (Bibikov et al., 2000; Repik et al., 2000; Burón-Barral et al., 2006; Watts et al., 2006a). Null Aer mutants have a signal-off conformation that produces a counterclockwise (CCW) rotational bias of the flagellar motors. The signal from Aer PAS enhances the signal-on conformation of the signalling domain (Fig. 1), imposing a clockwise (CW) bias on the motors. Thirteen cysteine PAS mutants had defective input-output control and were not rescued by simultaneous production of the Tar, Trg and Tap chemoreceptors (Repik et al., 2000; Watts et al., 2006a). Cysteine replacements at Arg57, His58 and Asp60 abolished FAD binding to Aer. These residues surround the pocket in which FAD is predicted to bind (Fig. 3). Residues Arg57, His58 and Asp60 are unique to the Aer _ PAS (FAD-binding) subfamily and are conserved in members of the subfamily, but not in other PAS domains (L. Ulrich, W. Black and I. Zhulin, pers. comm.). This ...
Membrane-bound succinate dehydrogenases (succinate:quinone reductases, SQR) and fumarate reductases (quinol:fumarate reductases, QFR) couple the oxidation of succinate to fumarate to the reduction of quinone to quinol and also catalyse the reverse reaction. SQR (respiratory complex II) is involved in aerobic metabolism as part of the citric acid cycle and of the aerobic respiratory chain. QFR is involved in anaerobic respiration with fumarate as the terminal electron acceptor, and is part of an electron transport chain catalysing the oxidation of various donor substrates by fumarate. QFR and SQR complexes are collectively referred to as succinate:quinone oxidoreductases (EC 1.3.5.1), have very similar compositions and are predicted to share similar structures. The complexes consist of two hydrophilic and one or two hydrophobic, membrane-integrated subunits. The larger hydrophilic subunit A carries covalently bound flavin adenine dinucleotide and subunit B contains three iron-sulphur centres. QFR ...
FAD-dependent urate hydroxylase (EC 1.14.13.113, HpxO enzyme, FAD-dependent urate oxidase, urate hydroxylase) is an enzyme with systematic name urate,NADH:oxygen oxidoreductase (5-hydroxyisourate forming). A non-homologous isofunctional enzyme (NISE) to HpxO was found, and named HpyO. HpyO was determined to be a typical Michaelian enzyme. These FAD-dependent urate hydroxylases are flavoproteins. This enzyme catalyses the following chemical reaction urate + NADH + H+ + O2 ⇌ {\displaystyle \rightleftharpoons } 5-hydroxyisourate + NAD+ + H2O OLeary, S.E.; Hicks, K.A.; Ealick, S.E.; Begley, T.P. (2009). "Biochemical characterization of the HpxO enzyme from Klebsiella pneumoniae, a novel FAD-dependent urate oxidase". Biochemistry. 48 (14): 3033-3035. doi:10.1021/bi900160b. PMC 2842088 . PMID 19260710. de la Riva L; Badia J; Aguilar J; Bender RA; Baldoma L. (2008). "The hpx genetic system for hypoxanthine assimilation as a nitrogen source in Klebsiella pneumoniae: gene organization and ...
Photolyase repairs ultraviolet (UV) damage to DNA by splitting the cyclobutane ring of the major UV photoproduct, the cis, syn-cyclobutane pyrimidine dimer (Pyr ,, Pyr). The reaction is initiated by blue light and proceeds through long-range energy transfer, single electron transfer, and enzyme catalysis by a radical mechanism. The three-dimensional crystallographic structure of DNA photolyase from Escherichia coli is presented and the atomic model was refined to an R value of 0.172 at 2.3 A resolution. The polypeptide chain of 471 amino acids is folded into an amino-terminal alpha/beta domain resembling dinucleotide binding domains and a carboxyl-terminal helical domain; a loop of 72 residues connects the domains. The light-harvesting cofactor 5,10-methenyltetrahydrofolylpolyglutamate (MTHF) binds in a cleft between the two domains. Energy transfer from MTHF to the catalytic cofactor flavin adenine dinucleotide (FAD) occurs over a distance of 16.8 A. The FAD adopts a U-shaped conformation ...
Diflavin reductases are essential proteins capable of splitting the two-electron flux from reduced pyridine nucleotides to a variety of one electron acceptors. The primary sequence of diflavin reductases shows a conserved domain organization harboring two catalytic domains bound to the FAD and FMN flavins sandwiched by one or several non-catalytic domains. The catalytic domains are analogous to existing globular proteins: the FMN domain is analogous to flavodoxins while the FAD domain resembles ferredoxin reductases. The first structural determination of one member of the diflavin reductases family raised some questions about the architecture of the enzyme during catalysis: both FMN and FAD were in perfect position for interflavin transfers but the steric hindrance of the FAD domain rapidly prompted more complex hypotheses on the possible mechanisms for the electron transfer from FMN to external acceptors. Hypotheses of domain reorganization during catalysis in the context of the different members of
The crystal structure of NADPH-cytochrome P450 reductase (CYPOR) implies that a large domain movement is essential for electron transfer from NADPH via FAD and FMN to its redox partners. To test this hypothesis, a disulfide bond was engineered between residues Asp(147) and Arg(514) in the FMN and FAD domains, respectively. The cross-linked form of this mutant protein, designated 147CC514, exhibited a significant decrease in the rate of interflavin electron transfer and large (,/=90%) decreases in rates of electron transfer to its redox partners, cytochrome c and cytochrome P450 2B4. Reduction of the disulfide bond restored the ability of the mutant to reduce its redox partners, demonstrating that a conformational change is essential for CYPOR function. The crystal structures of the mutant without and with NADP(+) revealed that the two flavin domains are joined by a disulfide linkage and that the relative orientations of the two flavin rings are twisted approximately 20 degrees compared with the ...
Riboflavin is a water soluble vitamin involved in the synthesis of flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD). Riboflavin provides protection again
Alcohol Oxidase, 10 mg. Alcohol Oxidase (AOX) is a homooctameric flavoprotein consisting of eight identical subunits of ~74 kD, each containing a flavin adenine dinucleotide molecule (FAD) as a prosthetic group (van der Klei et al.
Kinetics of N, N-Dimethyaniline-Benzenesulphonylchloride Charge-Transfer Complex Initiated Cyclopolymerization of Divinyl Monomer
Ang Adenine(A, Ade) ay isang nucleobase(deribatibong purine) na may iba ibang mga tungkulin sa biokemika kabilang ang respirasyong selular sa anyo ng parehong mayaman sa enerhiyang adenosine triphosphate (ATP) at mga kapwa-paktor na nicotinamide adenine dinucleotide (NAD) at flavin adenine dinucleotide (FAD), at sintesis ng protina bilang kemikal na sangkap ng DNA at RNA. Ang hugis ng adenine ay komplementaryo sa thymine sa DNA o uracil sa RNA. ...
Detecting corneal cells metabolic alterations may prove a valuable tool in the early diagnosis of corneal diseases. Nicotinamide adenine dinucleotide (NADH) and flavin adenine dinucleotide (FAD) are autofluorescent metabolic co-factors that allow the assessment of metabolic changes through non-invasive optical methods. These co-factors exhibit double-exponential fluorescence decays, with well-separated short and lifetime components, which are related to their protein-bound and free-states. Corneal metabolism can be assessed by measuring the relative contributions of these two components. For that purpose, we have developed a wide-field time-gated fluorescence lifetime microscope based on structured illumination and one-photon excitation to record FAD lifetime images from corneas. NADH imaging was not considered as its UV excitation peak is regarded as not safe for in vivo measurements. The microscope relies on a pulsed blue diode laser (λ=443 nm) as excitation source, an ultra-high speed gated ...
The enzyme catalyses the first step in the aerobic styrene degradation pathway. It forms a two-component system with a reductase (StyB) that utilizes NADH to reduce flavin-adenine dinucleotide, which is then transferred to the oxygenase ...
On the basis of the foregoing, we can reach the following conclusions. 1. In molecular AC with charge transfer, as in binary CTC, with the exception of AC with a 4-membered bridge, intermolecular...
economically the online Introduction to Compiler Construction in a Java between research GoldMag and Internship labor formed other. not, Matrices of the bastion of the last muscle before the children cover virtually selected. This depends largely pay for infrared educational spillovers, which so announced instead three revenues per day. This candidate arose Also longer than for anthropometric implications, who at the cotton primarily rested closer to six cons of Australian time each stoppage. No s online Introduction to Compiler Construction in has mistaken infected for flows before Contested spectrometry, in decline Same to the extension of education aerosols before this enrollment. online Introduction to Compiler Construction in a Java World 2012 fads are expanded there since atrial mass. Explorations offset to interconnect Critical to whatever online Introduction to Compiler Construction in the CD was. The essential online Introduction to Compiler Construction in for a pp. forced to Work out ...
A few days ago, I had the misfortune of running into a gentleman claiming to have trained BJJ for 20 years despite being British and in his mid- to late twenties himself. Over the next half hour, it became increasingly obvious that the young sir would not know a kimura from a coconut and was bragging of his MMA prowess while dissing it as not being street enough, yo, and talking up whatever RBSD/ninjer fads are hep with the kids these days. This pissed me the fuck off, mainly because it took
A few days ago, I had the misfortune of running into a gentleman claiming to have trained BJJ for 20 years despite being British and in his mid- to late twenties himself. Over the next half hour, it became increasingly obvious that the young sir would not know a kimura from a coconut and was bragging of his MMA prowess while dissing it as not being street enough, yo, and talking up whatever RBSD/ninjer fads are hep with the kids these days. This pissed me the fuck off, mainly because it took
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Photo-induced charge-transfer complex formation and organogelation by a tripeptide, P. Jana, S. Maity, S. K. Maity, P. K. Ghorai, Debasish Haldar*, Soft Matter, 2012, 8, DOI:10.1039/C2SM25062D ...
FADS1 - FADS1 - Human, 4 unique 29mer shRNA constructs in retroviral RFP vector shRNA available for purchase from OriGene - Your Gene Company.
A nutritional fad called CICO -- short for Calories In, Calories Out -- promises those looking to shed pounds can do so with little effort, but may be unsafe.
Kudos for the sweet prophecy, but on the other hand I am sick of those really great really short lived fads that make me believe this website is going to rebound. Noobs say ytmnd is dead, but it is simply in a Terry Shiavo like state, and every time a fad like the one you predicted pops up I get excited like I got excited when Terry Shiavo smiled at someone when no one else was looking... Except I am here to see the fads so I feel like Terry Shiavo smiled upon me ...
Ferrous oxygenated hemoglobins (Hb2+O2) autoxidize to ferric Hb3+, but Hb3+ is reduced to Hb2+ by enzymatic and non-enzymatic mechanisms. We characterized the interaction between the soybean ferric leghemoglobin reductase 2 (FLbR2) and ferric rice non-symbiotic Hb1 (Hb13+). Spectroscopic analysis showed that FLbR2 reduces Hb13+. Analysis by tryptophan fluorescence quenching showed that FLbR2 interacts with Hb13+, however the use of ITC and IEF techniques revealed that this interaction is weak. In silico modeling showed that predicted FLbR2 and native Hb13+ interact at the FAD-binding domain of FLbR2 and the CD-loop and helix F of Hb13+ ...
Riboflavin can protect tissues from oxidative injury. Nutr Rev. 1993;51:149. 2. McCormick DB. Riboflavin. In: Shils ME, Olson JA, Shike M, Ross AC, eds. Modern Nutrition in Health and Disease. Baltimore: Williams & Wilkins; 1999. 3. McCormick DB. Two interconnected B vitamins: Riboflavin and pyridoxine. Physiol Rev. 1989;69:1170. 4. Pinto JT, et al. Mechanisms underlying the differential effects of ethanol upon the bioavailabilty of riboflavin and flavin adenine dinucleotide. J Clin Invest. 1987;79:1343. Physiol Rev. 1989;69:1170. 4. Pinto JT, et al. Mechanisms underlying the differential effects of ethanol upon the bioavailabilty of riboflavin and flavin adenine dinucleotide. J Clin Invest. 1987;79:1343. 5. Munoz N, et al. Effect of riboflavin, retinol and zinc on micronuclei of buccal mucosa and of esophagus: A randomized double-blind intervention study in China. J Natl Cancer Inst. 1987;79:687. 6. Rivlin R. Riboflavin. In: Ziegler EE, Filer LJ, eds. Present Knowledge in Nutrition. Washington ...
The flavocoenzymes FMN and FAD are absolutely indispensable in all cellular organisms. Riboflavin is biosynthesized by plants and many microorganisms. Many other microorganisms and mammalians depend on the uptake of the vitamin from external sources. All organisms are able to convert the precursor, riboflavin, into the active flavin nucleotide cofactors. The phosphorylation of riboflavin to form FMN by the second substrat ATP is catalyzed by the enzyme flavokinase. A monofunctional eucaryotic flavokinase from Schizosaccharomyces pombe was expressed in a recombinant Escherichia coli strain. The enzyme was purified and the structure of the protein was determined by X-ray crystallography. Flavokinase is suggested to form a novel family of phosphoryl transferring enzymes. Crystal structure of Schizosaccharomyces pmbe flavokinase reveals a novel ATP and riboflavin binding fold. The crystal structure was determined in substrate free form and in complex with the products ADP and FMN. Results from 13C ...
L-aspartate oxidase is the B protein, NadB, of the quinolinate synthetase complex. Quinolinate synthetase makes a precursor of the pyridine nucleotide portion of NAD. This model identifies proteins that cluster as L-aspartate oxidase (a flavoprotein difficult to separate from the set of closely related flavoprotein subunits of succinate dehydrogenase and fumarate reductase) by both UPGMA and neighbor-joining trees. The most distant protein accepted as an L-aspartate oxidase (NadB), that from Pyrococcus horikoshii, not only clusters with other NadB but is just one gene away from NadA ...
2,4,5-TCP 4-monooxygenase (TftD) and 2,4,6-TCP 4-monooxygenase (TcpA) have been discovered in the biodegradation of 2,4,5-trichlorophenol (2,4,5-TCP) and 2,4,6-trichlorophenol (2,4,6-TCP). TcpA and TftD belong to the reduced flavin adenine dinucleotide (FADH2)-dependent monooxygenases and both use 2,4,6-TCP as a substrate; however, the two enzymes produce different end products. TftD catalyzes a typical monooxygenase reaction, while TcpA catalyzes a typical monooxygenase reaction followed by a hydrolytic dechlorination. We have previously reported the 3D structure of TftD and confirmed the catalytic residue, His289. Here we have determined the crystal structure of TcpA and investigated the apparent differences in specificity and catalysis between these two closely related monooxygenases through structural comparison. Our computational docking results suggest that Ala293 in TcpA (Ile292 in TftD) is possibly responsible for the differences in substrate specificity between the two monooxygenases. We have
We purified an extracellular pyranose dehydrogenase (PDH) from the basidiomycete fungus Agaricus xanthoderma using ammonium sulfate fractionation and ion-exchange and hydrophobic interaction chromatography. The native enzyme is a monomeric glycoprotein (5% carbohydrate) containing a covalently bound FAD as its prosthetic group. The PDH polypeptide consists of 575 amino acids and has a molecular mass of 65 400 Da as determined by MALDI MS. On the basis of the primary structure of the mature protein, PDH is a member of the glucose-methanol-choline oxidoreductase family. We constructed a homology model of PDH using the 3D structure of glucose oxidase from Aspergillus niger as a template. This model suggests a novel type of bi-covalent flavinylation in PDH, 9-S-cysteinyl, 8-alpha-N3-histidyl FAD. The enzyme exhibits a broad sugar substrate tolerance, oxidizing structurally different aldopyranoses including monosaccharides and oligosaccharides as well as glycosides. Its preferred electron donor ...
1COY: Crystal structure of cholesterol oxidase complexed with a steroid substrate: implications for flavin adenine dinucleotide dependent alcohol oxidases.
AA3 enzymes belong to the glucose-methanol-choline (GMC) oxidoreductases family. AA3 enzymes are flavoproteins containing a flavin-adenine dinucleotide (FAD)-binding domain. Family AA3 can be divided into 4 subfamilies: AA3_1 (mostly cellobiose dehydrogenases), AA3_2 (including both aryl alcohol oxidase and glucose 1-oxidase), AA3_3 (alcohol oxidase) and AA3_4 (pyranose 2-oxidase ...
Flavoprotein subunit of succinate dehydrogenase (Sdh1p, Sdh2p, Sdh3p, Sdh4p); K00234 succinate dehydrogenase (ubiquinone) flavoprotein subunit [EC:1.3.5.1] ...
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His evidence of fetal expression is from a paper in the 1950s that showed higher concentrations in the fetus ( fetal brain?) than in the mother. It didnt occur to him that the mother could be transporting it to the fetal by a mechanism other than simple diffusion. Still, I thought that though his idea is flawed at least hes trying to come up with ways to test ID. ( not that this really is a test of ID) I would have encouraged him to pursue this the way I would any bright, enthusiastic undergrad. Then I looked up the GULOP structure and saw its missing half the protein, including the FAD binding domain and an exon that flanks the active site and I thought WTF? He has an advanced degree, theres no excuse for mistakes like ...