L-Gulonolactone Oxidase
Sugar Alcohol Dehydrogenases
Ascorbic Acid
Sugar Acids
NADPH Oxidase
Ascorbate-mediated electron transfer in protein thiol oxidation in the endoplasmic reticulum. (1/48)
Addition of, or gulonolactone oxidase-dependent in situ generation of, ascorbate provoked the oxidation of protein thiols, which was accompanied by ascorbate consumption in liver microsomal vesicles. The maximal rate of protein thiol oxidation was similar upon gulonolactone, ascorbate or dehydroascorbate addition. Cytochrome P450 inhibitors (econazole, proadifen, quercetin) decreased ascorbate consumption and the gulonolactone or ascorbate-stimulated thiol oxidation. The results demonstrate that the ascorbate/dehydroascorbate redox couple plays an important role in electron transfer from protein thiols to oxygen in the hepatic endoplasmic reticulum, even in gulonolactone oxidase deficient species. (+info)Induction and peroxisomal appearance of gulonolactone oxidase upon clofibrate treatment in mouse liver. (2/48)
Various antihyperlipemic peroxisome proliferators are known to be carcinogenic in rodents but not in human, other primates and guinea pig, which species lost their ability to synthesize ascorbate due to mutations in the gulonolactone oxidase gene. Ascorbate synthesis is accompanied by H2O2 production, consequently its induction can be potentially harmful; therefore, the in vivo effect of the peroxisome proliferator clofibrate was investigated on gulonolactone oxidase expression in mouse liver. Liver weights and peroxisomal protein contents were increased upon clofibrate treatment. Elevated plasma ascorbate concentrations were found in clofibrate-treated mice due to the higher microsomal gulonolactone oxidase activities. Remarkable gulonolactone oxidase activity appeared in the peroxisomal fraction upon the treatment. Increased activity of the enzyme was associated with an elevation of its mRNA level. According to the present results the evolutionary loss of gulonolactone oxidase may contribute to the explanation of the missing carcinogenic effect of peroxisome proliferators in humans. (+info)Random nucleotide substitutions in primate nonfunctional gene for L-gulono-gamma-lactone oxidase, the missing enzyme in L-ascorbic acid biosynthesis. (3/48)
Humans and other primates have no functional gene for L-gulono-gamma-lactone oxidase that catalyzes the last step of L-ascorbic acid biosynthesis. The 164-nucleotide sequence of exon X of the gene was compared among human, chimpanzee, orangutan, and macaque, and it was found that nucleotide substitutions had occurred at random throughout the sequence with a single nucleotide deletion, indicating that the primate L-gulono-gamma-lactone oxidase genes are a typical example of pseudogene. (+info)Different induction of gulonolactone oxidase in aromatic hydrocarbon-responsive or -unresponsive mouse strains. (4/48)
The role of aromatic hydrocarbon receptor (AhR)-mediated signal transduction pathways was investigated in the regulation of ascorbate synthesis by using Ah-responsive and Ah-unresponsive mouse strains. In vivo 3-methylcholanthrene treatment increased hepatic and plasma ascorbate concentrations only in the Ah-responsive strain. The mRNA level of gulonolactone oxidase and the microsomal ascorbate production from p-nitrophenyl glucuronide, D-glucuronic acid or gulonolactone in the liver of Ah-responsive and Ah-unresponsive mice were compared. In Ah-responsive mice, these parameters were higher originally, and they further increased upon in vivo addition of 3-methylcholanthrene, while in Ah-unresponsive mice the treatment was not effective. These results suggest that the transcription of gulonolactone oxidase gene is regulated by an Ah receptor-dependent signal transduction pathway. (+info)Aortic wall damage in mice unable to synthesize ascorbic acid. (5/48)
By inactivating the gene for L-gulono-gamma-lactone oxidase, a key enzyme in ascorbic acid synthesis, we have generated mice that, like humans, depend on dietary vitamin C. Regular chow, containing about 110 mg/kg of vitamin C, is unable to support the growth of the mutant mice, which require L-ascorbic acid supplemented in their drinking water (330 mg/liter). Upon withdrawal of supplementation, plasma and tissue ascorbic acid levels decreased to 10-15% of normal within 2 weeks, and after 5 weeks the mutants became anemic, began to lose weight, and die. Plasma total antioxidative capacities were approximately 37% normal in homozygotes after feeding the unsupplemented diet for 3-5 weeks. As plasma ascorbic acid decreased, small, but significant, increases in total cholesterol and decreases in high density lipoprotein cholesterol were observed. The most striking effects of the marginal dietary vitamin C were alterations in the wall of aorta, evidenced by the disruption of elastic laminae, smooth muscle cell proliferation, and focal endothelial desquamation of the luminal surface. Thus, marginal vitamin C deficiency affects the vascular integrity of mice unable to synthesize ascorbic acid, with potentially profound effects on the pathogenesis of vascular diseases. Breeding the vitamin C-dependent mice with mice carrying defined genetic mutations will provide numerous opportunities for systematic studies of the role of antioxidants in health and disease. (+info)Ascorbic acid synthesis in fetal and neonatal pigs and in pregnant and postpartum sows. (6/48)
The ontogeny of ascorbic acid synthesis and its concentration in fetal pigs from mid- to late gestation, and the effect of birth order and premature or normal delivery ages were evaluated. In Experiment 1, fetal pigs were collected from three sows at 60, 80, 100, 107 and 111 d of development. Liver L-gulono-gamma-lactone oxidase (GLO) activity and ascorbic acid concentration were measured. High liver GLO activity in fetal liver occurred at 60 d but declined as pregnancy advanced (P < 0.01), whereas ascorbic acid concentration increased (P < 0.01). Experiment 2 evaluated ascorbic acid synthesis and concentration in neonates born early (1st and 2nd) or late (7th and 8th) in the birthing sequence, or when born 2 d prematurely vs. the normal delivery age. Pigs born early in the birthing sequence (P < 0.01) and those born at the natural delivery age (P < 0.05) had higher liver ascorbic acid concentrations, but liver GLO activity did not differ among groups. Sows were killed at each period; liver GLO activity was constant during gestation but increased postpartum (P < 0.01). Liver ascorbic acid concentration was constant during gestation, except for a decline during late gestation, and increased postpartum (P < 0.05). These results suggest that more ascorbic acid was transferred from the dam to the fetuses as pregnancy advanced, possibly suppressing fetal GLO activity. Thus, fetal liver GLO activity was the primary source of ascorbic acid during early fetal development, but more fetal ascorbic acid was transferred from the dam during later pregnancy. (+info)Liver L-gulonolactone oxidase activity and tissue ascorbic acid concentrations in nursing pigs and the effect of various weaning ages. (7/48)
In Experiment 1, we evaluated liver L-gulono-gamma-lactone oxidase (GLO) activity and tissue concentration of ascorbic acid in young pigs from birth to weaning (14 d) and through a 28-d postweaning period; in Experiment 2, we evaluated the effect of three weaning ages on these measurements. Sow colostrum and milk collected in both experiments demonstrated a linear decline (P < 0.01) in ascorbic acid concentration as lactation progressed. In Experiment 1, three pigs were killed at 0, 3, 7, 14, 21, 28, 35 and 42 d of age for determining liver GLO activity and serum and tissue ascorbic acid. Liver GLO activity decreased by 80% from 0 to 3 d of age and remained low until d 14 (weaning). After weaning, liver GLO activity increased linearly (P < 0.01). Tissue ascorbic acid concentrations decreased during the nursing period and again after weaning, but then increased to 42 d of age (P < 0.01). In Experiment 2, pigs were weaned at 10, 17 or 24 d of age. Three pigs from each group were killed at weaning and at each week postweaning until 38 d of age. Liver GLO activity was low during the nursing period but increased linearly (P < 0.01) for each group during the subsequent postweaning period. Pig serum and tissue ascorbic acid concentrations increased postweaning in each group. These results suggest that a factor in sow's milk, possibly ascorbic acid, suppressed liver GLO activity of nursing pigs but upon weaning, liver GLO activity of pigs increased in a linear manner (P < 0.01). (+info)Vulnerable atherosclerotic plaque morphology in apolipoprotein E-deficient mice unable to make ascorbic Acid. (8/48)
BACKGROUND: Oxidative stress is thought to play an important role in atherogenesis, suggesting that antioxidants could prevent coronary artery disease. However, the efficacy of vitamin C in reducing atherosclerosis is debatable in humans and has not been tested rigorously in animals. METHODS AND RESULTS: Gulo(-/-)Apoe(-/-) mice were used to test a hypothesis that chronic vitamin C deficiency enhances the initiation and development of atherosclerosis. These mice are dependent on dietary vitamin C because of the lack of L-gulonolactone-gamma-oxidase and are prone to develop atherosclerosis because of lacking apolipoprotein E. Beginning at 6 weeks of age, the Gulo(-/-)Apoe(-/-) mice were fed regular chow or Western-type diets containing high fat and supplemented with either 0.033 g or 3.3 g/L of vitamin C in their drinking water. This regimen produced mice with chronically low vitamin C (average 1.5 microg/mL in plasma) or high vitamin C (average 10 to 30 microg/mL in plasma). Morphometric analysis showed that within each sex, age, and diet group, the sizes of the atherosclerotic plaques were not different between low vitamin C mice and high vitamin C mice. However, advanced plaques in the low vitamin C mice had significantly reduced amounts of Sirius red-staining collagen (36.4+/-2.2% versus 54.8+/-2.3%, P<0.0001), larger necrotic cores within the plaques, and reduced fibroproliferation and neovascularization in the aortic adventitia. CONCLUSIONS: Chronic vitamin C deficiency does not influence the initiation or progression of atherosclerotic plaques but severely compromises collagen deposition and induces a type of plaque morphology that is potentially vulnerable to rupture. (+info)L-Gulonolactone oxidase is a human gene that encodes for the enzyme L-gulonolactone oxidase, which is involved in the synthesis of ascorbic acid (vitamin C) in many animals. However, this gene is believed to be nonfunctional in humans due to multiple mutations, and therefore, humans are unable to synthesize vitamin C endogenously. Instead, humans must obtain vitamin C through their diet.
Sugar alcohol dehydrogenases (SADHs) are a group of enzymes that catalyze the interconversion between sugar alcohols and sugars, which involves the gain or loss of a pair of electrons, typically in the form of NAD(P)+/NAD(P)H. These enzymes play a crucial role in the metabolism of sugar alcohols, which are commonly found in various plants and some microorganisms.
Sugar alcohols, also known as polyols, are reduced forms of sugars that contain one or more hydroxyl groups instead of aldehyde or ketone groups. Examples of sugar alcohols include sorbitol, mannitol, xylitol, and erythritol. SADHs can interconvert these sugar alcohols to their corresponding sugars through a redox reaction that involves the transfer of hydrogen atoms.
The reaction catalyzed by SADHs is typically represented as follows:
R-CH(OH)-CH2OH + NAD(P)+ ↔ R-CO-CH2OH + NAD(P)H + H+
where R represents a carbon chain, and CH(OH)-CH2OH and CO-CH2OH represent the sugar alcohol and sugar forms, respectively.
SADHs are widely distributed in nature and have been found in various organisms, including bacteria, fungi, plants, and animals. These enzymes have attracted significant interest in biotechnology due to their potential applications in the production of sugar alcohols and other value-added products. Additionally, SADHs have been studied as targets for developing novel antimicrobial agents, as inhibiting these enzymes can disrupt the metabolism of certain pathogens that rely on sugar alcohols for growth and survival.
Ascorbic acid is the chemical name for Vitamin C. It is a water-soluble vitamin that is essential for human health. Ascorbic acid is required for the synthesis of collagen, a protein that plays a role in the structure of bones, tendons, ligaments, and blood vessels. It also functions as an antioxidant, helping to protect cells from damage caused by free radicals.
Ascorbic acid cannot be produced by the human body and must be obtained through diet or supplementation. Good food sources of vitamin C include citrus fruits, strawberries, bell peppers, broccoli, and spinach.
In the medical field, ascorbic acid is used to treat or prevent vitamin C deficiency and related conditions, such as scurvy. It may also be used in the treatment of various other health conditions, including common cold, cancer, and cardiovascular disease, although its effectiveness for these uses is still a matter of scientific debate.
Sugar acids are a type of organic acid that are derived from sugars through the process of hydrolysis or oxidation. They have complex structures and can be found in various natural sources such as fruits, vegetables, and honey. In the medical field, sugar acids may be used in the production of pharmaceuticals and other chemical products.
Some common examples of sugar acids include:
* Gluconic acid, which is derived from glucose and has applications in the food industry as a preservative and stabilizer.
* Lactic acid, which is produced by fermentation of carbohydrates and is used in the production of various pharmaceuticals, foods, and cosmetics.
* Citric acid, which is found in citrus fruits and is widely used as a flavoring agent, preservative, and chelating agent in food, beverages, and personal care products.
It's worth noting that while sugar acids have important applications in various industries, they can also contribute to tooth decay and other health problems when consumed in excess. Therefore, it's important to consume them in moderation as part of a balanced diet.
NADPH oxidase is an enzyme complex that plays a crucial role in the production of reactive oxygen species (ROS) in various cell types. The primary function of NADPH oxidase is to catalyze the transfer of electrons from NADPH to molecular oxygen, resulting in the formation of superoxide radicals. This enzyme complex consists of several subunits, including two membrane-bound components (gp91phox and p22phox) and several cytosolic components (p47phox, p67phox, p40phox, and rac1 or rac2). Upon activation, these subunits assemble to form a functional enzyme complex that generates ROS, which serve as important signaling molecules in various cellular processes. However, excessive or uncontrolled production of ROS by NADPH oxidase has been implicated in the pathogenesis of several diseases, such as cardiovascular disorders, neurodegenerative diseases, and cancer.
Microsomes, liver refers to a subcellular fraction of liver cells (hepatocytes) that are obtained during tissue homogenization and subsequent centrifugation. These microsomal fractions are rich in membranous structures known as the endoplasmic reticulum (ER), particularly the rough ER. They are involved in various important cellular processes, most notably the metabolism of xenobiotics (foreign substances) including drugs, toxins, and carcinogens.
The liver microsomes contain a variety of enzymes, such as cytochrome P450 monooxygenases, that are crucial for phase I drug metabolism. These enzymes help in the oxidation, reduction, or hydrolysis of xenobiotics, making them more water-soluble and facilitating their excretion from the body. Additionally, liver microsomes also host other enzymes involved in phase II conjugation reactions, where the metabolites from phase I are further modified by adding polar molecules like glucuronic acid, sulfate, or acetyl groups.
In summary, liver microsomes are a subcellular fraction of liver cells that play a significant role in the metabolism and detoxification of xenobiotics, contributing to the overall protection and maintenance of cellular homeostasis within the body.
L-gulonolactone oxidase
Carbohydrate dehydrogenase
Gulo (disambiguation)
Bat
Vitamin C megadosage
Vitamin C
Glucuronic acid
L-galactonolactone oxidase
Scurvy
Argument from poor design
Anne Stone (academic)
Oxidase
Tarsier
Glutaric aciduria type 1
Lipoprotein(a)
Ficus yoponensis
List of enzymes
Why Evolution is True
Platypodium elegans
List of MeSH codes (D08)
GLO
Human vestigiality
Dollo's law of irreversibility
List of EC numbers (EC 1)
Vestigiality
Conserved non-coding sequence
L-gulonolactone oxidase - Wikipedia
Top 10 Signs Of Evolution In Modern Man - Listverse
How to Determine Vitamin C Dosage
amino acid metabolic disorder - Ontology Browser - Rat Genome Database
Ascorbic Acid Competes with Sugar
Common descent - RationalWiki
MeSH Browser
A Simple UV-spectrophotometric Method for the Determination of Vitamin C Content in Various Fruits and Vegetables at Sylhet...
Vitamin C's Historical and Miraculous Record | The Health Matrix
Newly Approved Injectable Cholesterol Drug Is A Cardiologist's Dream And It Just May, Unlike Cholesterol-Lowering Statin Drugs,...
Search results - OMIA - Online Mendelian Inheritance in Animals
Ascorbic acid. Medical search
SustainPineDB
Vitamin C Deficiency Article
Vitamin C / Ascorbic Acid - Functions | Deficiency | Best Sources
Why Your Guinea Pig Needs Vitamin C But Your Dog Doesn't | Veterinarian in POOLESVILLE, MD | Poolesville Veterinary Clinic
Why Your Guinea Pig Needs Vitamin C But Your Dog Doesn't | Veterinarian in Allen, TX | Allen Veterinary Hospital
How to Reduce Stress and How it Affects Our Health - Nutrition In Focus
February | 2018 | Mirna Mimics
MediGuard Vitamin C - Royal Horse Boutique
Re-Writing The Human Genome And Implanting It Into A Living Cell Proposed. Prospect Of A Human With Laboratory-Determined...
Why Your Guinea Pig Needs Vitamin C But Your Dog Doesn't | Veterinarian in Murrieta, CA | Murrieta Family Pet Hospital
Westside Animal Clinic - Veterinarian in Edmonton, Alberta Canada
Why Your Guinea Pig Needs Vitamin C But Your Dog Doesn't | Veterinarian in Alpharetta, GA | Veterinary Medical Center
vitaminC Archives - Right To Heal
Vitamin C - UPC Food Search
The relationship between glucose and vitamin C plays a huge role in health (via NaturalNews) - Templeton Wellness Foundation
Pesquisa | Portal Regional da BVS
Effect of Dietary Supplementation of Vitamin C and Seeds of Achyranthes aspera on Growth, Digestive Enzyme Activities, Immune...
Optimizing production of Fc-amidated peptides by Chinese hamster ovary cells | BMC Biotechnology | Full Text
Enzyme L-gulonol9
- The enzyme L-gulonolactone oxidase that accomplishes this chemical reaction does not work in these beings. (life-enthusiast.com)
- Humans lack the active form of the enzyme L -gulonolactone oxidase required for synthesizing ascorbic acid, making it essential to acquire vitamin C from dietary sources or supplements. (statpearls.com)
- Humans cannot synthesize vitamin C as we lack the enzyme L-gulonolactone oxidase. (zenithnutrition.com)
- This defect causes the inability to make the enzyme L-gulonolactone oxidase in the liver. (poolesvilleveterinaryclinic.com)
- Normally, it is produced in sufficient quantities given the presence of enzyme, L-gulonolactone oxidase. (royalhorse.ae)
- In 1957 the American J.J. Burns showed that the reason some mammals were susceptible to scurvy was the inability of their liver to produce the active enzyme L-gulonolactone oxidase, which is the last of the chain of four enzymes which synthesize vitamin C. American biochemist Irwin Stone was the first to exploit vitamin C for its food preservative properties. (upcfoodsearch.com)
- Dr Levy says that "a human's inability to make the enzyme L-gulonolactone Oxidase must be considered an inborn error of metabolism. (vitaminc.co.nz)
- The enzyme L-gulonolactone oxidase responsible for the conversion of gulonolactone to ascorbic acid is absent in primates making ascorbic acid required in the diet. (melbournefooddepot.com)
- Humans have lost the ability to make Vitamin C because of a mutation in the gene that codes for the enzyme (L-gulonolactone oxidase or GLO). (hyaluxe.com)
Gene14
- The loss of activity of the gene encoding L-gulonolactone oxidase (GULO) has occurred separately in the history of several species. (wikipedia.org)
- Humans and other primates have lost the ability to synthesize vitamin C as a result of a mutation in the gene coding for L-gulonolactone oxidase, an enzyme required for the biosynthesis of vitamin C via the glucuronic acid pathway (Woodall and Ames, 1997). (scialert.net)
- He later developed the theory that humans possess a mutated form of the L-gulonolactone oxidase coding gene. (upcfoodsearch.com)
- The gene crucial for converting L-Gulonolactone into ascorbic acid, the active form of vitamin C, is heavily mutated. (xcode.life)
- This gene contains instructions for producing an enzyme called gluconolactone oxidase or Gulon. (xcode.life)
- Drug addicts, like other humans, are born carrying a defective gene for the synthesis of the liver-enzyme protein, L-gulonolactone oxidase (GLO). (omarchives.org)
- But, humans do not make vitamin C because we have mutation in the coding of the gene guloolactone oxidase (GULO)-the gene that codes the enzyme guloolactone oxidase which converts glucose to vitamin C. As a result, humans can only obtain vitamin C through diet or supplementation. (drgoodyear.com)
- Because of a mutation in the GULO gene the gulonolactone oxidase enzyme, which is necessary and essential for vitamin C production, is absent [2] . (drgoodyear.com)
- Man, with other primates, lost the ability to synthesize vitamin C through an inactivating mutation of the gene encoding gulonolactone oxidase (GULO) millions of years ago. (drcalapai.com)
- It is a frequency enhanced elixir instructing the body to make vitamin C. Humans have not been able to make vitamin C, as most mammals do, because the gene turning on production of the gulonolactone oxidase enzyme is missing. (21stcenturyhealthshop.com)
- Consequently, the instructions in Optimal C will be able to take the place of this gene as they tell the body to turn on L-gulonolactone oxidase production. (21stcenturyhealthshop.com)
- The GULO gene produces the gulonolactone oxidase enzyme, the last of four enzymes required to convert blood sugar as it passes through the liver to ascorbate - vitamin C . (formula216.com)
- The gulonolactose oxidase gene became nonfunctional in a common primate ancestor ( 5 ). (basicmedicalkey.com)
- Many scientists believe that at one time the human body had the ability to make vitamin C, but due to a genetic mutation (in the L-gulonolactone oxidase gene), we lost this capacity over time. (iherb.com)
Ascorbic2
- The L-xylo-hex-3-gulonolactone then converts to ascorbic acid spontaneously, without enzymatic action. (wikipedia.org)
- Snow trout being a teleost, lacks the enzyme L-gulono-lactone oxidase which is responsible for the endogenous synthesis of ascorbic acid (AA) from L-gulonolacetone in liver and kidney [8] . (madridge.org)
Vitamin8
- L-Gulonolactone oxidase (EC 1.1.3.8) is an enzyme that produces vitamin C, but is non-functional in Haplorrhini (including humans), in some bats, and in guinea pigs. (wikipedia.org)
- Humans have structures in their genetic make-up that were once used to produces enzymes to process vitamin C (it is called L-gulonolactone oxidase). (listverse.com)
- A famous example of this is the L-gulonolactone oxidase that synthesizes vitamin C . All simians, including humans , share one pseudogene of inactivated L-gulonolactone oxidase, but the guinea pig has a different pseudogene indicating a different mutation. (rationalwiki.org)
- Humans lack the L-gulonolactone oxidase enzyme that is critical for the last step of vitamin C synthesis. (templetonwellness.com)
- While glucose is in abundant supply in humans and animals, there are four enzymes that are required to convert glucose into Vitamin C. Humans, have only three of these enzymes having lost the ability to make the fourth L-gulonolactone Oxidase somewhere in evolution. (vitaminc.co.nz)
- Horses (unlike humans) have the ability to manufacture vitamin C from glucose, because they produce an enzyme in their liver called L-gulonolactone oxidase. (horsenation.com)
- Most other animals endogenously produce vitamin C. Guinea pigs, fruit bats, primate monkeys, a Japanese killfish suffer the same plight as human - they are missing an enzyme (gulonolactone oxidase) that converts blood sugar (glucose from the liver, sucrose and fructose from the diet) to ascorbate as blood passes through the liver. (formula216.com)
- Vitamin C is not synthesized by humans and nonhuman primates because of their lack of gulonolactone oxidase, the terminal enzyme in the biosynthetic pathway of vitamin C from glucose. (basicmedicalkey.com)
Humans2
- L-Gulonolactone oxidase deficiency has been called "hypoascorbemia" and is described by OMIM (Online Mendelian Inheritance in Man) as "a public inborn error of metabolism", as it affects all humans. (wikipedia.org)
- It is even more interesting to contemplate the impact on mankind if it were possible to re-install the L-gulonolactone Oxidase enzyme in humans? (vitaminc.co.nz)
Pseudogene1
- The non-functional gulonolactone oxidase pseudogene (GULOP) was mapped to human chromosome 8p21, which corresponds to an evolutionarily conserved segment on either porcine chromosome 4 (SSC4) or 14 (SSC14). (wikipedia.org)
Make1
- What we all have in common if that we cannot make L-gulonolactone oxidase (GLO), the enzyme. (righttoheal.com)
Form1
- It catalyzes the reaction of L-gulono-1,4-lactone with oxygen to form L-xylo-hex-3-gulonolactone (2-keto-gulono-γ-lactone) and hydrogen peroxide. (wikipedia.org)
Role2
- Crane JK, Naeher TM, Broome JE, Boedeker EC: Role of host xanthine oxidase in infection Due to enteropathogenic and shiga-toxigenic escherichia coli. (mek-inhibitors.com)
- Peinado H, Del Carmen Iglesias-de la Cruz M, Olmeda D, Csiszar K, Fong KS, Vega S, Nieto MA, Cano A, Portillo F: A molecular role for lysyl oxidase-like 2 enzyme in snail regulation and tumor progression. (bcl-2inhibitors.com)
GULO4
- The loss of activity of the gene encoding L-gulonolactone oxidase (GULO) has occurred separately in the history of several species. (wikipedia.org)
- 19. Restoration of vitamin C synthesis in transgenic Gulo-/- mice by helper-dependent adenovirus-based expression of gulonolactone oxidase. (nih.gov)
- Loss of the vitamin C pathway due to deletions in the GULO (L-gulonolactone oxidase) gene has been detected in humans, apes, guinea pigs, bats, mice, rats, pigs, and passerine birds. (blogspot.com)
- The GULO gene encodes the enzyme L-glucono-γ-lactone oxidase, the terminal enzyme in the synthesis of ascorbic acid. (blogspot.com)
Enzyme L-Gulonol3
- Humans are deficient in enzyme L-Gulonolactone oxidase which is required for Vitamin-C synthesis. (saranskinclinic.com)
- This defect causes the inability to make the enzyme L-gulonolactone oxidase in the liver. (mcclellandsah.com)
- Normally, it is produced in sufficient quantities given the presence of enzyme, L-gulonolactone oxidase, in the liver. (plusvital.com)
Oxygen1
- It catalyzes the reaction of L-gulono-1,4-lactone with oxygen to form L-xylo-hex-3-gulonolactone (2-keto-gulono-γ-lactone) and hydrogen peroxide. (wikipedia.org)
Activity1
- Four male fish having the transgene in their germs cells came to maturity, and progeny derived from one of the fish possessed L-gulono-y-lactone oxidase activity. (formula216.com)