Pyridoxal Kinase
Pyridoxal
Pyridoxal Phosphate
Pyridoxamine
Pyridoxaminephosphate Oxidase
Pyridoxine
Phosphotransferases
Vitamin B 6
Sheep
Binding Sites
Vitamin B 6 Deficiency
Neurotransmitter Agents
Update on interconversions of vitamin B-6 with its coenzyme. (1/67)
Biosynthesis of pyridoxal 5'-phosphate (PLP) depends upon the relatively specific action of two consecutive enzymes, viz. pyridoxal (pyridoxine, pyridoxamine) kinase and pyridoxine (pyridoxamine) phosphate oxidase. Less specific phosphatases catalyze hydrolyses of the 5'-phosphates of the vitamers pyridoxal, pyridoxamine, and pyridoxine. From the recognition a generation ago of these processes by which the three forms of vitamin B-6 and their 5'-phosphates are interconverted, more recent studies have provided a fairly sophisticated understanding of the molecular characteristics of the enzymes involved. The evolutionary retention of homologous portions of pyridoxal kinase in humans as well as bacteria and the most recent finding of a highly conserved region of the pyridoxine (pyridoxamine) phosphate oxidase, also from both prokaryotic and eukaryotic organisms, emphasize the importance of these catalysts in the formation of a coenzyme that is essential for most organisms. Both kinase and oxidase involved in B-6 metabolism are potential targets for pharmacologic agents. (+info)Adrenocorticotropic hormone increases hydrolysis of B-6 vitamers in swine adrenal glands. (2/67)
Shipping stress is an economic problem because of its effect on meat quality. Because shipping increases plasma cortisol and pyridoxal 5'-phosphate interacts with steroid hormones, we examined the interaction between adrenocorticotropic hormone (ACTH) and vitamin B-6 metabolism in pigs. Six crossbred pigs with ear vein catheters received 50 IU of porcine ACTH intravenously at 3-h intervals from 0800 to 2100 h on d 1-3 and 100 IU intramuscularly at 0800, 1400 and 2000 h on d 6 and 7. Controls received saline. ACTH had no effect on pyridoxal 5'-phosphate in adrenal tissue but decreased pyridoxamine 5'-phosphate from 6.1 +/- 0.7 to 4.7 +/- 1.0 nmol/g (P < 0.05). Adrenal pyridoxal and pyridoxamine concentrations were 0.4 +/- 0.1 nmol/g in controls and 1.1 +/- 0.3 and 1.3 +/- 0.5 nmol/g, respectively, in ACTH-treated pigs (P < 0.01). Pyridoxal 5'-phosphate phosphatase activity [median (25-75 percentile value)] at pH 7.4 in adrenal tissue was 66.6 (47.8-75.5) nmol/(g. min) in the controls and 764 (626-771) in the ACTH-treated pigs (P < 0.01). There was no significant difference in pyridoxal kinase activity. However, kinase activity in the adrenals was about twice as high as in other tissues. These data suggest an active turnover of vitamin B-6 in adrenal tissue. (+info)Human pyridoxal kinase: overexpression and properties of the recombinant enzyme. (3/67)
Pyridoxal kinase catalyses the phosphorylation of the vitamin B6. A human brain pyridoxal kinase cDNA was isolated, and the recombinant enzyme was overexpressed in E. coli as a fusion protein with maltose binding protein (MBP). Pure pyridoxal kinase exhibits a molecular mass of about 40 kDa when examined by SDS-PAGE and FPLC gel filtration. The recombinant enzyme is a monomer endowed with catalytic activity, indicating that the native quaternary structure of pyridoxal kinase is not a prerequisite for catalytic function. Zn2+ is the most effective divalent cation in the phosphorylation of pyridoxal, and the human enzyme has maximum catalytic activity in the narrow pH range of 5.5-6.0. The Km values for two substrates pyridoxal and ATP are 97 microM and 12 microM, respectively. In addition, the unfolding processes of the recombinant enzyme were monitored by circular dichroism. The values of the free energy change of unfolding (AGo = 1.2 kcal x mol(-1) x K(-1)) and the midpoint transition (1 M) suggested that the enzyme is more stable than ovine pyridoxal kinase against denaturation by guanidine hydrochloride. Intrinsic fluorescence spectra of the human enzyme from red-edge excitation and fluorescence quenching experiments showed that the tryptophanyl residues are not completely exposed and more accessible to neutral acrylamide than to the negatively charged iodide. The first complete set of catalytic and structural properties of human pyridoxal kinase provide valuable information for further biochemical studies on this enzyme. (+info)The Arabidopsis salt overly sensitive 4 mutants uncover a critical role for vitamin B6 in plant salt tolerance. (4/67)
Salt stress is a major environmental factor influencing plant growth and development. To identify salt tolerance determinants, a genetic screen for salt overly sensitive (sos) mutants was performed in Arabidopsis. We present here the characterization of sos4 mutants and the positional cloning of the SOS4 gene. sos4 mutant plants are hypersensitive to Na(+), K(+), and Li(+) ions. Under NaCl stress, sos4 plants accumulate more Na(+) and retain less K(+) compared with wild-type plants. SOS4 encodes a pyridoxal kinase that is involved in the biosynthesis of pyridoxal-5-phosphate, an active form of vitamin B6. The expression of SOS4 cDNAs complements an Escherichia coli mutant defective in pyridoxal kinase. Supplementation of pyridoxine but not pyridoxal in the growth medium can partially rescue the sos4 defect in salt tolerance. SOS4 is expressed ubiquitously in all plant tissues. As a result of alternative splicing, two transcripts are derived from the SOS4 gene, the relative abundance of which is modulated by development and environmental stresses. Besides being essential cofactors for numerous enzymes, as shown by pharmacological studies in animal cells, pyridoxal-5-phosphate and its derivatives are also ligands for P2X receptor ion channels. Our results demonstrate that pyridoxal kinase is a novel salt tolerance determinant important for the regulation of Na(+) and K(+) homeostasis in plants. We propose that pyridoxal-5-phosphate regulates Na(+) and K(+) homeostasis by modulating the activities of ion transporters. (+info)Study of substrate-enzyme interaction between immobilized pyridoxamine and recombinant porcine pyridoxal kinase using surface plasmon resonance biosensor. (5/67)
Pyridoxal kinase (PK) is an important enzyme involved in bioactivation of vitamin B(6). Binding of PK with its substrate is the prerequisite step for the subsequent catalytic phosphorylation of the substrate. In the present study, a surface plasmon resonance biosensor (BIAcore) was employed to characterize the binding interaction between wild-type porcine PK and an immobilized substrate, pyridoxamine. Pyridoxamine was modified with 11-mercaptoundecanic acid and immobilized on a sensor chip through the formation of a self-assembled monolayer. The binding of PK to the immobilized pyridoxamine was followed in real time and the kinetic parameters were derived from non-linear analysis of the sensorgram. The effects of buffer pH, monovalent cations (Na(+), K(+)) and divalent cations (Mn(2+), Zn(2+), Mg(2+)) on the binding kinetics were determined. Optimal pH for PK-pyridoxamine interaction in the absence of divalent ions is at around 7.4. While K(+) increased and Na(+) decreased the binding affinity (K(A)) of PK to immobilized pyridoxamine, all divalent cations increased the K(A) of PK for pyridoxamine. Solution phase affinity measurement based on a competitive binding assay was used to determine the affinities of PK for different vitamin B(6) analogues. The order of affinity of PK for different analogues is: pyridoxal-oxime>pyridoxine>pyridoxamine>pyridoxal>pyridoxal phosphate. This is the first study to demonstrate that buffer conditions such as pH and concentration of monovalent and/or divalent ions can directly alter the binding of PK for its substrates. The quantitative kinetic and thermodynamic parameters obtained by SPR measurement provide the insight information into the catalytic activity of this enzyme. (+info)SOS4, a pyridoxal kinase gene, is required for root hair development in Arabidopsis. (6/67)
Root hair development in plants is controlled by many genetic, hormonal, and environmental factors. A number of genes have been shown to be important for root hair formation. Arabidopsis salt overly sensitive 4 mutants were originally identified by screening for NaCl-hypersensitive growth. The SOS4 (Salt Overly Sensitive 4) gene was recently isolated by map-based cloning and shown to encode a pyridoxal (PL) kinase involved in the production of PL-5-phosphate, which is an important cofactor for various enzymes and a ligand for certain ion transporters. The root growth of sos4 mutants is slower than that of the wild type. Microscopic observations revealed that sos4 mutants do not have root hairs in the maturation zone. The sos4 mutations block the initiation of most root hairs, and impair the tip growth of those that are initiated. The root hairless phenotype of sos4 mutants was complemented by the wild-type SOS4 gene. SOS4 promoter-beta-glucuronidase analysis showed that SOS4 is expressed in the root hair and other hair-like structures. Consistent with SOS4 function as a PL kinase, in vitro application of pyridoxine and pyridoxamine, but not PL, partially rescued the root hair defect in sos4 mutants. 1-Aminocyclopropane-1-carboxylic acid and 2,4-dichlorophenoxyacetic acid treatments promoted root hair formation in both wild-type and sos4 plants, indicating that genetically SOS4 functions upstream of ethylene and auxin in root hair development. The possible role of SOS4 in ethylene and auxin biosynthesis is discussed. (+info)Crystal structure of brain pyridoxal kinase, a novel member of the ribokinase superfamily. (7/67)
The three-dimensional structures of brain pyridoxal kinase and its complex with the nucleotide ATP have been elucidated in the dimeric form at 2.1 and 2.6 A, respectively. Results have shown that pyridoxal kinase, as an enzyme obeying random sequential kinetics in catalysis, does not possess a lid shape structure common to all kinases in the ribokinase superfamily. This finding has been shown to be in line with the condition that pyridoxal kinase binds substrates with variable sizes of chemical groups at position 4 of vitamin B(6) and its derivatives. In addition, the enzyme contains a 12-residue peptide loop in the active site for the prevention of premature hydrolysis of ATP. Conserved amino acid residues Asp(118) and Tyr(127) in the peptide loop could be moved to a position covering the nucleotide after its binding so that its chance to hydrolyze in the aqueous environment of the active site was reduced. With respect to the evolutionary trend of kinase enzymes, the existence of this loop in pyridoxal kinase could be classified as an independent category in the ribokinase superfamily according to the structural feature found and mechanism followed in catalysis. (+info)Cutaneous metabolism of vitamin B-6. (8/67)
Vitamin B-6 is important for skin development and maintenance. We examined vitamin B-6 metabolism in human and mouse skin collected at different phases of the hair cycle; in hamster melanomas; in normal and immortalized human keratinocytes (HaCaT) and several human melanoma cell lines. Pyridoxamine 5'-phosphate content was higher in mouse and hamster than in human skin. Activity of both pyridoxamine 5'-phosphate oxidase and pyridoxal 5'-phosphate hydrolase was significantly increased in rapidly growing melanomas compared to either normal skin or slower growing skin tumors. Reducing the pyridoxine content of the culture medium significantly increased the activity of pyridoxal kinase and pyridoxamine 5'-phosphate oxidase. Pyridoxal 5'-phosphate hydrolase has been proposed as a regulatory enzyme for vitamin B-6, but we found B-6 vitamer content to be significantly correlated only with kinase and oxidase activity and not with pyridoxal 5'-phosphate hydrolase activity. Although pyridoxal 5'-phosphate hydrolase activity is usually attributed to tissue-nonspecific alkaline phosphatase, tissue-nonspecific alkaline phosphatase knockout mice showed preservation of normal histology of the skin and adnexal structures. Furthermore, expression of tissue-nonspecific alkaline phosphatase mRNA was not detected in either HaCaT cells or human skin, both of which exhibited significant pyridoxal 5'-phosphate hydrolase activity. This suggests that an enzyme different from the classical tissue-nonspecific alkaline phosphatase may perform cutaneous pyridoxal 5'-phosphate hydrolase activity. (+info)Pyridoxal Kinase (PK) is an enzyme that plays a crucial role in the metabolism of amino acids. The medical definition of Pyridoxal Kinase is as follows:
Pyridoxal Kinase (PK, EC 2.7.1.35) is an enzyme involved in the activation of vitamin B6 (pyridoxine, pyridoxal, or pyridoxamine) and its derivatives. Specifically, PK catalyzes the phosphorylation of pyridoxal to form pyridoxal 5'-phosphate (PLP), which is the biologically active cofactor for many enzymes involved in amino acid metabolism, neurotransmitter synthesis, and other essential physiological processes.
In humans, there are two isoforms of Pyridoxal Kinase: PKL (liver-type) and PKR (rotype). Mutations in the PKL gene can lead to a rare autosomal recessive disorder called Pyridox(am)ine 5'-phosphate oxidase deficiency (PNPO Deficiency), which is characterized by seizures, developmental delay, and other neurological symptoms. This disorder results from impaired synthesis of the active form of vitamin B6, PLP, due to defective PK enzyme activity.
Pyridoxal is a form of vitamin B6, specifically the alcohol form of pyridoxine. It is a cofactor for many enzymes involved in protein metabolism and synthesis of neurotransmitters. Pyridoxal can be converted to its active form, pyridoxal 5'-phosphate (PLP), which serves as a coenzyme in various biochemical reactions, including transamination, decarboxylation, and racemization/elimination reactions. Deficiency in vitamin B6 can lead to neurological disorders and impaired synthesis of amino acids and neurotransmitters.
Pyridoxal phosphate (PLP) is the active form of vitamin B6 and functions as a cofactor in various enzymatic reactions in the human body. It plays a crucial role in the metabolism of amino acids, carbohydrates, lipids, and neurotransmitters. Pyridoxal phosphate is involved in more than 140 different enzyme-catalyzed reactions, making it one of the most versatile cofactors in human biochemistry.
As a cofactor, pyridoxal phosphate helps enzymes carry out their functions by facilitating chemical transformations in substrates (the molecules on which enzymes act). In particular, PLP is essential for transamination, decarboxylation, racemization, and elimination reactions involving amino acids. These processes are vital for the synthesis and degradation of amino acids, neurotransmitters, hemoglobin, and other crucial molecules in the body.
Pyridoxal phosphate is formed from the conversion of pyridoxal (a form of vitamin B6) by the enzyme pyridoxal kinase, using ATP as a phosphate donor. The human body obtains vitamin B6 through dietary sources such as whole grains, legumes, vegetables, nuts, and animal products like poultry, fish, and pork. It is essential to maintain adequate levels of pyridoxal phosphate for optimal enzymatic function and overall health.
Pyridoxamine is a form of vitamin B6, which is a water-soluble vitamin that plays an essential role in the body's protein metabolism, neurotransmitter synthesis, and hemoglobin production. Pyridoxamine is a specific chemical compound that is a derivative of pyridoxine, another form of vitamin B6.
Pyridoxamine functions as a cofactor for various enzymes involved in the metabolism of amino acids, the building blocks of proteins. It helps to convert harmful homocysteine into the essential amino acid methionine, which is important for maintaining normal levels of homocysteine and supporting cardiovascular health.
Pyridoxamine has been studied for its potential role in treating or preventing certain medical conditions, such as diabetic nephropathy and neurodegenerative diseases, due to its antioxidant properties and ability to protect against protein glycation, a process that can damage tissues and contribute to aging and disease. However, more research is needed to establish its safety and efficacy for these uses.
Pyridoxamine Phosphate Oxidase (PNPO) is an enzyme that is involved in the metabolism of the vitamin B6. The protein code for this enzyme is PNPO, and its systematic name is pyridoxamine 5'-phosphate:oxygen oxidoreductase (dephosphorylating).
The primary function of Pyridoxamine Phosphate Oxidase is to convert pyridoxamine phosphate (PMP) into pyridoxal 5'-phosphate (PLP), which is an active form of vitamin B6 and a cofactor for many enzymatic reactions in the body, particularly those involved in amino acid metabolism.
Deficiency or dysfunction of Pyridoxamine Phosphate Oxidase can lead to neurological disorders and seizures, as PLP is essential for the synthesis of neurotransmitters and other vital compounds in the brain.
Pyridoxine is the chemical name for Vitamin B6. According to the medical definition, Pyridoxine is a water-soluble vitamin that is part of the B-vitamin complex and is essential for the metabolism of proteins, carbohydrates, and fats. It plays a vital role in the regulation of homocysteine levels in the body, the formation of neurotransmitters such as serotonin and dopamine, and the synthesis of hemoglobin.
Pyridoxine can be found naturally in various foods, including whole grains, legumes, vegetables, nuts, seeds, meat, poultry, and fish. It is also available as a dietary supplement and may be prescribed by healthcare providers to treat or prevent certain medical conditions, such as vitamin B6 deficiency, anemia, seizures, and carpal tunnel syndrome.
Like other water-soluble vitamins, Pyridoxine cannot be stored in the body and must be replenished regularly through diet or supplementation. Excessive intake of Pyridoxine can lead to toxicity symptoms such as nerve damage, skin lesions, and light sensitivity.
Phosphotransferases are a group of enzymes that catalyze the transfer of a phosphate group from a donor molecule to an acceptor molecule. This reaction is essential for various cellular processes, including energy metabolism, signal transduction, and biosynthesis.
The systematic name for this group of enzymes is phosphotransferase, which is derived from the general reaction they catalyze: D-donor + A-acceptor = D-donor minus phosphate + A-phosphate. The donor molecule can be a variety of compounds, such as ATP or a phosphorylated protein, while the acceptor molecule is typically a compound that becomes phosphorylated during the reaction.
Phosphotransferases are classified into several subgroups based on the type of donor and acceptor molecules they act upon. For example, kinases are a subgroup of phosphotransferases that transfer a phosphate group from ATP to a protein or other organic compound. Phosphatases, another subgroup, remove phosphate groups from molecules by transferring them to water.
Overall, phosphotransferases play a critical role in regulating many cellular functions and are important targets for drug development in various diseases, including cancer and neurological disorders.
Medical Definition of Vitamin B6:
Vitamin B6, also known as pyridoxine, is a water-soluble vitamin that plays a crucial role in various bodily functions. It is involved in the process of making serotonin and norepinephrine, which are chemicals that transmit signals in the brain. Vitamin B6 is also necessary for the formation of myelin, a protein layer that forms around nerve cells. Additionally, it helps the body to metabolize proteins, carbohydrates, and fats, and is involved in the creation of red blood cells.
Vitamin B6 can be found in a wide variety of foods, including poultry, seafood, bananas, potatoes, and fortified cereals. A deficiency in vitamin B6 can lead to anemia, confusion, and a weakened immune system. On the other hand, excessive intake of vitamin B6 can cause nerve damage and skin lesions. It is important to maintain appropriate levels of vitamin B6 through a balanced diet and, if necessary, supplementation under the guidance of a healthcare provider.
I apologize, but "sheep" is not a term that has a medical definition. It is a common animal with the scientific name Ovis aries. If you have any medical or health-related questions, I would be happy to try and help answer those for you.
In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."
1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.
2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.
3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.
4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).
Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.
In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.
The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.
In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.
Vitamin B6 deficiency refers to the condition in which there is an insufficient amount of vitamin B6 (pyridoxine) in the body. Vitamin B6 is an essential nutrient that plays a crucial role in various bodily functions, including protein metabolism, neurotransmitter synthesis, hemoglobin production, and immune function.
A deficiency in vitamin B6 can lead to several health issues, such as:
1. Anemia: Vitamin B6 is essential for the production of hemoglobin, a protein in red blood cells that carries oxygen throughout the body. A deficiency in this nutrient can lead to anemia, characterized by fatigue, weakness, and shortness of breath.
2. Peripheral neuropathy: Vitamin B6 deficiency can cause nerve damage, leading to symptoms such as numbness, tingling, and pain in the hands and feet.
3. Depression and cognitive impairment: Pyridoxine is necessary for the synthesis of neurotransmitters like serotonin and dopamine, which are involved in mood regulation. A deficiency in vitamin B6 can lead to depression, irritability, and cognitive decline.
4. Seizures: In severe cases, vitamin B6 deficiency can cause seizures due to the impaired synthesis of gamma-aminobutyric acid (GABA), an inhibitory neurotransmitter that helps regulate brain activity.
5. Skin changes: A deficiency in this nutrient can also lead to skin changes, such as dryness, scaling, and cracks around the mouth.
Vitamin B6 deficiency is relatively uncommon in developed countries but can occur in individuals with certain medical conditions, such as malabsorption syndromes, alcoholism, kidney disease, or those taking medications that interfere with vitamin B6 metabolism. Additionally, older adults, pregnant women, and breastfeeding mothers may have an increased need for this nutrient, making them more susceptible to deficiency.
Neurotransmitter agents are substances that affect the synthesis, storage, release, uptake, degradation, or reuptake of neurotransmitters, which are chemical messengers that transmit signals across a chemical synapse from one neuron to another. These agents can be either agonists, which mimic the action of a neurotransmitter and bind to its receptor, or antagonists, which block the action of a neurotransmitter by binding to its receptor without activating it. They are used in medicine to treat various neurological and psychiatric disorders, such as depression, anxiety, and Parkinson's disease.
Decarboxylation is a chemical reaction that removes a carboxyl group from a molecule and releases carbon dioxide (CO2) as a result. In the context of medical chemistry, decarboxylation is a crucial process in the activation of certain acidic precursor compounds into their biologically active forms.
For instance, when discussing phytocannabinoids found in cannabis plants, decarboxylation converts non-psychoactive tetrahydrocannabinolic acid (THCA) into psychoactive delta-9-tetrahydrocannabinol (Δ9-THC) through the removal of a carboxyl group. This reaction typically occurs when the plant material is exposed to heat, such as during smoking or vaporization, or when it undergoes aging.
In summary, decarboxylation refers to the chemical process that removes a carboxyl group from a molecule and releases CO2, which can activate certain acidic precursor compounds into their biologically active forms in medical chemistry.
Pyridoxal kinase
PDXK
Ginkgotoxin
Pyridoxal phosphate
GATD3A
Vitamin B6
4-Deoxypyridoxine
Megavitamin-B6 syndrome
Donald B. McCormick
Chromosome 21
List of EC numbers (EC 2)
Glycogen storage disease type V
Glutamate decarboxylase
Selenocysteine
Helicoverpa zea nudivirus 2
Walker motifs
List of MeSH codes (D08)
PYGL
SPTLC2
Ethanolamine-phosphate phospho-lyase
Myophosphorylase
5-phosphonooxy-L-lysine phospho-lyase
Aromatic L-amino acid decarboxylase
Melatonin
Glycogen phosphorylase
List of EC numbers (EC 3)
Ornithine decarboxylase
Riboflavin
Reactive aldehyde species
Choline
Pyridoxal kinase - Wikipedia
5ZW9: Crystal structure of Pyridoxal kinase (PdxK) from Salmonella typhimurium
Surface plasmon resonance measurement of pyridoxal kinase-pyridoxamine binding on self-assembled monolayer - CityU Scholars | A...
The Crystal Structure of an ADP Complex of Bacillus subtilis Pyridoxal Kinase Provides Evidence for the Parallel Emergence of...
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Vitamin B6: MedlinePlus Supplements
B. subtilis Expression Data Browser
R)-Roscovitine - BML-CC205 - Enzo Life Sciences
Pyridoxine Deficiency: Practice Essentials, Pathophysiology, Etiology
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Ligand view of caffeine (7965 - RYYVLZVUVIJVGH-UHFFFAOYSA-N) - BRENDA Enzyme Database
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ECMDB: Pyridoxine (ECMDB00239) (M2MDB000099)
PdxK3
- Pyridoxal kinase (PdxK) receptor (PDB: 6K91) was the target protein of interest in this study. (springeropen.com)
- This requires the function of a kinase encoded by pdxK and of the pyridoxal reductase Plr1. (ecmdb.ca)
- This effect requires pyridoxal kinase (PDXK), the enzyme that generates the bioactive form of vitamin B6," the investigators wrote. (cancertherapyadvisor.com)
Pyridoxine9
- Other names in common use include pyridoxal kinase (phosphorylating), pyridoxal 5-phosphate-kinase, pyridoxal phosphokinase, and pyridoxine kinase. (wikipedia.org)
- Pyridoxine, pyridoxal, and pyridoxamine are all forms of vitamin B6. (medlineplus.gov)
- After absorption, pyridoxine, pyridoxamine, and pyridoxal are transported into hepatic cells by facilitated diffusion. (medscape.com)
- Pyridoxal kinase phosphorylates pyridoxine and pyridoxamine, after which they are converted to pyridoxal 5'-phosphate (PLP) by a flavin-dependent enzyme. (medscape.com)
- Pyridoxal kinase is an ATP dependent enzyme that phosphorylates pyridoxal, pyridoxine, and pyridoxamine forming their respective 5'-phosphorylated esters. (rhea-db.org)
- One of the two E. coli kinases has very low activity for pyridoxal, pyridoxine, and pyridoxamine. (rhea-db.org)
- Pyridoxal kinase phosphorylates pyridoxine and pyridoxamine, after which they are converted to PLP, a coenzyme in tryptophan and methionine metabolism. (medscape.com)
- Changes in the transcriptional levels of pyridoxal kinase and pyridoxine-5′-phosphate oxidase post exogenous hormone treatment in the silkworm, Bombyx mori [J]. , 2015, 58(12): 1285-1290. (insect.org.cn)
- The active forms of vitamin B6 namely plasma PLP and pyridoxal (PL) as well as the three enzymes expressed in the erythrocyte involved in B6 metabolism, PL kinase, PLP phosphatase and pyridoxamine -5'- phosphate (pyridoxine -5'- phosphate) [PMP(PNP) ] oxidase were measured by high performance liquid chromatography. (up.ac.za)
Phosphate10
- In enzymology, a pyridoxal kinase (EC 2.7.1.35) is an enzyme that catalyzes the chemical reaction ATP + pyridoxal ⇌ {\displaystyle \rightleftharpoons } ADP + pyridoxal 5'-phosphate Thus, the two substrates of this enzyme are ATP and pyridoxal, whereas its two products are ADP and pyridoxal 5'-phosphate. (wikipedia.org)
- Serum pyridoxal 5'-phosphate (PLP) is used as the primary index of whole-body pyridoxal levels. (medscape.com)
- Characterization of two kinases involved in thiamine pyrophosphate and pyridoxal phosphate biosynthesis in Bacillus subtilis: 4-amino-5-hydroxymethyl-2-methylpyrimidine kinase and pyridoxal kinase. (rhea-db.org)
- Vitamin B6 is a complex of 6 vitamers: pyridoxal, pyridoxol, pyridoxamine, and their 5'-phosphate esters. (medscape.com)
- Marked increases in serum pyridoxal phosphate (PLP) levels are seen in hypophosphatasia. (medscape.com)
- When hidden zinc deficiency is present, the body cannot convert B6 to its active form, pyridoxal-5-phosphate or P5P. (mychiroclub.net)
- We are currently working on the biosynthesis of thiamin, molybdopterin, pyridoxal phosphate and menaquinone. (tamu.edu)
- Pyridoxal-5-phosphate (MC-1), blocking purinergic receptors and intracellular influx of calcium, was shown to decrease the incidence of perioperative myocardial infarction in the prospective, randomized, double-blinded MC-1 to Eliminate Necrosis and Damage in CABG (MEND-CABG) clinical trial. (minervamedica.it)
- An active form of vitamin B 6 , pyridoxal 5′-phosphate (PLP) is a cofactor of KYN aminotransferas (KAT) enzymes, which are responsible for KYNA production. (encyclopedia.pub)
- The primal aim of this thesis was to establish whether kinetic aspects of vitamin B6 metabolism predispose to earlier observed racial differences found in plasma pyridoxal-5'-phosphate (PLP). (up.ac.za)
Enzyme3
- The systematic name of this enzyme class is ATP:pyridoxal 5'-phosphotransferase. (wikipedia.org)
- Cloning and characterization of the thiD/J gene of Escherichia coli encoding a thiamin-synthesizing bifunctional enzyme, hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase. (rhea-db.org)
- These results suggest that the two distinct enzyme activities, HMP kinase and HMP-P kinase, are indeed a bifunctional enzyme encoded by a single gene, designated thiDIJ. (rhea-db.org)
Inhibitors4
- Roscovitine and other purines as kinase inhibitors. (enzolifesciences.com)
- The newly designed compounds especially 36e have shown a marked pharmacological improvement over the template molecule and are therefore recommended for further practical evaluation as superior pyridoxal kinase inhibitors. (springeropen.com)
- There are several different types of EGFRIs, including small molecule tyrosine kinase inhibitors, monoclonal antibodies, and multikinase inhibitors. (medscape.com)
- Small molecule tyrosine kinase inhibitors, such as gefitinib and erlotinib, selectively bind the adenosine triphosphate (ATP)-binding site of the EGFR tyrosine kinase receptor, inhibiting the receptor's intracellular domain via preventing phosphorylation. (medscape.com)
Escherichia2
- Expression, purification, and kinetic constants for human and Escherichia coli pyridoxal kinases. (rhea-db.org)
- Clones of two pyridoxal kinases from Escherichia coli and one from human were inserted into a pET 22b plasmid and expressed in E. coli. (rhea-db.org)
Cyclin2
- cyclin dependent kinase 5 [So. (gsea-msigdb.org)
- cyclin dependent kinase inhibitor 2. (gsea-msigdb.org)
Adenosine6
- Adenosine Kinase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (ucdenver.edu)
- This graph shows the total number of publications written about "Adenosine Kinase" by people in this website by year, and whether "Adenosine Kinase" was a major or minor topic of these publications. (ucdenver.edu)
- Below are the most recent publications written about "Adenosine Kinase" by people in Profiles. (ucdenver.edu)
- Recombinant expression, purification, and characterization of Toxoplasma gondii adenosine kinase. (ucdenver.edu)
- Insertional tagging of at least two loci associated with resistance to adenine arabinoside in Toxoplasma gondii, and cloning of the adenosine kinase locus. (ucdenver.edu)
- Assignment of the gene for adenosine kinase to chromosome 14 in Mus musculus by somatic cell hybridization. (ucdenver.edu)
Metabolic2
- We conclude that in vivo this kinase may have an alternate substrate involved in another metabolic pathway and that pyridoxal has only a poor secondary activity for this kinase. (rhea-db.org)
- Phase three of this study was conducted to illustrate the metabolic interplay ofthe enzymes PL kinase and PMP (PNP) oxidase involved in PLP production. (up.ac.za)
Enzymes1
- The kinetic parameters, Michaelis- Menten constant and maximum velocity rate, at varying substrate concentrations, for the enzymes PL kinase and PMP (PNP) oxidase, were compared in 14 white - and 14 black male test subjects recruited from the SANDF. (up.ac.za)
Serum1
- PLP is the primary active pyridoxal form, and serum PLP is used as the primary index of whole-body pyridoxal levels. (medscape.com)
Species1
- Interestingly, rbf1 -induced apoptosis leads to a debcl - and drp1 -dependent Reactive Oxygen Species production, which in turn activates the Jun Kinase pathway to trigger cell death. (sdbonline.org)
FORM1
- Melatonin absorbed by the brain is concentrated in the midbrain and hypothalamus, which enhances the activity of brain pyridoxal kinase, thereby promoting the decarboxylation of glutamic acid to form γ-aminobutyric acid, and the decarboxylation of serotonin to form Serotonin, the increased content of these two inhibitory neurotransmitters, has a regulating and sedative effect on the central nervous system. (zhishangchemical.com)
Activity1
- Inhibits M phase promoting factor (MPF) kinase activity. (enzolifesciences.com)
Search1
- Search : Cell signalling - Kinases, GPCR. (interchim.com)
Clinical1
- Serial creatine kinase-myocardial band (CK-MB) determinations, ECGs and clinical evaluations were performed. (minervamedica.it)
Group1
- These are pyridoxal derivatives in which the carbaldehyde group at position 2 of the pyridoxal moiety is replaced by a hydroxymethyl group. (ecmdb.ca)
Source2
- adenylate kinase 1 [Source:HG. (gsea-msigdb.org)
- casein kinase 1 epsilon [Source:HGN. (gsea-msigdb.org)
Pyridoxamine10
- Pyridoxal kinase (PL kinase) and pyridoxine 5'-phosphate oxidase (PNP oxidase) are the two vitamin B6 salvage enzymes involved in metabolism of the primary inactive vitamin B6 (pyridoxal, pyridoxine and pyridoxamine) into the active cofactor form, pyridoxal 5'-phosphate (PLP). (vcu.edu)
- Natural substances that have vitamin B6 activity are pyridoxine in plants and pyridoxal or pyridoxamine in animals. (nih.gov)
- The physiologically active forms of vitamin B6 are pyridoxal phosphate (codecarboxylase) and pyridoxamine phosphate. (nih.gov)
- Vitamin B6 is a complex of 6 vitamers: pyridoxal, pyridoxol, pyridoxamine, and their 5'-phosphate esters. (medscape.com)
- After absorption, pyridoxine, pyridoxamine, and pyridoxal are transported into hepatic cells by facilitated diffusion. (medscape.com)
- Pyridoxal kinase phosphorylates pyridoxine and pyridoxamine, after which they are converted to PLP, a coenzyme in tryptophan and methionine metabolism. (medscape.com)
- Pyridoxal kinase is an ATP dependent enzyme that phosphorylates pyridoxal, pyridoxine, and pyridoxamine forming their respective 5'-phosphorylated esters. (rhea-db.org)
- One of the two E. coli kinases has very low activity for pyridoxal, pyridoxine, and pyridoxamine. (rhea-db.org)
- B 6 consists of a group of six related vitamers: pyridoxal (PL), pyridoxine (PN), pyridoxamine (PM) and the 5′-phosphates (PLP- pyridoxal 5'-phosphate, PNP- pyridoxine 5'-phosphate and PMP - pyridoxamine-5'-phosphate). (vitacolumbia.com)
- PN, PL and PM forms are mainly converted to PLP via some consecutive reactions that require a kinase (whose role is to phosphorylate the 5′hydroxymethyl group) and the pyridoxamine phosphate oxidase - PNPO (whose role is to phosphorylate the PNP and the PMP). (vitacolumbia.com)
PDXK1
- 37. [Pyridoxal kinase (PDXK) promotes the proliferation of serous ovarian cancer cells and is associated with poor prognosis]. (nih.gov)
PYRUVATE KINASE1
- Pyruvate kinase [Interproscan]. (ntu.edu.sg)
Histidine kinase4
- protein_coding" "AAC73720","dpiB","Escherichia coli","sensory histidine kinase in two-component regulatory system with CitB [Ensembl]. (ntu.edu.sg)
- protein_coding" "AAC73789","kdpD","Escherichia coli","fused sensory histidine kinase in two-component regulatory system with KdpE: signal sensing protein [Ensembl]. (ntu.edu.sg)
- GAF domain, Histidine kinase-, Domain of unknown function (DUF4118), His Kinase A (phospho-acceptor) domain, Osmosensitive K+ channel His kinase sensor domain [Interproscan]. (ntu.edu.sg)
- protein_coding" "AAC74078","torS","Escherichia coli","hybrid sensory histidine kinase in two-component regulatory system with TorR [Ensembl]. (ntu.edu.sg)
Vitamin B6 metabolism1
- A third objective is to understand how vitamin B6 metabolism by PL kinase is disrupted by the neurotoxic compound, ginkgotoxin. (vcu.edu)
Diacylglycerol kinase1
- diacylglycerol kinase iota [Sou. (gsea-msigdb.org)
Protein kinase1
- 25. Increased expression of protein kinase CK2α correlates with poor patient prognosis in epithelial ovarian cancer. (nih.gov)
Vitamers2
- 3][9] The intestine absorbs only the nonphosphorylated B 6 vitamers and, in the intracellular compartment of the intestine, most of them go to the liver and are converted to phosphorylated forms (PL to PLP by PL kinase for instance). (vitacolumbia.com)
- 7] After all these reactions, the B 6 vitamers must be rephosphorylated by pyridoxal kinase in the brains cells and in other target cells too, found mostly in the mitochondria and the cytosol (where quite similar mechanisms occur). (vitacolumbia.com)
Mutations1
- Similar to PLP excess, PLP deficiency, due to mutations in PL kinase and PNP oxidase or drug-induced inhibition of their activity, has been implicated in many pathological conditions. (vcu.edu)
Substrate3
- PLP was found to inhibit PL kinase by binding to the substrate PL site in the presence of substrate MgATP to form an abortive ternary complex (PL kinase-PLP-MgATP). (vcu.edu)
- X-ray crystallographic analysis of its binding mode to PL kinase confirmed its binding to the substrate PL site of the enzyme. (vcu.edu)
- We conclude that in vivo this kinase may have an alternate substrate involved in another metabolic pathway and that pyridoxal has only a poor secondary activity for this kinase. (rhea-db.org)
Dependent1
- cyclin dependent kinase 13 [Sou. (gsea-msigdb.org)
Acid1
- Finally, vitamin B 6 is catabolized through the oxidation of pyridoxal to 4-pyridoxic acid, which is excreted in the urine. (vitacolumbia.com)
Form1
- PLP is the primary active pyridoxal form, and serum PLP is used as the primary index of whole-body pyridoxal levels. (medscape.com)
Site1
- The mutant (hPL kinase S261F) was obtained using site-directed mutagenesis. (vcu.edu)
Found1
- Ginkgotoxin was found to be a competitive inhibitor of PL kinase with a Ki of 18 μM. (vcu.edu)