Ornithine Decarboxylase
Ornithine Carbamoyltransferase
Ornithine-Oxo-Acid Transaminase
Ornithine Carbamoyltransferase Deficiency Disease
Eflornithine
Putrescine
Carboxy-Lyases
Spermidine
Adenosylmethionine Decarboxylase
Biogenic Polyamines
Spermine
Gyrate Atrophy
Arginase
Carbamyl Phosphate
Transaminases
Enzyme Induction
Carbamoyl-Phosphate Synthase (Ammonia)
Hyperammonemia
Urea
Proline
Decarboxylation
Ammonia-Lyases
Ammonia
Amino Acids
Mitoguazone
Liver
Amino Acid Metabolism, Inborn Errors
Amino Acid Transport Systems, Basic
Molecular Sequence Data
Agmatine
Urea Cycle Disorders, Inborn
Amino-Acid N-Acetyltransferase
Glutamine
Cyclohexylamines
RNA, Messenger
Argininosuccinate Synthase
Spermidine Synthase
Cycloheximide
Neurospora
Argininosuccinate Lyase
Mitochondria, Liver
Gene Expression Regulation, Enzymologic
Selenomonas
Acetyltransferases
Phosphotransferases (Carboxyl Group Acceptor)
Carboxyl and Carbamoyl Transferases
Amino Acid Sequence
1-Pyrroline-5-Carboxylate Dehydrogenase
Hyperargininemia
Rats, Inbred Strains
Base Sequence
Pyridoxal Phosphate
Thioacetamide
DNA
Protein Biosynthesis
Mutation
Tetradecanoylphorbol Acetate
Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)
Papilloma
Glutamates
Escherichia coli
Neurospora crassa
Cloning, Molecular
Enzyme Repression
Spermine Synthase
Cell Division
Pyrroline Carboxylate Reductases
Kidney
Proteins
Datura stramonium
Hydrolases
Molecular enzymology of mammalian Delta1-pyrroline-5-carboxylate synthase. Alternative splice donor utilization generates isoforms with different sensitivity to ornithine inhibition. (1/1042)
Delta1-Pyrroline-5-carboxylate synthase (P5CS; EC not assigned), a mitochondrial inner membrane, ATP- and NADPH-dependent, bifunctional enzyme, catalyzes the reduction of glutamate to Delta1-pyrroline-5-carboxylate, a critical step in the de novo biosynthesis of proline and ornithine. We utilized published plant P5CS sequence to search the expressed sequence tag data base and cloned two full-length human P5CS cDNAs differing in length by 6 base pairs (bp) in the open reading frame. The short cDNA has a 2379-bp open reading frame encoding a protein of 793 residues; the long cDNA, generated by "exon sliding," a form of alternative splicing, contains an additional 6-bp insert following bp +711 of the short form resulting in inclusion of two additional amino acids in the region predicted to be the gamma-glutamyl kinase active site of P5CS. The long form predominates in all tissues examined except gut. We also isolated the corresponding long and short murine P5CS transcripts. To confirm the identity of the putative P5CS cDNAs, we expressed both human forms in gamma-glutamyl kinase- and gamma-glutamyl phosphate reductase-deficient strains of Saccharomyces cerevisiae and showed that they conferred the proline prototrophy. Additionally, we found expression of the murine putative P5CS cDNAs conferred proline prototrophy to P5CS-deficient Chinese hamster ovary cells (CHO-K1). We utilized stable CHO-K1 cell transformants to compare the biochemical characteristics of the long and short murine P5CS isoforms. We found that both confer P5CS activity and that the short isoform is inhibited by L-ornithine with a Ki of approximately 0.25 mM. Surprisingly, the long isoform is insensitive to ornithine inhibition. Thus, the two amino acid insert in the long isoform abolishes feedback inhibition of P5CS activity by L-ornithine. (+info)Car: a cytoplasmic sensor responsible for arginine chemotaxis in the archaeon Halobacterium salinarum. (2/1042)
A new metabolic signaling pathway for arginine, both a chemoeffector and a fermentative energy source, is described for Halobacterium salinarum. Systematic screening of 80+ potentially chemotactic compounds with two behavioral assays identified leucine, isoleucine, valine, methionine, cysteine, arginine and several peptides as strong chemoattractants. Deletion analysis of a number of potential halobacterial transducer genes led to the identification of Car, a specific cytoplasmic arginine transducer which lacks transmembrane helices and was biochemically shown to be localized in the cytoplasm. Flow assays were used to show specific adaptive responses to arginine and ornithine in wild-type but not Deltacar cells, demonstrating the role of Car in sensing arginine. The signaling pathway from external arginine to the flagellar motor of the cell involves an arginine:ornithine antiporter which was quantitatively characterized for its transport kinetics and inhibitors. By compiling the chemotactic behavior, the adaptive responses and the characteristics of the arginine:ornithine antiporter to arginine and its analogs, we now understand how the combination of arginine uptake and its metabolic conversion is required to build an effective sensing system. In both bacteria and the archaea this is the first chemoeffector molecule of a soluble methylatable transducer to be identified. (+info)Effect of ornithine and lactate on urea synthesis in isolated hepatocytes. (3/1042)
1. In hepatocytes isolated from 24 h-starved rats, urea production from ammonia was stimulated by addition of lactate, in both the presence and the absence of ornithine. The relationship of lactate concentration to the rate of urea synthesis was hyperbolic. 2. Other glucose precursors also stimulated urea production to varying degrees, but none more than lactate. Added oleate and butyrate did not stimulate urea synthesis. 3. Citrulline accumulation was largely dependent on ornithine concentration. As ornithine was increased from 0 to 40 mM, the rate of citrulline accumulation increased hyperbolically, and was half-maximal when ornithine was 8-12 mM. 4. The rate of citrulline accumulation was independent of the presence of lactate, but with pyruvate the rate increased. 5. The rate of urea production continued to increase as ornithine was varied from 0 to 40 mM. 6. It was concluded that intermediates provided by both ornithine and lactate are limiting for urea production from ammonia in isolated liver cells. It was suggested that the stimulatory effect of lactate lies in increased availability of cytosolic aspartate for condensation with citrulline. (+info)Arginine biosynthesis in Neisseria gonorrhoeae: enzymes catalyzing the formation of ornithine and citrulline. (4/1042)
Many of the Neisseria gonorrhoeae strains isolated from patients require arginine for growth in a defined medium. As a basis for genetic studies of these Arg- strains, we examined two biosynthetic enzymes of Arg+ (nonrequiring) gonococci. Cell-free extracts contained (i) glutamate acetyltransferase, which catalyzes the formation of L-ornithine from alpha-N-acetyl-L-ornithine, and (ii) ornithine transcaramylase, which catalyzes the reaction between L-ornithine and carbamyl phosphate, yielding L-citrulline. Arg- strains were unable to utilze alpha-N-acetyl-L-ornithine for growth lacked significant activity of glutamate acetyltransferase, and activity was gained by Arg+ clones derived by DNA-mediated transformation. Some of the Arg- patient isolates were unable to use either alpha-N-acetyl-L-ornithine or L-ornithine in place of arginine, and two separate steps of genetic transformation were required to yield Arg+ cells. Extracts of these doubly auxotrophic cells lacked glutamate acetyltransferase activity, but, unexpectedly, they displayed normal ornithine transcarbamylase activity. This finding illustrates the importance of identifying the products specified by arg loci during genetic studies of arginine auxotrophy. (+info)Proline biosynthesis from L-ornithine in Clostridium sticklandii: purification of delta1-pyrroline-5-carboxylate reductase, and sequence and expression of the encoding gene, proC. (5/1042)
Clostridium sticklandii utilizes combinations of amino acids for growth by Stickland reactions. Proline is an efficient electron acceptor in these reactions and is reduced to 5-aminovalerate. Proline can be partly synthesized from ornithine by the action of ornithine aminotransferase and delta1-pyrroline-5-carboxylate (PCA) reductase. Both enzymes were present in crude extracts of C. sticklandii in sufficient activity of 0.93 nkat (mg protein)(-1) and 4.3 nkat (mg protein)(-1), respectively, whereas enzymes involved in proline biosynthesis from glutamate were not detected. PCA reductase was purified to homogeneity in a three-step procedure involving ammonium sulfate precipitation, affinity chromatography with Procion Red and gel filtration on Sephadex GF200. The homogeneous enzyme was most likely an octamer of 230 kDa with a subunit size of 25 kDa as obtained by SDS-PAGE and 28.9 kDa as calculated from the sequence. Apparent Km values for PCA and NADH were 0.19 mM and 0.025 mM, respectively. The enzyme also catalysed in vitro the reverse reaction, the oxidation of proline, at alkaline pH values above 8 and higher substrate concentrations (apparent Km values: 1.55 mM for proline and 10.5 mM for NAD at pH 10.0). Studies with growing cells of C. sticklandii and [15N]proline revealed that proline is not oxidized in vivo because 15N was solely detected by HPLC-MS in 5-aminovalerate as the product of proline reduction. The proC gene encoding PCA reductase of C. sticklandii was cloned, sequenced and heterologously expressed in Escherichia coli. The enzyme exhibited high homologies to PCA reductases from different sources. Thus, C. sticklandii is able to synthesize the electron acceptor proline from ornithine (a degradation product of arginine) by action of ornithine aminotransferase and PCA reductase. (+info)Role of ornithine in the N-acetylglutamate turnover in the liver of rats. (6/1042)
We determined whether the synthesis and degradation of N-acetylglutamate would regulate urea synthesis when the ornithine status was manipulated. Experiments were done on two groups of rats, each being treated with ornithine or saline (control). The plasma concentration of urea and the liver concentration of N-acetylglutamate in rats given ornithine were each significantly higher than in the control rats. Compared with the control rats, the liver N-acetylglutamate degradation was significantly lower in those rats treated with ornithine. Treatment of the rats with ornithine did not affect N-acetylglutamate synthesis in the liver. An inverse correlation between the liver N-acetylglutamate degradation and liver concentration of N-acetylglutamate was found. These results suggest that the lower degradation of N-acetylglutamate in the ornithine treatment group would be likely to increase the hepatic concentration of this compound and stimulate urea synthesis. (+info)Expression of Escherichia coli K-12 arginine genes in Pseudomonas fluorescens. (7/1042)
Escherichia coli argE and argH gene products were detected in Pseudomonas fluorescens argH122 carrying the E. coli F110 plasmid. (+info)The carbamoyl-phosphate synthetase of Pyrococcus furiosus is enzymologically and structurally a carbamate kinase. (8/1042)
The hyperthermophiles Pyrococcus furiosus and Pyrococcus abyssi make pyrimidines and arginine from carbamoyl phosphate (CP) synthesized by an enzyme that differs from other carbamoyl-phosphate synthetases and that resembles carbamate kinase (CK) in polypeptide mass, amino acid sequence, and oligomeric organization. This enzyme was reported to use ammonia, bicarbonate, and two ATP molecules as carbamoyl-phosphate synthetases to make CP and to exhibit bicarbonatedependent ATPase activity. We have reexamined these findings using the enzyme of P. furiosus expressed in Escherichia coli from the corresponding gene cloned in a plasmid. We show that the enzyme uses chemically made carbamate rather than ammonia and bicarbonate and catalyzes a reaction with the stoichiometry and equilibrium that are typical for CK. Furthermore, the enzyme catalyzes actively full reversion of the CK reaction and exhibits little bicarbonate-dependent ATPase. In addition, it cross-reacts with antibodies raised against CK from Enterococcus faecium, and its three-dimensional structure, judged by x-ray crystallography of enzyme crystals, is very similar to that of CK. Thus, the enzyme is, in all respects other than its function in vivo, a CK. Because in other organisms the function of CK is to make ATP from ADP and CP derived from arginine catabolism, this is the first example of using CK for making rather than using CP. The reasons for this use and the adaptation of the enzyme to this new function are discussed. (+info)Symptoms of OCTD typically appear during infancy and may include seizures, developmental delays, poor muscle tone, and abnormal brain activity (as detected by electroencephalogram (EEG)). Without treatment, OCTD can lead to serious health complications such as stroke, intellectual disability, and death. Treatment involves a strict diet that limits protein intake and supplementation with essential nutrients to support growth and development.
OCTD is usually diagnosed by measuring the activity of OCT enzyme in white blood cells or using genetic testing to identify mutations in the OCTD1 gene. Treatment options for OCTD are limited, but early detection and proper management can significantly improve outcomes for affected individuals.
The exact cause of gyrate atrophy is not well understood, but it is thought to be inherited in an autosomal recessive manner. The condition typically presents in childhood or adolescence and can progress rapidly, leading to significant vision loss over a short period of time.
Symptoms of gyrate atrophy may include blurred vision, peripheral vision loss, and sensitivity to light. The condition can be diagnosed through a comprehensive eye exam, including imaging tests such as optical coherence tomography (OCT) and fundus autofluorescence (FAF).
There is currently no cure for gyrate atrophy, but various treatments may be used to slow the progression of the condition and manage its symptoms. These may include vitamin supplements, anti-inflammatory medications, and protective eyewear to reduce exposure to bright light. In severe cases, surgical intervention such as retinal implantation or vision restoration therapy may be considered.
Early detection and ongoing monitoring are essential for managing gyrate atrophy and preserving vision as much as possible. With appropriate treatment and support, individuals with this condition can lead active and fulfilling lives despite significant vision loss.
Causes of Hyperammonemia:
1. Liver disease or failure: The liver is responsible for filtering out ammonia, so if it is not functioning properly, ammonia levels can rise.
2. Urea cycle disorders: These are genetic conditions that affect the body's ability to break down protein and produce urea. As a result, ammonia can build up in the bloodstream.
3. Inborn errors of metabolism: Certain inherited disorders can lead to hyperammonemia by affecting the body's ability to process ammonia.
4. Sepsis: Severe infections can cause inflammation in the body, which can lead to hyperammonemia.
5. Kidney disease or failure: If the kidneys are not functioning properly, they may be unable to remove excess ammonia from the bloodstream, leading to hyperammonemia.
Symptoms of Hyperammonemia:
1. Lethargy and confusion
2. Seizures
3. Coma
4. Vomiting
5. Diarrhea
6. Decreased appetite
7. Weight loss
8. Fatigue
9. Headache
10. Nausea and vomiting
Diagnosis of Hyperammonemia:
1. Blood tests: Measurement of ammonia levels in the blood is the most common method used to diagnose hyperammonemia.
2. Urine tests: Measurement of urea levels in the urine can help determine if the body is able to produce and excrete urea normally.
3. Imaging tests: Imaging tests such as CT or MRI scans may be ordered to look for any underlying liver or kidney damage.
4. Genetic testing: If the cause of hyperammonemia is suspected to be a genetic disorder, genetic testing may be ordered to confirm the diagnosis.
Treatment of Hyperammonemia:
1. Dietary changes: A low-protein diet and avoiding high-aminogram foods can help reduce ammonia production in the body.
2. Medications: Medications such as sodium benzoate, sodium phenylbutyrate, and ribavirin may be used to reduce ammonia production or increase urea production.
3. Dialysis: In severe cases of hyperammonemia, dialysis may be necessary to remove excess ammonia from the blood.
4. Liver transplantation: In cases where the cause of hyperammonemia is liver disease, a liver transplant may be necessary.
5. Nutritional support: Providing adequate nutrition and hydration can help support the body's metabolic processes and prevent complications of hyperammonemia.
Complications of Hyperammonemia:
1. Brain damage: Prolonged elevated ammonia levels in the blood can cause brain damage, leading to cognitive impairment, seizures, and coma.
2. Respiratory failure: Severe hyperammonemia can lead to respiratory failure, which can be life-threatening.
3. Cardiac complications: Hyperammonemia can cause cardiac complications such as arrhythmias and heart failure.
4. Kidney damage: Prolonged elevated ammonia levels in the blood can cause kidney damage and failure.
5. Infections: People with hyperammonemia may be more susceptible to infections due to impaired immune function.
In conclusion, hyperammonemia is a serious condition that can have severe consequences if left untreated. It is essential to identify the underlying cause of hyperammonemia and provide appropriate treatment to prevent complications. Early detection and management of hyperammonemia can improve outcomes and reduce the risk of long-term sequelae.
There are many different types of uveal diseases, including:
1. Uveitis: This is inflammation of the uvea, which can be caused by a variety of factors such as infection, injury, or autoimmune disorders.
2. Iridocyclitis: This is inflammation of the iris and ciliary body.
3. Choroiditis: This is inflammation of the choroid layer of the uvea.
4. Retinal vein occlusion: This is a blockage of the veins that carry blood away from the retina, which can cause vision loss.
5. Macular edema: This is swelling of the macula, the part of the retina responsible for central vision.
6. Age-related macular degeneration (AMD): This is a condition that affects the macula and can cause vision loss over time.
7. Diabetic retinopathy: This is a complication of diabetes that can cause damage to the blood vessels in the retina and lead to vision loss.
8. Retinal detachment: This is a condition where the retina becomes separated from the underlying tissue, leading to vision loss.
9. Retinal vein thrombosis: This is a blockage of the veins that carry blood away from the retina, which can cause vision loss.
10. Uveal melanoma: This is a type of cancer that affects the uvea and can be potentially life-threatening.
These are just a few examples of uveal diseases, and there are many other conditions that can affect the uvea as well. Treatment options for uveal diseases vary depending on the specific condition and its cause, but may include medications, laser surgery, or other procedures to treat inflammation, reduce swelling, or remove tumors.
There are several types of inborn errors of amino acid metabolism, including:
1. Phenylketonuria (PKU): This is the most common inborn error of amino acid metabolism and is caused by a deficiency of the enzyme phenylalanine hydroxylase. This enzyme is needed to break down the amino acid phenylalanine, which is found in many protein-containing foods. If phenylalanine is not properly broken down, it can build up in the blood and brain and cause serious health problems.
2. Maple syrup urine disease (MSUD): This is a rare genetic disorder that affects the breakdown of the amino acids leucine, isoleucine, and valine. These amino acids are important for growth and development, but if they are not properly broken down, they can build up in the blood and cause serious health problems.
3. Homocystinuria: This is a rare genetic disorder that affects the breakdown of the amino acid methionine. Methionine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
4. Arginase deficiency: This is a rare genetic disorder that affects the breakdown of the amino acid arginine. Arginine is important for the body's production of nitric oxide, a compound that helps to relax blood vessels and improve blood flow.
5. Citrullinemia: This is a rare genetic disorder that affects the breakdown of the amino acid citrulline. Citrulline is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
6. Tyrosinemia: This is a rare genetic disorder that affects the breakdown of the amino acid tyrosine. Tyrosine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
7. Maple syrup urine disease (MSUD): This is a rare genetic disorder that affects the breakdown of the amino acids leucine, isoleucine, and valine. These amino acids are important for growth and development, but if they are not properly broken down, they can build up in the blood and cause serious health problems.
8. PKU (phenylketonuria): This is a rare genetic disorder that affects the breakdown of the amino acid phenylalanine. Phenylalanine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
9. Methionine adenosyltransferase (MAT) deficiency: This is a rare genetic disorder that affects the breakdown of the amino acid methionine. Methionine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
10. Homocystinuria: This is a rare genetic disorder that affects the breakdown of the amino acid homocysteine. Homocysteine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
It is important to note that these disorders are rare and affect a small percentage of the population. However, they can be serious and potentially life-threatening, so it is important to be aware of them and seek medical attention if symptoms persist or worsen over time.
The primary symptoms of UCDs vary depending on the specific disorder but may include poor feeding, vomiting, seizures, lethargy, confusion, and difficulty breathing. Diagnosis of UCDs typically involves a combination of clinical presentation, laboratory tests such as blood ammonia levels, and genetic analysis. Treatment for UCDs includes dietary modifications, medication to reduce ammonia production in the body, and in some cases, liver transplantation.
UCDs are rare and affect approximately 1 in 8,500 people worldwide. They can affect individuals of all ages and backgrounds, although some types of UCDs are more common in specific populations or ethnic groups. Early detection and treatment of UCDs are critical to preventing long-term cognitive and physical disability and improving outcomes for affected individuals.
The symptoms of hyperargininemia typically become apparent within the first few months of life and may include:
1. Developmental delays
2. Seizures
3. Hypotonia (low muscle tone)
4. Cognitive impairment
5. Vision loss or blindness
6. Hearing loss
7. Kidney damage or failure
8. Increased risk of infections
Hyperargininemia is usually diagnosed through a combination of clinical evaluation, laboratory testing, and genetic analysis. Treatment for the disorder typically involves managing the symptoms and preventing complications. This may include:
1. Avoiding arginine-rich foods in the diet
2. Providing supplemental nutrition to support growth and development
3. Managing seizures with anticonvulsant medications
4. Physical therapy to improve muscle tone and mobility
5. Supportive care to address cognitive and vision impairments
6. Dialysis or kidney transplantation in cases of advanced kidney disease
The prognosis for individuals with hyperargininemia varies depending on the severity of the disorder and the presence of any additional medical conditions. With appropriate management, many individuals with hyperargininemia are able to lead active and fulfilling lives. However, the disorder can be life-threatening in some cases, particularly if left untreated or if complications arise.
Papillomas can occur anywhere on the body, but they are most commonly found on the face, neck, and scalp. They may appear as small bumps or growths that look like a wart. In some cases, papillomas may be associated with human papillomavirus (HPV) infection.
Papillomas are typically diagnosed through a physical examination of the affected area. In some cases, a biopsy may be performed to confirm the diagnosis and rule out other potential causes. Treatment for papillomas usually involves removal of the growth through a minor surgical procedure or cryotherapy (freezing).
Papillomas are not cancerous and do not typically pose any long-term health risks. However, they may be unsightly and can cause psychological distress for some people. In these cases, treatment may be sought for cosmetic reasons. It is important to note that papillomas should not be confused with squamous cell carcinoma, a type of skin cancer that can resemble a papilloma in appearance but has the potential to be more aggressive and harmful.
Ornithine
Ornithine cyclodeaminase
Ornithine aminotransferase
Ornithine decarboxylase
Ornithine oxoglutarate
Ornithine racemase
Ornithine translocase
Ornithine transcarbamylase
Ornithine aminotransferase deficiency
Ornithine(lysine) transaminase
Ornithine transcarbamylase deficiency
Ornithine translocase deficiency
Ornithine N-benzoyltransferase
Ornithine decarboxylase antizyme
L-ornithine N5 monooxygenase
N5-(carboxyethyl)ornithine synthase
D-ornithine 4,5-aminomutase
Pyridoxal phosphate
Orotic aciduria
List of OMIM disorder codes
Deinococcus
2,4-diaminopentanoate dehydrogenase
BH3 interacting-domain death agonist
Homocitrulline
Corbicula japonica
Shigella dysenteriae
ODC1
Acetylornithine transaminase
Glutamate N-acetyltransferase
Cyanophycin
Ornithine transcarbamylase deficiency - About the Disease - Genetic and Rare Diseases Information Center
RCSB PDB - 1OAT: ORNITHINE AMINOTRANSFERASE
Ornithine translocase deficiency: MedlinePlus Genetics
Ornithine translocase deficiency: MedlinePlus Genetics
Ornithine Decarboxylase Levels in Patients with Normal Colonic Mucosa
MedlinePlus - Search Results for: Ornithine carbamoyltransferase deficiency
Ornithine Transcarbamylase Deficiency - PubMed
NY J89568 - The tariff classification of L-Ornithine,N2[(1,1-Dimethylethoxy)Carbonyl]-N5-(Pyrazinecarbonyl)-(9-CL) (CAS 201046...
Ornithine Transcarbamylase Deficiency - GeneReviews® - NCBI Bookshelf
DailyMed - GOLD- l-carnitine, l-glutamine, l-ornithine, l-tryptophan, l-tryosine, human chorionic gonadotropin, liquid
CARNITINE OR GLUTAMINE OR HUMAN CHORIONIC GONADOTROPIN OR ORNITHINE OR - Books - NCBI
Ornithine aminotransferase deficiency - CheckOrphan
De novo synthesis is the main source of ornithine for citrulline production in neonatal pigs
YRC Public Data Repository - Gene Ontology - mitochondrial ornithine transport
Coating Coverslips with Poly-L-Ornithine or Poly-L-Lysine - Microscopy and Imaging Core | NICHD - Eunice Kennedy Shriver...
Ornithine
Conversion of Arginine to Ornithine during Malo-Lactic Fermentation in Red Swiss Wine | American Journal of Enology and...
Ornithine decarboxylase (ODC) Polymorphism and Breast and Prostate Cancer
Ornithine decarboxylase C-terminal domain superfamily models
ORNITHINE CAPSULES
Arginine Ornithine Powder
L-Ornithine Archives - Biogetica
Ornithine cyclodeaminase-based proline production by Corynebacterium glutamicum | Microbial Cell Factories | Full Text
ORNITHINE-DECARBOXYLASE INHIBITOR | SelfDecode | Genome Analysis
L-Ornithine 500mg - Quest Nutra Pharma
L-Ornithine, 500mg, Swanson, 60 capsule
L-Ornithine-L-Aspartate (Asparaginian ornityny) - LABS212
Buy L- Ornithine Medicines Online | Orion Life Science
L-Ornithine HCL | Naturally Occurring Amino Acid | MYVEGAN™
Transcarbamylase deficiency4
- When Do Symptoms of Ornithine transcarbamylase deficiency Begin? (nih.gov)
- Ornithine transcarbamylase deficiency is a genetic disease, which means that it is caused by one or more genes not working correctly. (nih.gov)
- Evaluation of neurocognitive function of prefrontal cortex in ornithine transcarbamylase deficiency. (bvsalud.org)
- Hyperammonia due to ornithine transcarbamylase deficiency (OTCD) can cause a range of deficiencies in domains of executive function and working memory . (bvsalud.org)
Deficiency19
- Ornithine transcarbamylase (OTC) deficiency is a genetic disease that causes too much ammonia to accumulate in the blood (hyperammonemia). (nih.gov)
- Ornithine translocase deficiency is an inherited disorder that causes ammonia and other substances to build up (accumulate) in the blood. (medlineplus.gov)
- Ornithine translocase deficiency varies widely in its severity and age of onset. (medlineplus.gov)
- Affected infants show signs and symptoms of ornithine translocase deficiency within days after birth. (medlineplus.gov)
- In most affected individuals, however, signs and symptoms of ornithine translocase deficiency do not appear until later in life, with health problems first appearing anytime from childhood to adulthood. (medlineplus.gov)
- Later-onset forms of ornithine translocase deficiency are usually less severe than the infantile form. (medlineplus.gov)
- Infants with ornithine translocase deficiency may lack energy (be lethargic), refuse to eat, vomit frequently, or have poorly controlled breathing or body temperature. (medlineplus.gov)
- Some people with later-onset ornithine translocase deficiency have episodes of vomiting, lethargy, problems with coordination (ataxia), vision problems, episodes of brain dysfunction (encephalopathy), developmental delay, learning disabilities, or stiffness caused by abnormal tensing of the muscles (spasticity). (medlineplus.gov)
- Individuals with ornithine translocase deficiency often cannot tolerate high-protein foods, such as meat. (medlineplus.gov)
- This rapid increase of ammonia likely leads to the signs and symptoms of ornithine translocase deficiency. (medlineplus.gov)
- While the signs and symptoms of ornithine translocase deficiency can vary greatly among affected individuals, proper treatment can prevent some complications from occurring and may improve quality of life. (medlineplus.gov)
- Ornithine translocase deficiency is a very rare disorder. (medlineplus.gov)
- Mutations in the SLC25A15 gene cause ornithine translocase deficiency. (medlineplus.gov)
- Ammonia is especially damaging to the brain, and excess ammonia causes neurological problems and other signs and symptoms of ornithine translocase deficiency. (medlineplus.gov)
- Other factors, many unknown, also contribute to the variable severity of ornithine translocase deficiency. (medlineplus.gov)
- Because ornithine translocase deficiency is caused by problems with the urea cycle, it belongs to a class of genetic diseases called urea cycle disorders. (medlineplus.gov)
- Did you mean Ornithine "carbamoyl transferase" deficiency ? (nih.gov)
- Ornithine transcarbamylase (OTC) deficiency can occur as a severe neonatal-onset disease in males (but rarely in females) and as a post-neonatal-onset (also known as "late-onset" or partial deficiency) disease in males and females. (nih.gov)
- Excessive levels of ornithine in the blood caused by a deficiency of mitochondrial ornithine aminotransferase. (checkorphan.org)
Mitochondrial ornithine4
- The SLC25A15 gene provides instructions for making a protein called mitochondrial ornithine transporter 1. (medlineplus.gov)
- Mutations in the SLC25A15 gene cause the production of a mitochondrial ornithine transporter 1 with reduced or absent function. (medlineplus.gov)
- Another version of the mitochondrial ornithine transporter protein is produced by a different gene. (medlineplus.gov)
- While this protein is not as abundant as mitochondrial ornithine transporter 1, it is thought that this other version of the protein may partially compensate for the loss of mitochondrial ornithine transporter 1 and contribute to the late age of onset and mild signs and symptoms in some affected individuals. (medlineplus.gov)
Arginine9
- During fasting, plasma proline (13%) and ornithine (19%) were the main precursors for citrulline synthesis, whereas plasma arginine (62%) was the main precursor for plasma ornithine. (nih.gov)
- Arginine, however, was the main source (47%) of plasma ornithine and in this way contributed to citrulline synthesis. (nih.gov)
- KAL L-Arginine L-Ornithine Description L-Arginine 500 mg / L-Ornithine 500 mg 1 Daily L-Arginine and L-Ornithine are closely related amino acids with similar structure and function. (priceplow.com)
- During malo-lactic fermentation in red Swiss wines by a mixture of different strains of Leuconostoc oenos stoichiometric conversion of arginine to ornithine was observed. (ajevonline.org)
- Recommendations: arginine together with ornithine favor muscle growth by increasing levels of anabolic hormones such as insulin and the growth hormone. (redis.ro)
- That's where Arginine Ornithine Powder comes in. (lotuslyfit.com)
- Alternatively, proline can be synthesised from ornithine, an intermediate of arginine biosynthesis. (biomedcentral.com)
- Some researches have shown that weight reduction can be improved with the use of a combination of the amino acids L-ornithine and L-arginine, enhanced by L-Lysine. (vitabase.com)
- D-Arginine and D-Ornithine metabolism highest concentration tested. (nih.gov)
Aminotransferase3
- In patients suffering from gyrate atrophy, a recessive hereditary genetic disorder that can cause blindness in humans, ornithine aminotransferase activity is lacking. (rcsb.org)
- A large number of frameshift and point mutations in the ornithine aminotransferase gene have been identified in such patients. (rcsb.org)
- It is contraindicated in people with genetic diseases that lack the enzyme ornithine delta aminotransferase, pregnant women and schizophrenics. (redis.ro)
Amino Acid6
- NOW L-Ornithine is an amino acid that has been used by fitness enthusiasts for years. (priceplow.com)
- L-Ornithine (500mg) Description from TwinLab Free Form Amino Acid. (priceplow.com)
- Ornithine is a nonessential amino acid produced by the body that plays a role in the formation of citrulline (vaso-dilator effect), proline (regeneration of collagen in the protein structure of the skin) and glutamic acid (provides energy for the brain, develops intelligence, treats depression and impotence). (redis.ro)
- Ornithine is a non-essential amino acid produced by the body, which plays a role in the formation of citrulline (with vasodilator effect), proline (regeneration of collagen in the protein structure of the skin) and glutamic acid (provides energy for the brain, develops intelligence, treats depression and impotence). (redis.ro)
- Provides 500mg of the amino acid L-ornithine. (qnutrapharma.com)
- L-ornithine is a naturally occurring amino acid that can't be found in many plant-based foods. (myvegan.ie)
Metabolism1
- Ornithine helps to prompt the release of growth hormone, which promotes the metabolism of body fat. (vitabase.com)
Biosynthesis1
- An alternative route to proline biosynthesis involves ornithine cyclodeaminase (OCD) which catalyses the conversion of ornithine to proline and ammonia with deamination of the α-amino group prior to cyclisation (Figure 1 ). (biomedcentral.com)
Precursor1
- In conclusion, during the neonatal period, the de novo pathway is the predominant source for the ornithine utilized in the synthesis of citrulline, and proline is the preferred precursor. (nih.gov)
Swanson1
- Swanson L-Ornithine was created. (priceplow.com)
Proline3
- Enteral proline and glutamine were utilized directly by the gut to produce ornithine utilized for citrulline synthesis. (nih.gov)
- The direct conversion of ornithine to proline is catalysed by ornithine cyclodeaminase. (biomedcentral.com)
- Plasmid-based expression of ocd encoding the putative ornithine cyclodeaminase of C. glutamicum did not result in detectable proline accumulation in the culture medium. (biomedcentral.com)
Powder1
- Our convenient-to-take powder can be added to your everyday smoothie or shake to help ensure you're getting the daily L-ornithine you need. (myvegan.ie)
Protein1
- the energy-producing centers in cells), where the protein transports a molecule called ornithine so it can participate in the urea cycle. (medlineplus.gov)
Formula1
- The Biogetica Freedom kit with VITA F, Reguline & OM 24 EN formula is a basic combination of the Ayurvedic. (biogetica.com)
Muscle2
- The L-ornithine stimulates the secretion of the growth hormone that develops muscle tissue, strengthens the immune system, accelerates healing, mobilizes body fat, increasing their combustion. (redis.ro)
- L-Ornithine helps to release growth hormone, normally lacking in adults, which burns fat and builds muscle. (vitabase.com)
Production2
- An ornithine overproducing platform strain with deletions of argR and argF (ORN1) has been employed for production of derived compounds such as putrescine. (biomedcentral.com)
- Upon further development of the ornithine overproducing platform strain, industrial production of amino acids of the glutamate family and derived bioproducts such as diamines might become within reach. (biomedcentral.com)
Result1
- As a result, ornithine transport is impaired and the urea cycle cannot proceed normally. (medlineplus.gov)
Transport1
- Byproducts of impaired ornithine transport in people with this condition include the accumulation of a substance called ornithine in the blood (hyperornithinemia) and the excretion of a substance called homocitrulline in the urine (homocitrullinuria). (medlineplus.gov)
Improve2
- Poly-ornithine or poly-lysine improve the growth and adhesion of, among other, oligodendrocytes. (nih.gov)
- There are researches also suggests that L-Ornithine has the potential to relieve stress and improve sleep quality related to fatigue. (vitabase.com)
High1
- There are high concentrations of ornithine in the skin and connective tissue. (vitabase.com)
Body1
- Ascorbic acid, alpha-tocopherol, lecithin and L-ornithine-L-aspartate exhibited an ability to counteract the alcohol-induced changes in the body weight and biochemical parameters in preventive and therapeutic models in varying degree. (who.int)
Effect2
- IMSEAR at SEARO: Effect of ascorbic acid, alpha-tocopherol, lecithin and L-ornithine-L-aspartate on ethanol induced hypoproteinemia and hyperlipidemia in rats. (who.int)
- We studied effect of exogenous ascorbic acid, alpha-tocopherol, lecithin and L-ornithine-L-aspartate on serum lipids and proteins in experimental hepatotoxic Wistar rats. (who.int)
Subscribe2
- Subscribe for more Ornithine news and alerts! (priceplow.com)
- Subscribe to PricePlow on YouTube , follow PricePlow on Instagram or click the button below to sign up for our latest Ornithine news and reviews! (priceplow.com)
Transcarbamylase36
- Ornithine transcarbamylase (OTC) deficiency is a genetic disease that causes too much ammonia to accumulate in the blood (hyperammonemia). (nih.gov)
- When Do Symptoms of Ornithine transcarbamylase deficiency Begin? (nih.gov)
- Ornithine transcarbamylase deficiency is a genetic disease, which means that it is caused by one or more genes not working correctly. (nih.gov)
- Ornithine transcarbamylase deficiency is an inherited disorder that causes ammonia to accumulate in the blood. (medlineplus.gov)
- Ornithine transcarbamylase deficiency can become evident at any age. (medlineplus.gov)
- An infant with the neonatal-onset form of ornithine transcarbamylase deficiency may be lacking in energy (lethargic) or unwilling to eat, and have a poorly-controlled breathing rate or body temperature. (medlineplus.gov)
- Complications from ornithine transcarbamylase deficiency may include developmental delay and intellectual disability. (medlineplus.gov)
- In some affected individuals, signs and symptoms of ornithine transcarbamylase deficiency may be less severe, and may not appear until later in life. (medlineplus.gov)
- People with late-onset ornithine transcarbamylase deficiency may experience episodes of altered mental status, such as delirium, erratic behavior, or a reduced level of consciousness. (medlineplus.gov)
- Estimates of the prevalence of ornithine transcarbamylase deficiency have ranged from 1 in 14,000 to 1 in 77,000 people. (medlineplus.gov)
- Mutations in the OTC gene cause ornithine transcarbamylase deficiency. (medlineplus.gov)
- The OTC gene provides instructions for making the ornithine transcarbamylase enzyme. (medlineplus.gov)
- Ornithine transcarbamylase deficiency belongs to a class of genetic diseases called urea cycle disorders. (medlineplus.gov)
- The ornithine transcarbamylase enzyme starts a specific reaction within the urea cycle. (medlineplus.gov)
- In ornithine transcarbamylase deficiency, as its name suggests, the ornithine transcarbamylase enzyme is damaged or missing. (medlineplus.gov)
- Ammonia is especially damaging to the nervous system, so ornithine transcarbamylase deficiency causes neurological problems as well as eventual damage to the liver. (medlineplus.gov)
- Ornithine transcarbamylase deficiency is an X-linked disorder. (medlineplus.gov)
- Some females with only one altered copy of the OTC gene also show signs and symptoms of ornithine transcarbamylase deficiency. (medlineplus.gov)
- However, many females with one altered copy of this gene have ornithine transcarbamylase deficiency similar to affected males because the X chromosome with the normal copy of the OTC gene is turned off through a process called X-inactivation . (medlineplus.gov)
- Late-onset ornithine transcarbamylase deficiency: a potentially fatal yet treatable cause of coma. (medscape.com)
- Preclinical evaluation of a clinical candidate AAV8 vector for ornithine transcarbamylase (OTC) deficiency reveals functional enzyme from each persisting vector genome. (medscape.com)
- Genotype-phenotype correlations in ornithine transcarbamylase deficiency: a mutation update. (medscape.com)
- Acute treatment of hyperammonemia by continuous renal replacement therapy in a newborn patient with ornithine transcarbamylase deficiency. (medscape.com)
- Gascon-Bayarri J, Campdelacreu J, Estela J, Reñé R. Severe hyperammonemia in late-onset ornithine transcarbamylase deficiency triggered by steroid administration. (medscape.com)
- Late-onset ornithine transcarbamylase deficiency: treatment and outcome of hyperammonemic crisis. (medscape.com)
- Long-term outcomes in Ornithine Transcarbamylase deficiency: a series of 90 patients. (medscape.com)
- Cerebral dysfunction in asymptomatic carriers of ornithine transcarbamylase deficiency. (medscape.com)
- Ornithine transcarbamylase deficiency: a cause of lethal neonatal hyperammonemia in males. (medscape.com)
- Late-onset ornithine transcarbamylase deficiency in male patients. (medscape.com)
- Prenatal diagnosis of ornithine transcarbamylase deficiency with use of DNA polymorphisms. (medscape.com)
- Ornithine transcarbamylase (OTC) deficiency can occur as a severe neonatal-onset disease in males (but rarely in females) and as a post-neonatal-onset (also known as "late-onset" or partial deficiency) disease in males and females. (nih.gov)
- Ornithine transcarbamylase deficiency of a male newborn with fatal outcome. (nih.gov)
- OTC gene in ornithine transcarbamylase deficiency: clinical course and mutational spectrum in seven Korean patients. (nih.gov)
- Ornithine transcarbamylase (OTC) deficiency is an X-linked genetic disorder of the urea cycle that leads to elevated levels of ammonia in the blood. (medscape.com)
- the mediating enzyme is ornithine transcarbamylase. (medscape.com)
- Ornithine transcarbamylase (OTC) deficiency is the most common urea cycle disorder. (medscape.com)
Decarboxylase activity4
- Chloroform induction of ornithine decarboxylase activity in rats. (nih.gov)
- Cooperative action of insulin and catecholamines on stimulation of ornithine decarboxylase activity in neonatal rat heart cells. (cdc.gov)
- 1. Increasing ornithine decarboxylase activity is another way of prolactin preventing methotrexate-induced apoptosis: crosstalk between ODC and BCL-2. (nih.gov)
- 15. Tumor necrosis factor stimulates ornithine decarboxylase activity in human fibroblasts and tumor target cells. (nih.gov)
Mitochondrial6
- The SLC25A15 gene provides instructions for making a protein called mitochondrial ornithine transporter 1. (nih.gov)
- Mutations in the SLC25A15 gene cause the production of a mitochondrial ornithine transporter 1 with reduced or absent function. (nih.gov)
- Another version of the mitochondrial ornithine transporter protein is produced by a different gene. (nih.gov)
- While this protein is not as abundant as mitochondrial ornithine transporter 1, it is thought that this other version of the protein may partially compensate for the loss of mitochondrial ornithine transporter 1 and contribute to the late age of onset and mild signs and symptoms in some affected individuals. (nih.gov)
- 6. Antizyme, a natural ornithine decarboxylase inhibitor, induces apoptosis of haematopoietic cells through mitochondrial membrane depolarization and caspases' cascade. (nih.gov)
- 13. Inhibition of ornithine decarboxylase alters the roscovitine-induced mitochondrial-mediated apoptosis in MCF-7 breast cancer cells. (nih.gov)
Enzyme3
- A mutant enzyme protein impairs the reaction that leads to condensation of carbamyl phosphate and ornithine to form citrulline. (medscape.com)
- Estradiol control of ornithine decarboxylase mRNA, enzyme activity, and polyamine levels in MCF-7 breast cancer cells: therapeutic implications. (nih.gov)
- Ornithine decarboxylase (ODC) is the first enzyme of the polyamine biosynthetic pathway. (nih.gov)
Urea3
- Ornithine and aspartate are important substrates in the metabolic conversion of ammonia to urea and glutamine, respectively. (medscape.com)
- the energy-producing centers in cells), where the protein transports a molecule called ornithine so it can participate in the urea cycle. (nih.gov)
- As a result, ornithine transport is impaired and the urea cycle cannot proceed normally. (nih.gov)
People1
- Byproducts of impaired ornithine transport in people with this condition include the accumulation of a substance called ornithine in the blood (hyperornithinemia) and the excretion of a substance called homocitrulline in the urine (homocitrullinuria). (nih.gov)
Patients1
- To our knowledge, there was only one report, which was titled 'L-Ornithine aspartate among cirrhotic patients with hepatic encephalopathy: does it make a difference? (medscape.com)
Cells3
- 4. Anti-IgM-induced growth inhibition and apoptosis are independent of ornithine decarboxylase in Ramos cells. (nih.gov)
- 5. Ornithine decarboxylase attenuates leukemic chemotherapy drugs-induced cell apoptosis and arrest in human promyelocytic HL-60 cells. (nih.gov)
- 8. Curcumin induces apoptosis through an ornithine decarboxylase-dependent pathway in human promyelocytic leukemia HL-60 cells. (nih.gov)