An enzyme that catalyzes the oxidation of 1-pyrroline-5-carboxylate to L-GLUTAMATE in the presence of NAD. Defects in the enzyme are the cause of hyperprolinemia II.
A group of enzymes that catalyze the reduction of 1-pyrroline carboxylate to proline in the presence of NAD(P)H. Includes both the 2-oxidoreductase (EC 1.5.1.1) and the 5-oxidoreductase (EC 1.5.1.2). The former also reduces 1-piperidine-2-carboxylate to pipecolate and the latter also reduces 1-pyrroline-3-hydroxy-5-carboxylate to hydroxyproline.
The first enzyme of the proline degradative pathway. It catalyzes the oxidation of proline to pyrroline-5-carboxylic acid in the presence of oxygen and water. The action is not reversible. The specific activity of proline oxidase increases with age. EC 1.5.3.-.
Enzymes catalyzing the dehydrogenation of secondary amines, introducing a C=N double bond as the primary reaction. In some cases this is later hydrolyzed.
A non-essential amino acid that is synthesized from GLUTAMIC ACID. It is an essential component of COLLAGEN and is important for proper functioning of joints and tendons.
A metabolite in the principal biochemical pathway of lysine. It antagonizes neuroexcitatory activity modulated by the glutamate receptor, N-METHYL-D-ASPARTATE; (NMDA).
A PYRIDOXAL PHOSPHATE containing enzyme that catalyzes the transfer of amino group of L-LYSINE onto 2-oxoglutarate to generate 2-aminoadipate 6-semialdehyde and L-GLUTAMATE.
Heterocyclic compounds in which an oxygen is attached to a cyclic nitrogen.
A technique for detecting short-lived reactive FREE RADICALS in biological systems by providing a nitrone or nitrose compound for an addition reaction to occur which produces an ELECTRON SPIN RESONANCE SPECTROSCOPY-detectable aminoxyl radical. In spin trapping, the compound trapping the radical is called the spin trap and the addition product of the radical is identified as the spin adduct. (Free Rad Res Comm 1990;9(3-6):163)
Molecules which contain an atom or a group of atoms exhibiting an unpaired electron spin that can be detected by electron spin resonance spectroscopy and can be bonded to another molecule. (McGraw-Hill Dictionary of Chemical and Technical Terms, 4th ed)
Highly reactive molecules with an unsatisfied electron valence pair. Free radicals are produced in both normal and pathological processes. They are proven or suspected agents of tissue damage in a wide variety of circumstances including radiation, damage from environment chemicals, and aging. Natural and pharmacological prevention of free radical damage is being actively investigated.
Proteins found in any species of bacterium.
A technique applicable to the wide variety of substances which exhibit paramagnetism because of the magnetic moments of unpaired electrons. The spectra are useful for detection and identification, for determination of electron structure, for study of interactions between molecules, and for measurement of nuclear spins and moments. (From McGraw-Hill Encyclopedia of Science and Technology, 7th edition) Electron nuclear double resonance (ENDOR) spectroscopy is a variant of the technique which can give enhanced resolution. Electron spin resonance analysis can now be used in vivo, including imaging applications such as MAGNETIC RESONANCE IMAGING.
A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.
Inorganic oxides that contain nitrogen.
A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen.
The univalent radical OH. Hydroxyl radical is a potent oxidizing agent.

Molecular enzymology of mammalian Delta1-pyrroline-5-carboxylate synthase. Alternative splice donor utilization generates isoforms with different sensitivity to ornithine inhibition. (1/62)

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)

The sfr6 mutation in Arabidopsis suppresses low-temperature induction of genes dependent on the CRT/DRE sequence motif. (2/62)

The sfr mutations, which result in sensitivity to freezing after cold acclimation, define genes that are required for freezing tolerance. We tested plants homozygous for mutations sfr2 to sfr7 for cold-induced gene expression and found that sfr 6 plants were deficient in cold-inducible expression of the genes KIN1, COR15a, and LTI78, which all contain the C repeat/dehydration-responsive element (CRT/DRE) motif in their promoters. Similarly, sfr 6 plants failed to induce KIN1 normally in response to either osmotic stress or the application of abscisic acid. In contrast, cold-inducible expression of genes CBF1, CBF2, CBF3, and ATP5CS1, which lack the CRT/DRE motif, was not affected. The freezing-sensitive phenotype that defines sfr 6 also was found to be tightly linked to the gene expression phenotype. To determine whether the failure of cold induction of CRT/DRE-containing genes in sfr 6 was due to altered low-temperature calcium signaling, cold-induced cytosolic-free calcium ([Ca2+]cyt) elevations were investigated in the sfr 6 mutant, but these were found to be indistinguishable from those of the wild type. We discuss the possibilities that CRT/DRE binding proteins (such as CBF1) require activation to play a role in transcription and that the SFR6 protein is a vital component of their activation.  (+info)

Proline accumulation in developing grapevine fruit occurs independently of changes in the levels of delta1-pyrroline-5-carboxylate synthetase mRNA or protein. (3/62)

Mature fruit of grapevine (Vitis vinifera) contains unusually high levels of free proline (Pro; up to 24 micromol or 2.8 mg/g fresh weight). Pro accumulation does not occur uniformly throughout berry development but only during the last 4 to 6 weeks of ripening when both berry growth and net protein accumulation have ceased. In contrast, the steady-state levels of both the mRNA encoding V. vinifera Delta1-pyrroline-5-carboxylate synthetase (VVP5CS), a key regulatory enzyme in Pro biosynthesis, and its protein product remain relatively uniform throughout fruit development. In addition, the steady-state protein levels of Pro dehydrogenase, the first enzyme in Pro degradation, increased throughout early fruit development but thereafter remained relatively constant. The developmental accumulation of free Pro late in grape berry ripening is thus clearly distinct from the osmotic stress-induced accumulation of Pro in plants. It is not associated with either sustained increases in steady-state levels of P5CS mRNA or protein or a decrease in steady-state levels of Pro dehydrogenase protein, suggesting that other physiological factors are important for its regulation.  (+info)

Metabolite repression and inducer exclusion in the proline utilization gene cluster of Aspergillus nidulans. (4/62)

The clustered prnB, prnC, and prnD genes are repressed by the simultaneous presence of glucose and ammonium. A derepressed mutation inactivating a CreA-binding site acts in cis only on the permease gene (prnB) while derepression of prnD and prnC is largely the result of reversal of inducer exclusion.  (+info)

Removal of feedback inhibition of delta(1)-pyrroline-5-carboxylate synthetase results in increased proline accumulation and protection of plants from osmotic stress. (5/62)

The Delta(1)-pyrroline-5-carboxylate synthetase (P5CS; EC not assigned) is the rate-limiting enzyme in proline (Pro) biosynthesis in plants and is subject to feedback inhibition by Pro. It has been suggested that the feedback regulation of P5CS is lost in plants under stress conditions. We compared Pro levels in transgenic tobacco (Nicotiana tabacum) plants expressing a wild-type form of Vigna aconitifolia P5CS and a mutated form of the enzyme (P5CSF129A) whose feedback inhibition by Pro was removed by site-directed mutagenesis. Transgenic plants expressing P5CSF129A accumulated about 2-fold more Pro than the plants expressing V. aconitifolia wild-type P5CS. This difference was further increased in plants treated with 200 mM NaCl. These results demonstrated that the feedback regulation of P5CS plays a role in controlling the level of Pro in plants under both normal and stress conditions. The elevated Pro also reduced free radical levels in response to osmotic stress, as measured by malondialdehyde production, and significantly improved the ability of the transgenic seedlings to grow in medium containing up to 200 mM NaCl. These findings shed new light on the regulation of Pro biosynthesis in plants and the role of Pro in reducing oxidative stress induced by osmotic stress, in addition to its accepted role as an osmolyte.  (+info)

Genetic manipulation of the metabolism of polyamines in poplar cells. The regulation of putrescine catabolism. (6/62)

We investigated the catabolism of putrescine (Put) in a non-transgenic (NT) and a transgenic cell line of poplar (Populus nigra x maximowiczii) expressing a mouse (Mus musculus) ornithine (Orn) decarboxylase (odc) cDNA. The transgenic cells produce 3- to 4-fold higher amounts of Put than the NT cells. The rate of loss of Put from the cells and the initial half-life of cellular Put were determined by feeding the cells with [U-(14)C]Orn and [1,4-(14)C]Put as precursors and following the loss of [(14)C]Put in the cells at various times after transfer to label-free medium. The amount of Put converted into spermidine as well as the loss of Put per gram fresh weight were significantly higher in the transgenic cells than the NT cells. The initial half-life of exogenously supplied [(14)C]Put was not significantly different in the two cell lines. The activity of diamine oxidase, the major enzyme involved in Put catabolism, was comparable in the two cell lines even though the Put content of the transgenic cells was severalfold higher than the NT cells. It is concluded that in poplar cells: (a) exogenously supplied Orn enters the cells and is rapidly converted into Put, (b) the rate of Put catabolism is proportional to the rate of its biosynthesis, and (c) the increased Put degradation occurs without significant changes in the activity of diamine oxidase.  (+info)

A plant gene up-regulated at rust infection sites. (7/62)

Expression of the fis1 gene from flax (Linum usitatissimum) is induced by a compatible rust (Melampsora lini) infection. Infection of transgenic plants containing a beta-glucuronidase (GUS) reporter gene under the control of the fis1 promoter showed that induction is highly localized to those leaf mesophyll cells within and immediately surrounding rust infection sites. The level of induction reflects the extent of fungal growth. In a strong resistance reaction, such as the hypersensitive fleck mediated by the L6 resistance gene, there is very little fungal growth and a microscopic level of GUS expression. Partially resistant flax leaves show levels of GUS expression that were intermediate to the level observed in the fully susceptible infection. Sequence and deletion analysis using both transient Agrobacterium tumefaciens expression and stable transformation assays have shown that the rust-inducible fis1 promoter is contained within a 580-bp fragment. Homologs of fis1 were identified in expressed sequence tag databases of a range of plant species including dicots, monocots, and a gymnosperm. Homologous genes isolated from maize (Zea mays; mis1), barley (Hordeum vulgare; bis1), wheat (Triticum aestivum; wis1), and Arabidopsis encode proteins that are highly similar (76%-82%) to the FIS1 protein. The Arabidopsis homologue has been reported to encode a delta1-pyrroline-5-carboxylate dehydrogenase that is involved in the catabolism of proline to glutamate. RNA-blot analysis showed that mis1 in maize and the bis1 homolog in barley are both up-regulated by a compatible infection with the corresponding species-specific rust. The rust-induced genes homologous to fis1 are present in many plants. The promoters of these genes have potential roles for the engineering of synthetic rust resistance genes by targeting transgene expression to the sites of rust infection.  (+info)

Molecular mechanisms of proline-mediated tolerance to toxic heavy metals in transgenic microalgae. (8/62)

Pro has been shown to play an important role in ameliorating environmental stress in plants and microorganisms, including heavy metal stress. Here, we describe the effects of the expression of a mothbean delta(1)-pyrroline-5-carboxylate synthetase (P5CS) gene in the green microalga Chlamydomonas reinhardtii. We show that transgenic algae expressing the mothbean P5CS gene have 80% higher free-Pro levels than wild-type cells, grow more rapidly in toxic Cd concentrations (100 microM), and bind fourfold more Cd than wild-type cells. In addition, Cd-K edge extended x-ray absorption fine structure studies indicated that Cd does not bind to free Pro in transgenic algae with increased Pro levels but is coordinated tetrahedrally by sulfur of phytochelatin. In contrast to P5CS-expressing cells, Cd is coordinated tetrahedrally by two oxygen and two sulfur atoms in wild-type cells. Measurements of reduced/oxidized GSH ratios and analyses of levels of malondialdehyde, a product of the free radical damage of lipids, indicate that free Pro levels are correlated with the GSH redox state and malondialdehyde levels in heavy metal-treated algae. These results suggest that the free Pro likely acts as an antioxidant in Cd-stressed cells. The resulting increased GSH levels facilitate increased phytochelatin synthesis and sequestration of Cd, because GSH-heavy metal adducts are the substrates for phytochelatin synthase.  (+info)

1-Pyrroline-5-Carboxylate Dehydrogenase (PCD) is an enzyme that catalyzes the chemical reaction involved in the metabolism of proline, an amino acid. The enzyme converts 1-pyrroline-5-carboxylate to glutamate semialdehyde, which is then further metabolized to glutamate. This reaction is important in the regulation of proline levels in cells and is also a part of the cell's stress response. A deficiency in PCD can lead to an accumulation of 1-pyrroline-5-carboxylate, which can cause neurological symptoms and other health problems.

Pyrroline-5-carboxylate reductase (PCR) is an enzyme that belongs to the family of oxidoreductases. Specifically, it is a part of the subclass of aldo-keto reductases. This enzyme catalyzes the chemical reaction that converts pyrroline-5-carboxylate to proline, which is an essential step in the biosynthesis of proline, an important proteinogenic amino acid.

The reaction catalyzed by PCR involves the reduction of a keto group to a hydroxyl group, and it requires the cofactor NADPH as a reducing agent. The systematic name for this enzyme is pyrroline-5-carboxylate:NADP+ oxidoreductase (proline-forming).

Deficiencies in PCR have been associated with several human diseases, including hyperprolinemia type II, a rare inherited disorder characterized by an accumulation of pyrroline-5-carboxylate and proline in body fluids.

Proline oxidase is an enzyme that catalyzes the chemical reaction of oxidizing proline to Δ^1^-pyrroline-5-carboxylate (P5C) and hydrogen peroxide (H2O2). The reaction is a part of the catabolic pathway for proline utilization in some organisms.

The systematic name for this enzyme is L-proline:oxygen oxidoreductase (deaminating, decarboxylating). It belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with oxygen as an acceptor. This enzyme participates in arginine and proline metabolism.

Oxidoreductases acting on CH-NH group donors are a class of enzymes within the larger group of oxidoreductases, which are responsible for catalyzing oxidation-reduction reactions. Specifically, this subclass of enzymes acts on CH-NH group donors, where the CH-NH group is a chemical functional group consisting of a carbon atom (C) bonded to a nitrogen atom (N) via a single covalent bond.

These enzymes play a crucial role in various biological processes by transferring electrons from the CH-NH group donor to an acceptor molecule, which results in the oxidation of the donor and reduction of the acceptor. This process can lead to the formation or breakdown of chemical bonds, and plays a key role in metabolic pathways such as amino acid degradation and nitrogen fixation.

Examples of enzymes that fall within this class include:

* Amino oxidases, which catalyze the oxidative deamination of amino acids to produce alpha-keto acids, ammonia, and hydrogen peroxide.
* Transaminases, which transfer an amino group from one molecule to another, often in the process of amino acid biosynthesis or degradation.
* Amine oxidoreductases, which catalyze the oxidation of primary amines to aldehydes and secondary amines to ketones, with the concomitant reduction of molecular oxygen to hydrogen peroxide.

Proline is an organic compound that is classified as a non-essential amino acid, meaning it can be produced by the human body and does not need to be obtained through the diet. It is encoded in the genetic code as the codon CCU, CCC, CCA, or CCG. Proline is a cyclic amino acid, containing an unusual secondary amine group, which forms a ring structure with its carboxyl group.

In proteins, proline acts as a structural helix breaker, disrupting the alpha-helix structure and leading to the formation of turns and bends in the protein chain. This property is important for the proper folding and function of many proteins. Proline also plays a role in the stability of collagen, a major structural protein found in connective tissues such as tendons, ligaments, and skin.

In addition to its role in protein structure, proline has been implicated in various cellular processes, including signal transduction, apoptosis, and oxidative stress response. It is also a precursor for the synthesis of other biologically important compounds such as hydroxyproline, which is found in collagen and elastin, and glutamate, an excitatory neurotransmitter in the brain.

2-Aminoadipic acid (2-AAA) is a type of amino acid that is formed as a byproduct of the metabolism of lysine, which is an essential amino acid. It is not commonly considered a building block of proteins, but it does play a role in various biochemical pathways in the body.

Abnormally high levels of 2-AAA have been found in certain medical conditions, such as genetic disorders of lysine metabolism and in some neurodegenerative diseases like multiple sclerosis and Alzheimer's disease. However, it is not currently clear whether elevated levels of 2-AAA are a cause or a consequence of these conditions.

Research is ongoing to better understand the role of 2-AAA in human health and disease.

L-Lysine 6-Transaminase, also known as L-lysine alpha-ketoglutarate transaminase or AKTA, is an enzyme that catalyzes the transfer of an amino group from L-lysine to alpha-ketoglutarate, resulting in the formation of L-glutamate and saccharopine. This enzyme plays a role in the metabolism of lysine, an essential amino acid, in various organisms including bacteria, yeast, and plants. In humans, this enzyme is not present, but other transaminases such as aspartate transaminase (AST) and alanine transaminase (ALT) are used to indirectly assess liver function.

Cyclic N-oxides are a class of organic compounds that contain a cyclic structure with a nitrogen atom bonded to an oxygen atom as an N-oxide. An N-oxide is a compound in which the nitrogen atom has a positive charge and the oxygen atom has a negative charge, forming a polar covalent bond. In cyclic N-oxides, this N-O group is part of a ring structure, which can be composed of various combinations of carbon, nitrogen, and other atoms. These compounds have been studied for their potential use in pharmaceuticals, agrochemicals, and materials science.

Spin trapping is a technique used in free radical research to detect and study short-lived, reactive free radicals. It involves the use of spin trap compounds, which react with the radicals to form more stable, longer-lived radical adducts. These adducts can then be detected and analyzed using various techniques such as electron paramagnetic resonance (EPR) spectroscopy.

The spin trap compound is typically a nitrone or nitroso compound, which reacts with the free radical to form a nitroxide radical. The nitroxide radical has a characteristic EPR spectrum that can be used to identify and quantify the original free radical. This technique allows for the direct detection and measurement of free radicals in biological systems, providing valuable insights into their role in various physiological and pathological processes.

"Spin labels" are a term used in the field of magnetic resonance, including nuclear magnetic resonance (NMR) and electron paramagnetic resonance (EPR). They refer to molecules or atoms that have been chemically attached to a system of interest and possess a stable, unpaired electron. This unpaired electron behaves like a tiny magnet and can be manipulated using magnetic fields and radiofrequency pulses in EPR experiments. The resulting changes in the electron's spin state can provide information about the local environment, dynamics, and structure of the system to which it is attached. Spin labels are often used in biochemistry and materials science to study complex biological systems or materials at the molecular level.

Free radicals are molecules or atoms that have one or more unpaired electrons in their outermost shell, making them highly reactive. They can be formed naturally in the body through processes such as metabolism and exercise, or they can come from external sources like pollution, radiation, and certain chemicals. Free radicals can cause damage to cells and contribute to the development of various diseases, including cancer, cardiovascular disease, and neurodegenerative disorders. Antioxidants are substances that can neutralize free radicals and help protect against their harmful effects.

Bacterial proteins are a type of protein that are produced by bacteria as part of their structural or functional components. These proteins can be involved in various cellular processes, such as metabolism, DNA replication, transcription, and translation. They can also play a role in bacterial pathogenesis, helping the bacteria to evade the host's immune system, acquire nutrients, and multiply within the host.

Bacterial proteins can be classified into different categories based on their function, such as:

1. Enzymes: Proteins that catalyze chemical reactions in the bacterial cell.
2. Structural proteins: Proteins that provide structural support and maintain the shape of the bacterial cell.
3. Signaling proteins: Proteins that help bacteria to communicate with each other and coordinate their behavior.
4. Transport proteins: Proteins that facilitate the movement of molecules across the bacterial cell membrane.
5. Toxins: Proteins that are produced by pathogenic bacteria to damage host cells and promote infection.
6. Surface proteins: Proteins that are located on the surface of the bacterial cell and interact with the environment or host cells.

Understanding the structure and function of bacterial proteins is important for developing new antibiotics, vaccines, and other therapeutic strategies to combat bacterial infections.

Electron Spin Resonance (ESR) Spectroscopy, also known as Electron Paramagnetic Resonance (EPR) Spectroscopy, is a technique used to investigate materials with unpaired electrons. It is based on the principle of absorption of energy by the unpaired electrons when they are exposed to an external magnetic field and microwave radiation.

In this technique, a sample is placed in a magnetic field and microwave radiation is applied. The unpaired electrons in the sample absorb energy and change their spin state when the energy of the microwaves matches the energy difference between the spin states. This absorption of energy is recorded as a function of the magnetic field strength, producing an ESR spectrum.

ESR spectroscopy can provide information about the number, type, and behavior of unpaired electrons in a sample, as well as the local environment around the electron. It is widely used in physics, chemistry, and biology to study materials such as free radicals, transition metal ions, and defects in solids.

L-Lactate Dehydrogenase (LDH) is an enzyme found in various tissues within the body, including the heart, liver, kidneys, muscles, and brain. It plays a crucial role in the process of energy production, particularly during anaerobic conditions when oxygen levels are low.

In the presence of the coenzyme NADH, LDH catalyzes the conversion of pyruvate to lactate, generating NAD+ as a byproduct. Conversely, in the presence of NAD+, LDH can convert lactate back to pyruvate using NADH. This reversible reaction is essential for maintaining the balance between lactate and pyruvate levels within cells.

Elevated blood levels of LDH may indicate tissue damage or injury, as this enzyme can be released into the circulation following cellular breakdown. As a result, LDH is often used as a nonspecific biomarker for various medical conditions, such as myocardial infarction (heart attack), liver disease, muscle damage, and certain types of cancer. However, it's important to note that an isolated increase in LDH does not necessarily pinpoint the exact location or cause of tissue damage, and further diagnostic tests are usually required for confirmation.

Nitrogen oxides (NOx) are a group of highly reactive gases, primarily composed of nitric oxide (NO) and nitrogen dioxide (NO2). They are formed during the combustion of fossil fuels, such as coal, oil, gas, or biomass, and are emitted from various sources, including power plants, industrial boilers, transportation vehicles, and residential heating systems. Exposure to NOx can have adverse health effects, particularly on the respiratory system, and contribute to the formation of harmful air pollutants like ground-level ozone and fine particulate matter.

Alcohol dehydrogenase (ADH) is a group of enzymes responsible for catalyzing the oxidation of alcohols to aldehydes or ketones, and reducing equivalents such as NAD+ to NADH. In humans, ADH plays a crucial role in the metabolism of ethanol, converting it into acetaldehyde, which is then further metabolized by aldehyde dehydrogenase (ALDH) into acetate. This process helps to detoxify and eliminate ethanol from the body. Additionally, ADH enzymes are also involved in the metabolism of other alcohols, such as methanol and ethylene glycol, which can be toxic if allowed to accumulate in the body.

A hydroxyl radical is defined in biochemistry and medicine as an extremely reactive species, characterized by the presence of an oxygen atom bonded to a hydrogen atom (OH-). It is formed when a water molecule (H2O) is split into a hydroxide ion (OH-) and a hydrogen ion (H+) in the process of oxidation.

In medical terms, hydroxyl radicals are important in understanding free radical damage and oxidative stress, which can contribute to the development of various diseases, including cancer, cardiovascular disease, and neurodegenerative disorders. They are also involved in the body's natural defense mechanisms against pathogens. However, an overproduction of hydroxyl radicals can cause damage to cellular components such as DNA, proteins, and lipids, leading to cell dysfunction and death.

III Delta1-Pyrroline-5-carboxylic acid dehydrogenase". J. Biol. Chem. 235: 3218-3223. Portal: Biology (Articles with short ... L-pyrroline-5-carboxylate-NAD+ oxidoreductase, and 1-pyrroline-5-carboxylate:NAD+ oxidoreductase. This enzyme participates in ... In enzymology, a 1-pyrroline-5-carboxylate dehydrogenase (EC 1.2.1.88) is an enzyme that catalyzes the chemical reaction (S)-1- ... pyrroline-5-carboxylate + NAD+ + 2 H2O ⇌ {\displaystyle \rightleftharpoons } L-glutamate + NADH + H+ The three substrates of ...
Protein target information for 1-pyrroline-5-carboxylate dehydrogenase (Geobacillus sp. WCH70). Find diseases associated with ...
The ALDH4A1 gene provides instructions for producing the enzyme pyrroline-5-carboxylate dehydrogenase, which is found in ... Pyrroline-5-carboxylate dehydrogenase starts the second step in the process that breaks down the protein building block (amino ... Yoshida A, Rzhetsky A, Hsu LC, Chang C. Human aldehyde dehydrogenase gene family. Eur J Biochem. 1998 Feb 1;251(3):549-57. doi ... A lack of pyrroline-5-carboxylate dehydrogenase function leads to decreased breakdown of proline and elevated levels of proline ...
6. Probable proline dehydrogenase 2. General function:. Involved in proline dehydrogenase activity. Specific function:. ... These are amino acids in which the amino group is attached to the carbon atom immediately adjacent to the carboxylate group ( ... Pyrroline-5-carboxylate is highly reactive and excess quantities have been shown to cause cell death and apoptosis (PMID: ... Under certain conditions, pyrroline-5-carboxylate can act as a neurotoxin and a metabotoxin. A neurotoxin causes damage to ...
... dehydrogenase), showed milder illness or no symptoms at all. Next, state-of-the-art 2-photon intravital microscopy (IVM) was ... Notably, mice infected with fungal cells unable to catabolize proline, e.g., cells lacking the Put2 enzyme (1-pyrroline-5- ... carboxylate (P5C) ...
... pyrroline-5-carboxylate is converted into 4-hydroxyglutamate and (R)- 1-pyrroline-5-carboxylate is converted into D-glutamate. ... S)-1-pyrroline-5-carboxylate, the product of the first enzyme of the pathway (EC 1.5.5.2) is in spontaneous equilibrium with ... All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.2.1.-. All ENZYME / UniProtKB/Swiss-Prot entries corresponding to ... The enzyme can also oxidize other 1-pyrrolines, e.g. 3-hydroxy-1- ...
3A). Glutamate degradation occurs through the reaction catalyzed by glutamate dehydrogenase (RocG) and glutamate synthetase ( ... 5. Effect of exogenous addition of glutamate and proline on a growth-dependent butanol tolerance of B. subtilis 168. Cells were ... 1. Butanol tolerance of B. subtilis 168. Cells were inoculated in LB medium and exposed to butanol at various concentrations ( ... Additional file 1. One-dimensional SDS-PAGE for protein separation of B. subtilis 168 with and without butanol treatment. ...
Pyrroline Carboxylate Reductases [D08.811.682.662.695] Pyrroline Carboxylate Reductases * Saccharopine Dehydrogenases [D08.811. ... Dehydrogenase, GGS Dehydrogenase, Glutamic-Gamma-Semialdehyde Dehydrogenase, Glutamyl-Gamma-Semialdehyde Delta(1)-Pyrroline-5- ... Carboxylate Dehydrogenase GGS Dehydrogenase Glutamic Gamma Semialdehyde Dehydrogenase Glutamic-Gamma-Semialdehyde Dehydrogenase ... Dehydrogenase, GGS. Dehydrogenase, Glutamic-Gamma-Semialdehyde. Dehydrogenase, Glutamyl-Gamma-Semialdehyde. Delta(1)-Pyrroline- ...
Pyrroline Carboxylate Reductases 9% * Metabolome 9% * Lipids 9% * Biomarkers 9% * Thiazolidines 9% ... Uridine Diphosphate Glucose Dehydrogenase 7% * In Vitro Techniques 7% * X-Rays 7% ...
citronellyl-CoA dehydrogenase activity GO:0034824 * positive regulation by symbiont of defense-related host calcium ion flux ...
malate dehydrogenase (menaquinone) activity GO:0052589 * tumor necrosis factor-activated receptor activity ...
L-threonate 3-dehydrogenase activity GO:0050036 * negative regulation of lipoprotein lipase activity ...
L-alanine dehydrogenase (RefSeq). 90, 256. BSU33540. yvaB. azoreductase (RefSeq). 90, 353. ... POSITION A C G T 1 0.9 0.0 0.1 0.0 2 0.05 0.3 0.65 0.0 3 0.0 0.15 0.85 0.0 4 0.95 0.0 0.05 0.0 5 0.05 0.0 0.95 0.0 6 0.45 0.05 ... 1. All genomic elements for the organism are represented as a circle and each element is separated by black tick marks. In this ... 1. All genomic elements for the organism are represented as a circle and each element is separated by black tick marks. In this ...
Delta-1-pyrroline-5-carboxylate dehydrogenase deficiency From NCATS Genetic and Rare Diseases Information Center ...
AZOBR_RS32620: aldehyde dehydrogenase. is similar to:. PaperBLAST. putA / GB,BAA35791.1: proline dehydrogenase/delta-1- ... pyrroline-5-carboxylate dehydrogenase; EC 1.5.1.12; EC 1.5.99.8 from Escherichia coli ... AZOBR_RS29750: aldehyde dehydrogenase. is similar to:. PaperBLAST. putA / GB,BAA35791.1: proline dehydrogenase/delta-1- ... AZOBR_RS31000: aldehyde dehydrogenase. is similar to:. PaperBLAST. putA / GB,BAA35791.1: proline dehydrogenase/delta-1- ...
aldehyde dehydrogenase 4 (glutamate gamma-semialdehyde dehydrogenase;. pyrroline-5-carboxylate dehydrogenase) * P5C ... aldehyde dehydrogenase 4 (glutamate gamma-semialdehyde dehydrogenase; pyrroline-5-carboxylate dehydrogenase). * converting ... aldehyde dehydrogenase family. CATEGORY enzyme , transport SUBCELLULAR LOCALIZATION intracellular intracellular,cytoplasm, ... 10 Kb 5 upstream gene genomic sequence study MAPPING cloned Y linked N status confirmed RNA. ...
Ortholog function: Delta-1-pyrroline-5-carboxylate dehydrogenase (EC 1.5.1.12) Oceanobacillus iheyensis HTE831 OB1349 -29. 4.2 ... Ortholog function: Acetyltransferase, GNAT family (EC 2.3.1.-) Anoxybacillus flavithermus WK1 Aflv_0223 -64. 4.6. ...
Gene: RBAM_034980: Delta-1-pyrroline-5-carboxylate dehydrogenase (EC 1.5.1.12). Gene: RBAM_003450: Delta-1-pyrroline-5- ... carboxylate dehydrogenase (EC 1.5.1.12) Bacillus pumilus SAFR-032 Gene: BPUM_0301: Delta-1-pyrroline-5-carboxylate ... Gene: GK0187: Delta-1-pyrroline-5-carboxylate dehydrogenase (EC 1.5.1.12). Gene: GK2889: Delta-1-pyrroline-5-carboxylate ... Gene: Aflv_0249: Delta-1-pyrroline-5-carboxylate dehydrogenase (EC 1.5.1.12) ...
6-phosphogluconate dehydrogenase [3] (data from MRSA252). SAOUHSC_01633. glycine dehydrogenase subunit 1 [3] (data from MRSA252 ... glyceraldehyde 3-phosphate dehydrogenase 2 [3] (data from MRSA252). SAOUHSC_01801. isocitrate dehydrogenase [3] (data from ... pyruvate dehydrogenase complex, E1 component subunit alpha [3] (data from MRSA252). SAOUHSC_01041. pyruvate dehydrogenase ... 2-oxoglutarate dehydrogenase E1 component [3] (data from MRSA252). SAOUHSC_01216. (sucC). succinyl-CoA synthetase subunit beta ...
DEHYDROGENASE, NAD+, OXIDOREDUCTASE 4fgw:B (LYS81) to (SER149) STRUCTURE OF GLYCEROL-3-PHOSPHATE DEHYDROGENASE, GPD1, FROM ... DEHYDROGENASE 1o95:C (PRO66) to (VAL145) TERNARY COMPLEX BETWEEN TRIMETHYLAMINE DEHYDROGENASE AND ELECTRON TRANSFERRING ... COLI PYRUVATE DEHYDROGENASE E1 COMPONENT E401K MUTANT WITH THIAMIN DIPHOSPHATE , PYRUVATE DEHYDROGENASE, THIAMIN DIPHOSPHATE, ... STRUCTURE OF SALMONELLA D-LACTATE DEHYDROGENASE , OXIDOREDUCTASE, D-2-HYDROXYACID DEHYDROGENASES, LDH, PYRUVATE 3oc0:B (TRP563 ...
This enzyme begins the process of degrading proline by starting the reaction that converts it to pyrroline-5-carboxylate.[ ... 2-Methylbutyryl-CoA dehydrogenase deficiency. *Beta-ketothiolase deficiency. *Maple syrup urine disease ... This enzyme helps to break down the pyrroline-5-carboxylate produced in the previous reaction, converting it to the amino acid ... A deficiency of either proline oxidase or pyrroline-5-carboxylate dehydrogenase results in a buildup of proline in the body. A ...
Keywords: Aldehyde dehydrogenase; Alcoholic liver disease; Diacylglycerol lipase; Endocannabinoids; Homocysteine INTRODUCTION. ... where glutamate is converted to pyrroline-5-carboxylate (P5C) through P5C synthase and further metabolized into proline or ... Interestingly, P5C is conversely converted to glutamate by aldehyde dehydrogenase 4 family member A1 (ALDH4A1) [27]. ... which is further metabolized by acetaldehyde dehydrogenase to acetate in the mitochondria of hepatocytes [3]. In chronic ...
Pyruvate dehydrogenase E1 component subunit β (PdhB). P99063. 1.84 ↓. 2.23 ↓. 12. Dihydrolipoyl dehydrogenase (PdhD). P99084. ... Glyceraldehyde-3-phosphate dehydrogenase 1 (GapA1). P99136. 1.62 ↓. * the arrow denotes the direction of regulation; ↑ up- and ... Glyceraldehyde-3-phosphate dehydrogenase 1 (GapA1). P99136. 1.5 ↓. 16. 3-hexulose-6-phosphate synthase (HPS). Q7A774. 1.92 ↓. ... Pyruvate dehydrogenase E1 component subunit β (PdhB). P99063. 2.19 ↓. 1.82 ↓. 2. Succinate--CoA ligase (ADP-forming) subunit α ...
Some of the immunodominant antigens include charge variants of EF-Tu, glyceraldehyde-3-phosphate dehydrogenase, ... pyruvate dehydrogenase complex, and others exist as charge variants on two-dimensional gels. These charge variants have similar ... and a dihydrolipoamide dehydrogenase. Alanine racemase and neutral protease were uniquely immunogenic to B. anthracis. ... 5. Identification of human T cell leukemia virus type 1 tax amino acid signals and cellular factors involved in secretion of ...
... malate dehydrogenase and lactate dehydrogenase. Applied Microbiology and Biotechnology 40(5): 676-681 ... Baker, P.J.; Sha, J.A.; Mcbride, M.W. 1999: Expression of 3b-hydroxysteroid dehydrogenase type I and type VI isoforms in the ... Davie, J.R.; Wynn, R.Max; Meng, M. 1995: Expression and characterization of branched-chain a-ketoacid dehydrogenase kinase from ... Seong, H.H.; Shiota, K.; Noda, K. 1992: Expression of activities of two 20a-hydroxysteroid dehydrogenase isozymes in rat ...
carboxylate. dehydrogenase,. mitochondrial. Proline. dehydrogenase. 1,. mitochondrial. Pyrroline-5-. carboxylate. reductase 2. ... Pyrroline hydroxycarboxylic. acid. NAD. NADH. ATP. AMP. PP. i. Glycine. Ornithine. Dissipation. Guanidoacetic acid. S- ... 1-Pyrroline-2-carboxylic acid. NH. 3. H. 2. O. 2. H. 2. O. O. 2. 1-Pyrroline-4-hydroxy-2-. carboxylate. NH. 3. H. 2. O. 2. NAD ... 1-Pyrroline-5-carboxylic acid. NAD. H. 2. O. NADH. L-Proline. NAD. NADH. Oxoglutaric acid. O. 2. 4-Hydroxyproline. Succinic ...
carboxylate. dehydrogenase,. mitochondrial. Alanine. aminotransferase. 1. Glutamate. dehydrogenase. 1,. mitochondrial. ... pyrroline-5-. ... 5-carboxylic. acid. ATP. NH. 3. ADP. P. i. L-Glutamine. H. 2. O ... dehydrogenase,. mitochondrial. Glutamine--tRNA. ligase. L-Glutamic acid. Carbamoyl phosphate. 5-Phosphoribosylamine. γ- ... 5-phosphate. Magnesium. FAD. Pyridoxal. 5-phosphate. Pyridoxal. 5-phosphate. tRNA(Glu). L-Glutamyl-. tRNA(Glu). tRNA(Gln). L ...
carboxylate. dehydrogenase,. mitochondrial. Proline. dehydrogenase. 1,. mitochondrial. Pyrroline-5-. carboxylate. reductase 2. ... Pyrroline hydroxycarboxylic. acid. NAD. NADH. ATP. AMP. PP. i. Glycine. Ornithine. Guanidoacetic acid. S-Adenosylmethionine. S- ... 1-Pyrroline-2-carboxylic acid. NH. 3. H. 2. O. 2. H. 2. O. O. 2. 1-Pyrroline-4-hydroxy-2-. carboxylate. NH. 3. H. 2. O. 2. NAD ... 1-Pyrroline-5-carboxylic acid. NAD. H. 2. O. NADH. L-Proline. NAD. NADH. Oxoglutaric acid. O. 2. 4-Hydroxyproline. Succinic ...
BioCyc: META:L-DELTA1-PYRROLINE_5-CARBOXYLATE Provided by MetaNetX (CC BY 4.0) ...
Pyrroline Carboxylate Reductases [D08.811.682.662.695] * Saccharopine Dehydrogenases [D08.811.682.662.750] * Tetrahydrofolate ... Methylenetetrahydrofolate Dehydrogenase (NAD+) [D08.811.682.662.217] * Methylenetetrahydrofolate Dehydrogenase (NADP) [D08.811. ... Pyridoxine-5-Phosphate Oxidase Narrower Concept UI. M0018245. Registry Number. 0. Terms. Pyridoxine-5-Phosphate Oxidase ... Pyridoxine-5-Phosphate Oxidase Pyridoxinephosphate Oxidase Registry Number. EC 1.4.3.5. CAS Type 1 Name. Pyridoxamine 5- ...

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