A hydroxylated derivative of the amino acid LYSINE that is present in certain collagens.
A mixed-function oxygenase that catalyzes the hydroxylation of peptidyllysine, usually in protocollagen, to peptidylhydroxylysine. The enzyme utilizes molecular oxygen with concomitant oxidative decarboxylation of the cosubstrate 2-oxoglutarate to succinate. EC 1.14.11.4.
A paralytic condition of the legs caused by ingestion of lathyrogens, especially BETA-AMINOPROPIONITRILE or beta-N-oxalyl amino-L-alanine, which are found in the seeds of plants of the genus LATHYRUS.
A polypeptide substance comprising about one third of the total protein in mammalian organisms. It is the main constituent of SKIN; CONNECTIVE TISSUE; and the organic substance of bones (BONE AND BONES) and teeth (TOOTH).
An essential amino acid. It is often added to animal feed.
A hydroxylated form of the imino acid proline. A deficiency in ASCORBIC ACID can result in impaired hydroxyproline formation.
Derivatives of adipic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a 1,6-carboxy terminated aliphatic structure.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
A 28-amino acid peptide with the same biological activities of somatostatin-14 but with a 14-amino acid extension at the N-terminal. SRIF-28 is the major form of somatostatin in the GASTROINTESTINAL TRACT.
A group of compounds that are derivatives of heptanedioic acid with the general formula R-C7H11O4.
Protein hydrolysates are defined as complex mixtures of peptides produced by the enzymatic or chemical breakdown of whole proteins, which can vary in their degree of hydrolysis and molecular weight, and are used in various medical and nutritional applications due to their improved digestibility and bioavailability compared to intact proteins.
Any compound that contains a constituent sugar, in which the hydroxyl group attached to the first carbon is substituted by an alcoholic, phenolic, or other group. They are named specifically for the sugar contained, such as glucoside (glucose), pentoside (pentose), fructoside (fructose), etc. Upon hydrolysis, a sugar and nonsugar component (aglycone) are formed. (From Dorland, 28th ed; From Miall's Dictionary of Chemistry, 5th ed)
Formed from pig pepsinogen by cleavage of one peptide bond. The enzyme is a single polypeptide chain and is inhibited by methyl 2-diaazoacetamidohexanoate. It cleaves peptides preferentially at the carbonyl linkages of phenylalanine or leucine and acts as the principal digestive enzyme of gastric juice.
Placing of a hydroxyl group on a compound in a position where one did not exist before. (Stedman, 26th ed)
Techniques used to separate mixtures of substances based on differences in the relative affinities of the substances for mobile and stationary phases. A mobile phase (fluid or gas) passes through a column containing a stationary phase of porous solid or liquid coated on a solid support. Usage is both analytical for small amounts and preparative for bulk amounts.
An enzyme oxidizing peptidyl-lysyl-peptide in the presence of water & molecular oxygen to yield peptidyl-allysyl-peptide plus ammonia & hydrogen peroxide. EC 1.4.3.13.
An unnatural amino acid that is used experimentally to study protein structure and function. It is structurally similar to METHIONINE, however it does not contain SULFUR.
Cyanogen bromide (CNBr). A compound used in molecular biology to digest some proteins and as a coupling reagent for phosphoroamidate or pyrophosphate internucleotide bonds in DNA duplexes.
A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.
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.
The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.
Fibrous bands or cords of CONNECTIVE TISSUE at the ends of SKELETAL MUSCLE FIBERS that serve to attach the MUSCLES to bones and other structures.
A non-vascular form of connective tissue composed of CHONDROCYTES embedded in a matrix that includes CHONDROITIN SULFATE and various types of FIBRILLAR COLLAGEN. There are three major types: HYALINE CARTILAGE; FIBROCARTILAGE; and ELASTIC CARTILAGE.
Picolinic acid is an organic compound that belongs to the class of pyridine derivatives, acting as a chelating agent in mammals, primarily found in the liver and kidneys, and playing a significant role in the metabolism of proteins, vitamins, and minerals.
Reagents with two reactive groups, usually at opposite ends of the molecule, that are capable of reacting with and thereby forming bridges between side chains of amino acids in proteins; the locations of naturally reactive areas within proteins can thereby be identified; may also be used for other macromolecules, like glycoproteins, nucleic acids, or other.
The largest class of organic compounds, including STARCH; GLYCOGEN; CELLULOSE; POLYSACCHARIDES; and simple MONOSACCHARIDES. Carbohydrates are composed of carbon, hydrogen, and oxygen in a ratio of Cn(H2O)n.

Recombinant human type II collagens with low and high levels of hydroxylysine and its glycosylated forms show marked differences in fibrillogenesis in vitro. (1/120)

Type II collagen is the main structural component of hyaline cartilages where it forms networks of thin fibrils that differ in morphology from the much thicker fibrils of type I collagen. We studied here in vitro the formation of fibrils of pepsin-treated recombinant human type II collagen produced in insect cells. Two kinds of type II collagen preparation were used: low hydroxylysine collagen having 2.0 hydroxylysine residues/1,000 amino acids, including 1.3 glycosylated hydroxylysines; and high hydroxylysine collagen having 19 hydroxylysines/1,000 amino acids, including 8.9 glycosylated hydroxylysines. A marked difference in fibril formation was found between these two kinds of collagen preparation, in that the maximal turbidity of the former was reached within 5 min under the standard assay conditions, whereas the absorbance of the latter increased until about 600 min. The critical concentration with the latter was about 10-fold, and the absorbance/microgram collagen incorporated into the fibrils was about one-sixth. The morphology of the fibrils was also different, in that the high hydroxylysine collagen formed thin fibrils with essentially no interfibril interaction or aggregation, whereas the low hydroxylysine collagen formed thick fibrils on a background of thin ones. The data thus indicate that regulation of the extents of lysine hydroxylation and hydroxylysine glycosylation may play a major role in the regulation of collagen fibril formation and the morphology of the fibrils.  (+info)

Stimulation of collagen galactosyltransferase and glucosyltransferase activities by lysophosphatidylcholine. (2/120)

Lysophosphatidylcholine stimulated the activities of collagen galactosyl- and glucosyl-transferases in chick-embryo extract and its particulate fractions in vitro, whereas essentially no stimulation was noted in the high-speed supernatant, where the enzymes are soluble and membrane-free. The stimulatory effect of lysophosphatidylcholine was masked by 0.1% Triton X-100. In kinetic experiments lysophosphatidylcholine raised the maximum velocities with respect to the substrates and co-substrates, whereas no changes were observed in the apparant Km values. Phospholipase A preincubation of the chick-embryo extract resulted in stimulation of both transferase activities, probably gy generating lysophosphatides from endogenous phospholipids. No stimulation by lysophosphatidylcholine was found when tested with 500-fold-purified glycosyltransferase. The results suggest that collagen glycosyltransferases must be associated with the membrane structures of the cell in order to be stimulated by lysophosphatidylcholine. Lysophosphatidylcholine could have some regulatory significance in vivo, since its concentration in the cell is comparable with that which produced marked stimulation in vitro.  (+info)

Comparative study of carbohydrate-protein complexes. II. Determination of hydroxylysine and its glycosides in human skin and scar collagens by an improved method. (3/120)

A modification of the existing methods for measuring hydroxylysine, galactosylhydroxylysine, and glucosylgalactosylhydroxylysine is described. The method is based on analysis with an automated amino acid analyzer using a conventional separation system for basic amino acids. The prior removal of acidic and neutral amino acids was necessary. This was achieved by passing an alkaline hydrolysate of collagen through a column of Amberlite CG-120, Type II (H+) and washing the column with 8% aqueous pyridine. A basic fraction containing the hydroxylysine compounds was then recovered from the column by elution with 3 M NH4OH. Model experiments showed that hydroxylysine and its glycosides could be analyzed with an hour and that recoveries exceeded 90%. This method was applied to human tissues to investigate whether the dermal scar is different in collagen composition from normal skin. With the limited number of samples analyzed, the data suggested that long-standing scar tissues reverted to a composition similar to that of normal skin. The composition of hydroxylysine-linked carbohydrate units is also discussed on the basis of the age-related change.  (+info)

Effect of L-azetidine-2-carboxylic acid on glycosylations of collagen in chick-embryo tendon cells. (4/120)

The glycosylations of hydroxylysine during collagen biosynthesis in isolated chick-embryo tendon cells were studied by using pulse-chase labelling experiments with [14C]-lysine. The hydroxylation of lysine and the glycosylations of hydroxylysine continued after a 5 min pulse label for up to about 10 min during the chase period. These data differ from those obtained previously in isolated chick-embryo cartilage cells, in which, after a similar 5 min pulse label, these reactions continued during the chase period for up to about 20 min. The collagen synthesized by the isolated chick-embryo tendon cells differed markedly from the type I collagen of adult tissues in its degree of hydroxylation of lysine residues and glycosylations of hydroxylysine residues. When the isolated tendon cells were incubated in the presence of L-azetidine-2-carboxylic acid, the degree of glycosylations of hydroxylysine during the first 10 min of the chase period was identical with that in cells incubated without thcarboxylic acid for at least 60 min, whereas no additional glycosylations took place in the control cells after the 10 min time-point. As a consequence, the collagen synthesized in the presence of this compound contained more carbohydrate than did the collagen synthesized by the control cells. Additional experiments indicated that azetidine-2-carboxylic acid did not increase the collagen glycosyltransferase activities in the tendon cells or the rate of glycosylation reactions when added directly to the enzyme incubation mixture. Control experiments with colchicine indicated that the delay in the rate of collagen secretion, which was observed in the presence of azetidine-2-carboxylic acid, did not in itself affect the degree of glycosylations of collagen. The results thus suggest that the increased glycosylations were due to inhibition of the collagen triple-helix formation, which is known to occur in the presence of azetidine-2-carboxylic acid.  (+info)

Blockade of ATP-sensitive potassium channels in cerebral arterioles inhibits vasoconstriction from hypocapnic alkalosis in cats. (5/120)

BACKGROUND AND PURPOSE: Recent studies have shown that the cerebral arteriolar dilation from hypercapnic acidosis is blocked by agents which inhibit KATP channels. These findings suggested that this response is due to opening of KATP channels. Because the repose to CO2 is a continuum, with hypercapnic acidosis causing vasodilation and hypocapnic alkalosis causing vasoconstriction, it would be expected that the response to hypocapnic alkalosis would be due to closing of KATP channels. There are no studies of the effect of inhibition of KATP channels on the response to hypocapnic alkalosis. METHODS: We investigated the effect of 3 agents that in earlier studies were found to inhibit KATP channels--NG-nitro-L-arginine, hydroxylysine, and glyburide--on the cerebral arteriolar constriction caused by graded hypocapnia induced by hyperventilation in anesthetized cats equipped with cranial windows. RESULTS: Hypocapnic alkalosis caused dose-dependent vasoconstriction that was inhibited completely by each of the 3 inhibitors of KATP channels. The blockade induced by these agents was eliminated in the presence of topical L-lysine (5 micromol/L). CONCLUSIONS: The findings show that agents which inhibit ATP-sensitive potassium channels in cerebral arterioles inhibit the vasoconstriction from hypocapnic alkalosis. These and earlier results showing that inhibition of KATP channels inhibited dilation from hypercapnic acidosis demonstrate that the response to CO2 in cerebral arterioles is mediated by the opening and closing of KATP channels.  (+info)

Serum galactosyl hydroxylysine as a biochemical marker of bone resorption. (6/120)

BACKGROUND: Serum-based biochemical markers of bone resorption may provide better clinical information than urinary markers because direct comparison with serum markers of bone formation is possible and because the within-subject variability of serum markers may be lower. We describe a method for the measurement of free beta-1-galactosyl-O-hydroxylysine (Gal-Hyl) in serum. METHODS: The assay used preliminary ultrafiltration of serum, dansylation, and separation by reversed-phase HPLC with fluorescence detection. Healthy subjects were recruited from population-based studies of bone turnover. RESULTS: The within-run (n = 15) and between-run (n = 15) CVs were 7% and 14%, respectively, at a mean value of 48 nmol/L. In women and pubertal girls, serum free Gal-Hyl correlated with urine free Gal-Hyl (r = 0.84; P <0.001). Serum Gal-Hyl was higher during puberty and increased after menopause. The fractional renal clearance of free Gal-Hyl relative to that of creatinine was 0.90 (95% confidence interval, 0.82-0.98). Serum free Gal-Hyl decreased by 36% (SE = 4%) in 14 patients with mild Paget disease treated with an oral bisphosphonate, and this decrease was significantly (P <0. 001) greater than that seen for either serum tartrate-resistant acid phosphatase (9%; SE = 4%) or serum C-terminal telopeptide of collagen I (19%; SE = 8%). CONCLUSION: Serum free Gal-Hyl may be useful as a serum marker of bone resorption.  (+info)

Lysylhydroxylation and non-reducible crosslinking of human supraspinatus tendon collagen: changes with age and in chronic rotator cuff tendinitis. (7/120)

OBJECTIVES: To investigate age related and site specific variations in turnover and chemistry of the collagen network in healthy tendons as well as the role of collagen remodelling in the degeneration of the supraspinatus tendon (ST-D) in rotator cuff tendinitis. METHODS: Collagen content and the amount of hydroxylysine (Hyl), hydroxy-lysylpyridinoline (HP), lysylpyridinoline (LP), and the degree of non-enzymatic glycation (pentosidine) were investigated in ST-D and in normal human supraspinatus (ST-N) and biceps brachii tendons (BT-N) by high-performance liquid chromatography. RESULTS: In BT-N, tendons that served as control tissue as it shows rarely matrix abnormalities, pentosidine levels rise linearly with age (20-90 years), indicating little tissue remodelling (resulting in an undisturbed accumulation of pentosidine). A similar accumulation was observed in ST-N up to 50 years. At older ages, little pentosidine accumulation was observed and pentosidine levels showed large interindividual variability. This was interpreted as remodelling of collagen in normal ST after age 50 years because of microruptures (thus diluting old collagen with newly synthesised collagen). All degenerate ST samples showed decreased pentosidine levels compared with age matched controls, indicating extensive remodelling in an attempt to repair the tendon defect. Collagen content and the amount of Hyl, HP, and LP of ST-N and BT-N did not change with age. With the exception of collagen content, which did not differ, all parameters were significantly (p < 0.001) lower in BT-N. The ST-D samples had a reduced collagen content and had higher Hyl, HP, and LP levels than ST-N (p < 0.001). CONCLUSIONS: Inasmuch as Hyl, HP, and LP levels in ST-N did not change with age, tissue remodelling as a consequence of microruptures does not seem to affect the quality of the tendon collagen. On the other hand, the clearly different profile of post-translational modifications in ST-D indicates that the newly deposited collagen network in degenerated tendons is qualitatively different. It is concluded that in ST-D the previously functional and carefully constructed matrix is replaced by aberrant collagen. This may result in a mechanically less stable tendon; as the supraspinatus is constantly subjected to considerable forces this could explain why tendinitis is mostly of a chronic nature.  (+info)

Adenoviral gene transfer restores lysyl hydroxylase activity in type VI Ehlers-Danlos syndrome. (8/120)

Type VI Ehlers-Danlos syndrome is a disease characterized by disturbed lysine hydroxylation of collagen. The disease is caused by mutations in lysyl hydroxylase 1 gene and it affects several organs including the cardiovascular system, the joint and musculoskeletal system, and the skin. The skin of type VI Ehlers-Danlos syndrome patients is hyperelastic, scars easily, and heals slowly and poorly. We hypothesized that providing functional lysyl hydroxylase 1 gene to the fibroblasts in and around wounds in these patients would improve healing. In this study we tested the feasibility of transfer of the lysyl hydroxylase 1 gene into fibroblasts derived from rats and a type VI Ehlers-Danlos syndrome patient (in vitro) and into rat skin (in vivo). We first cloned human lysyl hydroxylase 1 cDNA into a recombinant adenoviral vector (Ad5RSV-LH). Transfection of human type VI Ehlers-Danlos syndrome fibroblasts (about 20% of normal lysyl hydroxylase 1 activity) with the vector increased lysyl hydroxylase 1 activity in these cells to near or greater levels than that of wild type, unaffected fibroblasts. The adenoviral vector successfully transfected rat fibroblasts producing both beta-galactosidase and lysyl hydroxylase 1 gene activity. We next expanded our studies to a rodent model. Intradermal injections of the vector to the abdominal skin of rats produced lysyl hydroxylase 1 mRNA and elevated lysyl hydroxylase 1 activity, in vivo. These data suggest the feasibility of gene replacement therapy to modify skin wound healing in type VI Ehlers-Danlos syndrome patients.  (+info)

Hydroxylysine is a modified form of the amino acid lysine, which is formed by the addition of a hydroxyl group (-OH) to the lysine molecule. This process is known as hydroxylation and is catalyzed by the enzyme lysyl hydroxylase.

In the human body, hydroxylysine is an important component of collagen, which is a protein that provides structure and strength to tissues such as skin, tendons, ligaments, and bones. Hydroxylysine helps to stabilize the triple-helix structure of collagen by forming cross-links between individual collagen molecules.

Abnormalities in hydroxylysine metabolism can lead to various connective tissue disorders, such as Ehlers-Danlos syndrome and osteogenesis imperfecta, which are characterized by joint hypermobility, skin fragility, and bone fractures.

Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase is an enzyme that plays a crucial role in the biosynthesis of collagen. The medical definition of this enzyme is:

"An enzyme that catalyzes the post-translational modification of specific lysine residues in procollagens and related proteins. This enzyme requires Fe2+, 2-oxoglutarate, molecular oxygen, and ascorbic acid as cofactors. It hydroxylates certain lysine residues to form hydroxylysine, which is essential for the stabilization of collagen triple helices and for the formation of covalent cross-links between individual collagen molecules. Mutations in this gene have been associated with several types of Ehlers-Danlos syndrome."

The systematic name for this enzyme is "procollagen-lysine, 2-oxoglutarate 5-dioxygenase (hydroxylating)." It is also known as "procollagen-lysine, lysine hydroxylase," or simply "LH." This enzyme is responsible for the hydroxylation of specific lysine residues in procollagens and related proteins during their biosynthesis. The hydroxylation reaction catalyzed by this enzyme involves the incorporation of a hydroxyl group (-OH) into the lysine side chain, resulting in the formation of hydroxylysine. This modification is essential for the proper folding and stabilization of collagen molecules, as well as for their subsequent cross-linking and assembly into extracellular matrix structures.

Defects or mutations in the gene encoding this enzyme can lead to various types of Ehlers-Danlos syndrome (EDS), a group of heritable connective tissue disorders characterized by joint hypermobility, skin hyperextensibility, and tissue fragility.

Lathyrism is a neurological disorder caused by the consumption of large amounts of food sources containing a toxin called β-N-oxalyl-L-α,β-diaminopropionic acid (ODAP), which is found in certain legumes of the genus Lathyrus, particularly in grass peas (L. sativus). This disorder is characterized by the irreversible spastic paralysis of lower limbs due to damage in the upper motor neurons of the spinal cord. The onset and severity of lathyrism depend on the amount and duration of ODAP-containing food intake, with higher doses and longer exposure leading to more severe symptoms. Lathyrism is more prevalent in regions where grass peas are a staple food and access to diverse nutrition is limited.

Collagen is the most abundant protein in the human body, and it is a major component of connective tissues such as tendons, ligaments, skin, and bones. Collagen provides structure and strength to these tissues and helps them to withstand stretching and tension. It is made up of long chains of amino acids, primarily glycine, proline, and hydroxyproline, which are arranged in a triple helix structure. There are at least 16 different types of collagen found in the body, each with slightly different structures and functions. Collagen is important for maintaining the integrity and health of tissues throughout the body, and it has been studied for its potential therapeutic uses in various medical conditions.

Lysine is an essential amino acid, which means that it cannot be synthesized by the human body and must be obtained through the diet. Its chemical formula is (2S)-2,6-diaminohexanoic acid. Lysine is necessary for the growth and maintenance of tissues in the body, and it plays a crucial role in the production of enzymes, hormones, and antibodies. It is also essential for the absorption of calcium and the formation of collagen, which is an important component of bones and connective tissue. Foods that are good sources of lysine include meat, poultry, fish, eggs, and dairy products.

Hydroxyproline is not a medical term per se, but it is a significant component in the medical field, particularly in the study of connective tissues and collagen. Here's a scientific definition:

Hydroxyproline is a modified amino acid that is formed by the post-translational modification of the amino acid proline in collagen and some other proteins. This process involves the addition of a hydroxyl group (-OH) to the proline residue, which alters its chemical properties and contributes to the stability and structure of collagen fibers. Collagen is the most abundant protein in the human body and is a crucial component of connective tissues such as tendons, ligaments, skin, and bones. The presence and quantity of hydroxyproline can serve as a marker for collagen turnover and degradation, making it relevant to various medical and research contexts, including the study of diseases affecting connective tissues like osteoarthritis, rheumatoid arthritis, and Ehlers-Danlos syndrome.

Adipates are a group of chemical compounds that are esters of adipic acid. Adipic acid is a dicarboxylic acid with the formula (CH₂)₄(COOH)₂. Adipates are commonly used as plasticizers in the manufacture of polyvinyl chloride (PVC) products, such as pipes, cables, and flooring. They can also be found in cosmetics, personal care products, and some food additives.

Adipates are generally considered to be safe for use in consumer products, but like all chemicals, they should be used with caution and in accordance with recommended guidelines. Some adipates have been shown to have potential health effects, such as endocrine disruption and reproductive toxicity, at high levels of exposure. Therefore, it is important to follow proper handling and disposal procedures to minimize exposure.

Amino acids are organic compounds that serve as the building blocks of proteins. They consist of a central carbon atom, also known as the alpha carbon, which is bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom (H), and a variable side chain (R group). The R group can be composed of various combinations of atoms such as hydrogen, oxygen, sulfur, nitrogen, and carbon, which determine the unique properties of each amino acid.

There are 20 standard amino acids that are encoded by the genetic code and incorporated into proteins during translation. These include:

1. Alanine (Ala)
2. Arginine (Arg)
3. Asparagine (Asn)
4. Aspartic acid (Asp)
5. Cysteine (Cys)
6. Glutamine (Gln)
7. Glutamic acid (Glu)
8. Glycine (Gly)
9. Histidine (His)
10. Isoleucine (Ile)
11. Leucine (Leu)
12. Lysine (Lys)
13. Methionine (Met)
14. Phenylalanine (Phe)
15. Proline (Pro)
16. Serine (Ser)
17. Threonine (Thr)
18. Tryptophan (Trp)
19. Tyrosine (Tyr)
20. Valine (Val)

Additionally, there are several non-standard or modified amino acids that can be incorporated into proteins through post-translational modifications, such as hydroxylation, methylation, and phosphorylation. These modifications expand the functional diversity of proteins and play crucial roles in various cellular processes.

Amino acids are essential for numerous biological functions, including protein synthesis, enzyme catalysis, neurotransmitter production, energy metabolism, and immune response regulation. Some amino acids can be synthesized by the human body (non-essential), while others must be obtained through dietary sources (essential).

Somatostatin-28 is a form of somatostatin, which is a naturally occurring hormone in the body that inhibits the release of several hormones and also acts as a neurotransmitter. Somatostatin exists in two major forms, namely somatostatin-14 and somatostatin-28, with the latter being a longer variant containing 28 amino acids.

Somatostatin-28 is produced by various tissues, including the hypothalamus, pancreas, and gastrointestinal tract. It exerts its effects through specific receptors (SST1-5) that are widely distributed in the body. Somatostatin-28 has a higher potency than somatostatin-14 in inhibiting the release of several hormones such as growth hormone, thyroid-stimulating hormone, insulin, glucagon, and gastrin.

In addition to its endocrine functions, somatostatin-28 also has neuromodulatory effects on the central nervous system, where it regulates neurotransmission and neural excitability. Overall, somatostatin-28 plays a crucial role in regulating various physiological processes, including hormonal homeostasis, appetite regulation, and neurotransmission.

I'm sorry for any confusion, but "Pimelic Acids" is not a recognized medical term or concept in physiology, pathology, or pharmacology. It appears to be a term used in chemistry and biochemistry, referring to a specific type of organic compound known as a dicarboxylic acid with a seven-carbon backbone.

In biochemistry, pimelic acid may be involved in various metabolic processes, such as the synthesis of certain amino acids and lipids. However, it is not typically considered a medical term or diagnostic marker in clinical settings. If you're looking for information related to a specific medical condition or treatment, I would be happy to help if you could provide more context!

Protein hydrolysates are defined as proteins that have been broken down into smaller peptide chains or individual amino acids through a process called hydrolysis. This process involves the use of water, enzymes, or acids to break the bonds between the amino acids in the protein molecule.

Protein hydrolysates are often used in medical and nutritional applications because they are easier to digest and absorb than intact proteins. They are also less likely to cause allergic reactions or digestive discomfort in individuals who have difficulty tolerating whole proteins. Protein hydrolysates can be derived from a variety of sources, including animal proteins such as collagen and casein, as well as plant proteins such as soy and wheat.

In addition to their use in medical and nutritional applications, protein hydrolysates are also used in the food industry as flavor enhancers, emulsifiers, and texturizers. They are commonly found in products such as infant formula, sports drinks, and clinical nutrition formulas.

Glycosides are organic compounds that consist of a glycone (a sugar component) linked to a non-sugar component, known as an aglycone, via a glycosidic bond. They can be found in various plants, microorganisms, and some animals. Depending on the nature of the aglycone, glycosides can be classified into different types, such as anthraquinone glycosides, cardiac glycosides, and saponin glycosides.

These compounds have diverse biological activities and pharmacological effects. For instance:

* Cardiac glycosides, like digoxin and digitoxin, are used in the treatment of heart failure and certain cardiac arrhythmias due to their positive inotropic (contractility-enhancing) and negative chronotropic (heart rate-slowing) effects on the heart.
* Saponin glycosides have potent detergent properties and can cause hemolysis (rupture of red blood cells). They are used in various industries, including cosmetics and food processing, and have potential applications in drug delivery systems.
* Some glycosides, like amygdalin found in apricot kernels and bitter almonds, can release cyanide upon hydrolysis, making them potentially toxic.

It is important to note that while some glycosides have therapeutic uses, others can be harmful or even lethal if ingested or otherwise introduced into the body in large quantities.

Pepsin A is defined as a digestive enzyme that is primarily secreted by the chief cells in the stomach's fundic glands. It plays a crucial role in protein catabolism, helping to break down food proteins into smaller peptides during the digestive process. Pepsin A has an optimal pH range of 1.5-2.5 for its enzymatic activity and is activated from its inactive precursor, pepsinogen, upon exposure to acidic conditions in the stomach.

Hydroxylation is a biochemical process that involves the addition of a hydroxyl group (-OH) to a molecule, typically a steroid or xenobiotic compound. This process is primarily catalyzed by enzymes called hydroxylases, which are found in various tissues throughout the body.

In the context of medicine and biochemistry, hydroxylation can have several important functions:

1. Drug metabolism: Hydroxylation is a common way that the liver metabolizes drugs and other xenobiotic compounds. By adding a hydroxyl group to a drug molecule, it becomes more polar and water-soluble, which facilitates its excretion from the body.
2. Steroid hormone biosynthesis: Hydroxylation is an essential step in the biosynthesis of many steroid hormones, including cortisol, aldosterone, and the sex hormones estrogen and testosterone. These hormones are synthesized from cholesterol through a series of enzymatic reactions that involve hydroxylation at various steps.
3. Vitamin D activation: Hydroxylation is also necessary for the activation of vitamin D in the body. In order to become biologically active, vitamin D must undergo two successive hydroxylations, first in the liver and then in the kidneys.
4. Toxin degradation: Some toxic compounds can be rendered less harmful through hydroxylation. For example, phenol, a toxic compound found in cigarette smoke and some industrial chemicals, can be converted to a less toxic form through hydroxylation by enzymes in the liver.

Overall, hydroxylation is an important biochemical process that plays a critical role in various physiological functions, including drug metabolism, hormone biosynthesis, and toxin degradation.

Chromatography is a technique used in analytical chemistry for the separation, identification, and quantification of the components of a mixture. It is based on the differential distribution of the components of a mixture between a stationary phase and a mobile phase. The stationary phase can be a solid or liquid, while the mobile phase is a gas, liquid, or supercritical fluid that moves through the stationary phase carrying the sample components.

The interaction between the sample components and the stationary and mobile phases determines how quickly each component will move through the system. Components that interact more strongly with the stationary phase will move more slowly than those that interact more strongly with the mobile phase. This difference in migration rates allows for the separation of the components, which can then be detected and quantified.

There are many different types of chromatography, including paper chromatography, thin-layer chromatography (TLC), gas chromatography (GC), liquid chromatography (LC), and high-performance liquid chromatography (HPLC). Each type has its own strengths and weaknesses, and is best suited for specific applications.

In summary, chromatography is a powerful analytical technique used to separate, identify, and quantify the components of a mixture based on their differential distribution between a stationary phase and a mobile phase.

Protein-Lysine 6-Oxidase (PLOX) is an enzyme that belongs to the family of copper-containing oxidases. It catalyzes the oxidative deamination of specific lysine residues in proteins, resulting in the formation of lysine-6-aldehydes, ammonia, and hydrogen peroxide. This enzyme plays a crucial role in various biological processes, including the regulation of protein function, modification of extracellular matrices, and the maintenance of copper homeostasis. Mutations in the gene encoding PLOX have been associated with certain diseases, such as Menkes disease, a rare X-linked recessive disorder characterized by copper deficiency and neurological symptoms.

Norleucine is not typically defined in a medical context, but it is a chemical compound used in research and biochemistry. It is an unnatural amino acid that is sometimes used as a substitute for the naturally occurring amino acid methionine in scientific studies. Norleucine has a different side chain than methionine, which can affect the properties of proteins when it is substituted for methionine.

In terms of its chemical structure, norleucine is a straight-chain aliphatic amino acid with a four-carbon backbone and a carboxyl group at one end and an amino group at the other end. It has a branched side chain consisting of a methyl group and an ethyl group.

While norleucine is not typically used as a therapeutic agent in medicine, it may have potential applications in the development of new drugs or in understanding the functions of proteins in the body.

Cyanogen bromide is a solid compound with the chemical formula (CN)Br. It is a highly reactive and toxic substance that is used in research and industrial settings for various purposes, such as the production of certain types of resins and gels. Cyanogen bromide is an alkyl halide, which means it contains a bromine atom bonded to a carbon atom that is also bonded to a cyano group (a nitrogen atom bonded to a carbon atom with a triple bond).

Cyanogen bromide is classified as a class B poison, which means it can cause harm or death if swallowed, inhaled, or absorbed through the skin. It can cause irritation and burns to the eyes, skin, and respiratory tract, and prolonged exposure can lead to more serious health effects, such as damage to the nervous system and kidneys. Therefore, it is important to handle cyanogen bromide with care and to use appropriate safety precautions when working with it.

In the context of medicine, "chemistry" often refers to the field of study concerned with the properties, composition, and structure of elements and compounds, as well as their reactions with one another. It is a fundamental science that underlies much of modern medicine, including pharmacology (the study of drugs), toxicology (the study of poisons), and biochemistry (the study of the chemical processes that occur within living organisms).

In addition to its role as a basic science, chemistry is also used in medical testing and diagnosis. For example, clinical chemistry involves the analysis of bodily fluids such as blood and urine to detect and measure various substances, such as glucose, cholesterol, and electrolytes, that can provide important information about a person's health status.

Overall, chemistry plays a critical role in understanding the mechanisms of diseases, developing new treatments, and improving diagnostic tests and techniques.

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.

Chemical phenomena refer to the changes and interactions that occur at the molecular or atomic level when chemicals are involved. These phenomena can include chemical reactions, in which one or more substances (reactants) are converted into different substances (products), as well as physical properties that change as a result of chemical interactions, such as color, state of matter, and solubility. Chemical phenomena can be studied through various scientific disciplines, including chemistry, biochemistry, and physics.

A tendon is the strong, flexible band of tissue that connects muscle to bone. It helps transfer the force produced by the muscle to allow various movements of our body parts. Tendons are made up of collagen fibers arranged in parallel bundles and have a poor blood supply, making them prone to injuries and slow to heal. Examples include the Achilles tendon, which connects the calf muscle to the heel bone, and the patellar tendon, which connects the kneecap to the shinbone.

Cartilage is a type of connective tissue that is found throughout the body in various forms. It is made up of specialized cells called chondrocytes, which are embedded in a firm, flexible matrix composed of collagen fibers and proteoglycans. This unique structure gives cartilage its characteristic properties of being both strong and flexible.

There are three main types of cartilage in the human body: hyaline cartilage, elastic cartilage, and fibrocartilage.

1. Hyaline cartilage is the most common type and is found in areas such as the articular surfaces of bones (where they meet to form joints), the nose, trachea, and larynx. It has a smooth, glassy appearance and provides a smooth, lubricated surface for joint movement.
2. Elastic cartilage contains more elastin fibers than hyaline cartilage, which gives it greater flexibility and resilience. It is found in structures such as the external ear and parts of the larynx and epiglottis.
3. Fibrocartilage has a higher proportion of collagen fibers and fewer chondrocytes than hyaline or elastic cartilage. It is found in areas that require high tensile strength, such as the intervertebral discs, menisci (found in joints like the knee), and the pubic symphysis.

Cartilage plays a crucial role in supporting and protecting various structures within the body, allowing for smooth movement and providing a cushion between bones to absorb shock and prevent wear and tear. However, cartilage has limited capacity for self-repair and regeneration, making damage or degeneration of cartilage tissue a significant concern in conditions such as osteoarthritis.

Picolinic acid is not specifically classified as a medical term, but it is a type of organic compound that belongs to the class of molecules known as pyridinecarboxylic acids. These are carboxylic acids derived from pyridine by the substitution of a hydrogen atom with a carboxyl group.

Picolinic acid, specifically, is a pyridine derivative with a carboxyl group at the 2-position of the ring. It is naturally produced in the body and can be found in various tissues and fluids, including the brain, where it plays a role in the metabolism of amino acids, particularly tryptophan.

In addition to its physiological functions, picolinic acid has been studied for its potential therapeutic applications. For example, it has been shown to have antibacterial and antifungal properties, and may also play a role in heavy metal chelation and neuroprotection. However, more research is needed to fully understand the medical significance of this compound.

Cross-linking reagents are chemical agents that are used to create covalent bonds between two or more molecules, creating a network of interconnected molecules known as a cross-linked structure. In the context of medical and biological research, cross-linking reagents are often used to stabilize protein structures, study protein-protein interactions, and develop therapeutic agents.

Cross-linking reagents work by reacting with functional groups on adjacent molecules, such as amino groups (-NH2) or sulfhydryl groups (-SH), to form a covalent bond between them. This can help to stabilize protein structures and prevent them from unfolding or aggregating.

There are many different types of cross-linking reagents, each with its own specificity and reactivity. Some common examples include glutaraldehyde, formaldehyde, disuccinimidyl suberate (DSS), and bis(sulfosuccinimidyl) suberate (BS3). The choice of cross-linking reagent depends on the specific application and the properties of the molecules being cross-linked.

It is important to note that cross-linking reagents can also have unintended effects, such as modifying or disrupting the function of the proteins they are intended to stabilize. Therefore, it is essential to use them carefully and with appropriate controls to ensure accurate and reliable results.

Carbohydrates are a major nutrient class consisting of organic compounds that primarily contain carbon, hydrogen, and oxygen atoms. They are classified as saccharides, which include monosaccharides (simple sugars), disaccharides (double sugars), oligosaccharides (short-chain sugars), and polysaccharides (complex carbohydrates).

Monosaccharides, such as glucose, fructose, and galactose, are the simplest form of carbohydrates. They consist of a single sugar molecule that cannot be broken down further by hydrolysis. Disaccharides, like sucrose (table sugar), lactose (milk sugar), and maltose (malt sugar), are formed from two monosaccharide units joined together.

Oligosaccharides contain a small number of monosaccharide units, typically less than 20, while polysaccharides consist of long chains of hundreds to thousands of monosaccharide units. Polysaccharides can be further classified into starch (found in plants), glycogen (found in animals), and non-starchy polysaccharides like cellulose, chitin, and pectin.

Carbohydrates play a crucial role in providing energy to the body, with glucose being the primary source of energy for most cells. They also serve as structural components in plants (cellulose) and animals (chitin), participate in various metabolic processes, and contribute to the taste, texture, and preservation of foods.

... (Hyl) is an amino acid with the molecular formula C6H14N2O3. It was first discovered in 1921 by Donald Van Slyke ... Hydroxylysine at University of Oulu de Lorenzo, V.; et al. (Feb 1986). "Aerobactin biosynthesis and transport genes of plasmid ... Hydroxylysine at the U.S. National Library of Medicine Medical Subject Headings (MeSH) (Articles without InChI source, Articles ... as the 5-hydroxylysine form. It arises from a post-translational hydroxy modification of lysine. It is most widely known as a ...
In enzymology, a hydroxylysine kinase (EC 2.7.1.81) is an enzyme that catalyzes the chemical reaction GTP + 5-hydroxy-L-lysine ... Hiles RA, Henderson LM (1972). "The partial purification and properties of hydroxylysine kinase from rat liver". J. Biol. Chem ... Other names in common use include hydroxylysine kinase (phosphorylating), and guanosine triphosphate:5-hydroxy-L-lysine O- ...
Other names in common use include N6-hydroxylysine:acetyl CoA N6-transacetylase, N6-hydroxylysine acetylase, and acetyl-CoA:6-N ... Coy M, Paw BH, Bindereif A, Neilands JB (1986). "Isolation and properties of N epsilon-hydroxylysine:acetyl coenzyme A N ... In enzymology, a N6-hydroxylysine O-acetyltransferase (EC 2.3.1.102) is an enzyme that catalyzes the chemical reaction acetyl- ...
... (EC 6.3.2.38, N(alpha)-citryl-N(epsilon)-acetyl-N(epsilon)-hydroxylysine synthase ... N2-citryl-N6-acetyl-N6-hydroxylysine+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: ... N6-acetyl-N6-hydroxylysine". J. Am. Chem. Soc. 104 (11): 3096-3101. doi:10.1021/ja00375a025. de Lorenzo V, Bindereif A, Paw BH ...
A possible way to prevent the build-up of metabolites is to limit lysine and hydroxylysine degradation, as lysine is one of the ... This enzyme is involved in degrading the amino acids lysine, hydroxylysine and tryptophan. Mutations in the GCDH gene prevent ... lysine thus becomes hydroxylysine. GA1 worsens during stresses and catabolic episodes, such as fasts and infections. Endogenous ... hydroxylysine and tryptophan. Excessive levels of their intermediate breakdown products (glutaric acid, glutaryl-CoA, 3- ...
The role of lysine in collagen has been outlined above, however, a lack of lysine and hydroxylysine involved in the ... Hydroxylysine-deficient collagen disease". The New England Journal of Medicine. 286 (19): 1013-1020. doi:10.1056/ ...
Glycosylation of specific hydroxylysine residues occurs. Triple alpha helical structure is formed inside the endoplasmic ... Hydroxyproline derived from proline Hydroxylysine derived from lysine - depending on the type of collagen, varying numbers of ... This enzyme acts on lysines and hydroxylysines producing aldehyde groups, which will eventually undergo covalent bonding ... to produce hydroxyproline and hydroxylysine) occurs to aid cross-linking of the alpha peptides. This enzymatic step requires ...
Second, some of the lysine residues are hydroxylated or glycosylated, and some lysine as well as hydroxylysine residues undergo ... In addition, crosslinks form between certain lysine and hydroxylysine residues. In the extracellular space in tissues, type III ...
The core-specific lectin contains hydroxyproline, hydroxylysine, and glucosylgalactosylhydroxylysine residues". J Biol Chem. ...
Butler WT, Cunningham LW (1966). "Evidence for the linkage of a disaccharide to hydroxylysine in tropocollagen". J. Biol. Chem ...
Bosmann HB, Eylar EH (1968). "Glycoprotein biosynthesis: the biosynthesis of the hydroxylysine-galactose linkage in collagen". ... Other names in common use include hydroxylysine galactosyltransferase, collagen galactosyltransferase, collagen hydroxylysyl ... 5-hydroxylysine-collagen galactosyltransferase. This enzyme participates in lysine degradation. ...
Secondary amino acid Imino acid Hydroxylysine R.H.A. Plimmer (1912) [1908]. R.H.A. Plimmer; F.G. Hopkins (eds.). The chemical ...
Lysine may also be hydroxylated on its δ-C atom, forming hydroxylysine (Hyl). These three reactions are catalyzed by very large ...
The systematic name is protein-α-D-glucosyl-1,2-β-D-galactosyl-L-hydroxylysine glucohydrolase. Other names in common use ... Isolation of 2-O-α-D-glucopyranosyl-O-β-D-galactopyranosyl-hydroxylysine glucohydrolase from rat spleens". Eur. J. Biochem. 111 ... Sternberg M, Spiro RG (1979). "Studies on the catabolism of the hydroxylysine-linked disaccharide units of basement membranes ... Hamazaki H, Hotta K (1979). "Purification and characterization of an α-glucosidase specific for hydroxylysine-linked ...
A major achievement during this time was the discovery of the amino acid hydroxylysine. Work with G. E. Cullen on urease led to ...
Because of this addition of an oxygen, hydroxylysine can then be modified by O-glycosylation. Addition of a galactose to the ... O-galactose is commonly found on lysine residues in collagen, which often have a hydroxyl group added to form hydroxylysine. ... Harwood R, Grant ME, Jackson DS (November 1975). "Studies on the glycosylation of hydroxylysine residues during collagen ... but occurs predominantly in the Golgi apparatus and only on hydroxylysine residues in a specific sequence. While this O- ...
Hydroxyproline and hydroxylysine are important for stabilizing collagen by cross-linking the propeptides in collagen. Collagen ...
N6-acetyl-N6-hydroxylysine". J. Am. Chem. Soc. 104 (11): 3096-3101. doi:10.1021/ja00375a025. de Lorenzo V, Bindereif A, Paw BH ...
"Molecular identification of hydroxylysine kinase and of ammoniophospholyases acting on 5-phosphohydroxy-L-lysine and ...
These bonds covalently connect hydroxylysine and methionine residues of adjacent polypeptide strands to form a larger collagen ...
... attached to collagen hydroxylysines. Collagen lysyl hydroxylation is the first step in collagen pyridinoline cross-linking, ... are alpha-ketoglutarate-dependent hydroxylases enzymes that catalyze the hydroxylation of lysine to hydroxylysine. Lysyl ...
... and hydroxylysine in mammals. Within mitochondria, 2-oxoadipate is converted into acetyl-CoA. Model organisms have been used in ...
The protein encoded by this gene is one of two enzymes that transfers galactose moieties to hydroxylysine residues of collagen ...
Kelly and Rice discovered that the protein lacked the presence of hydroxyproline and hydroxylysine, which are amino acids ...
... activity of minoxidil inhibition of enzyme lysyl hydroxylase present in fibroblast may result in synthesis of a hydroxylysine- ...
... or hydroxylysine; they, therefore, strongly resemble collagen fibrils. C1q is composed of 18 polypeptide chains: six A-chains, ...
O-linked glycans attached to the hydroxyl oxygen of serine, threonine, tyrosine, hydroxylysine, or hydroxyproline side-chains, ...
L-hydroxylysine, and L-tryptophan. Specifically, this enzyme catalyzes the decarboxylation of 2-oxoadipate to glutaryl-CoA. ... hydroxylysine, and tryptophan degradation. Only a handful of mutations have been observed in patients, including three missense ...
... and hydroxylysine. The way it completes this task is through a series of physical, chemical, and electron-transfer steps. It ... L-hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. The enzyme ...
... but also on tyrosine or non-canonical amino acids such as hydroxylysine and hydroxyproline. In P-glycosylation, sugars are ...
Hydroxylysine (Hyl) is an amino acid with the molecular formula C6H14N2O3. It was first discovered in 1921 by Donald Van Slyke ... Hydroxylysine at University of Oulu de Lorenzo, V.; et al. (Feb 1986). "Aerobactin biosynthesis and transport genes of plasmid ... Hydroxylysine at the U.S. National Library of Medicine Medical Subject Headings (MeSH) (Articles without InChI source, Articles ... as the 5-hydroxylysine form. It arises from a post-translational hydroxy modification of lysine. It is most widely known as a ...
5-Hydroxylysine is a hydroxylated derivative of the amino acid L-Lysine that is present in certain collagens. A ... Hydroxylysine is an amino acid and is most widely known as a component of collagen. ... Hydroxylysine is an amino acid and is most widely known as a component of collagen. 5-Hydroxylysine is a hydroxylated ...
The resulting galactosyl-hydroxylysine (Gal-Hyl) and less abundant glucosyl-galactosyl-hydroxylysine (Glc-Gal-Hyl) are amongst ... The resulting galactosyl-hydroxylysine (Gal-Hyl) and less abundant glucosyl-galactosyl-hydroxylysine (Glc-Gal-Hyl) are amongst ... Collagen hydroxylysine glycosylation: non-conventional substrates for atypical glycosyltransferase enzymes. De Giorgi, ... to specific hydroxylysine residues on procollagen alpha chains. ... to specific hydroxylysine residues on procollagen alpha chains ...
Explore the 1 paper that mention a possible interaction between Clodronic Acid and Hydroxylysine. ... hydroxylysine residues in the alpha-chains of bone, skin and cartilage collagen.. " ...
lysine, hydroxylysine, and tryptophan.. Mutations in the GCDH gene prevent production of the enzyme or result in the production ... lysine, hydroxylysine, and tryptophan, which are building blocks of protein. Excessive levels of these amino acids and their ... A shortage (deficiency) of this enzyme allows lysine, hydroxylysine and tryptophan and their intermediate breakdown products to ... The intermediate breakdown products resulting from incomplete processing of lysine, hydroxylysine, and tryptophan can damage ...
involved_in hydroxylysine biosynthetic process IEA Inferred from Electronic Annotation. more info ...
its post-translational form with one or two added groups (e.g., Cystine, Hydroxylysine, Hydroxyproline, Dimethylglycine, and 3- ...
hydroxylysine kinase [EC:2.7.1.81]. K22579 rifampicin phosphotransferase [EC:2.7.9.6]. All links ...
Pediatric Reference Intervals, Eighth Edition, is a must-have for clinical chemists, hematologists, pathologists, endocrinologists and pediatricians. This...
Improve your day-to-day wellness with Swanson Premium Collagen Peptides Unflavored 19.75 oz Pwdr from Swanson Health Products.
L-Hydroxylysine 132mg. L-Hydroxyproline 1254mg. L-Isoleucine 165mg. Leucine 318mg Lysine 374mg. Methionine 66mg. Phenylalanine ... L-Hydroxylysine 132mg. L-Hydroxyproline 1254mg. L-Isoleucine 165mg. Leucine 318mg Lysine 374mg. Methionine 66mg. Phenylalanine ...
Collagen molecules in cartilage contain large amounts of hydroxyproline and hydroxylysine. The molecules form a triple helix ...
Hydroxylysine, to improve skins firmness and elasticity.. *Hydroxyproline, which can reduce the appearance of wrinkles. ...
hydroxylysine (2) * hydroxyproline (2) * kidney (2) Issue Section. Filter by issue-section. * Original Articles (5) ...
Hydroxylation which occurs commonly on praline and hydroxylysine. Term. What enzyme causes Hydroxylation of praline and lysine? ...
Collagen is rich in hydroxylysine and hydroxyproline moieties, which enable it to form strong cross-links. The hydroxylation of ...
Hydroxylysine 170 mg**. Hydroxyproline 2,269 mg**. Isoleucine 298 mg**. Leucine 571 mg**. Lysine 717 mg**. Methionine 173 mg** ...
The 2-Oxoglutarate-Dependent Oxygenase JMJD6 Catalyses Oxidation of Lysine Residues to give 5S-Hydroxylysine Residues (2011). ...
A protein modification that effectively converts an L-lysine residue to O5-galactosyl-L-hydroxylysine. ...
2S,5R)-5-hydroxylysine PsiMod Definition A protein modification that effectively converts an L-lysine residue to 5-hydroxy-L- ...
Increased urinary hydroxyproline and hydroxylysine levels, suggestive of connective tissue breakdown, were measured immediately ...
QuickDetect Hydroxylysine (Human) ELISA Package deal ( Catalog # E4714-100 ; 96 assays ; Storage at 4ºC ) 05/19 I. Introduction ...
QuickDetect Hydroxylysine (Human) ELISA Package deal ( Catalog # E4714-100 ; 96 assays ; Storage at 4ºC ) 05/19 I. Introduction ...
For example, 4-hydroxyproline can be substituted for proline; 5-hydroxylysine can be substituted for lysine; 3-methylhistidine ...
iHyd-PseAAC: predicting hydroxyproline and hydroxylysine in proteins by incorporating dipeptide position-specific propensity ... iHyd-PseAAC: predicting hydroxyproline and hydroxylysine in proteins by incorporating dipeptide position-specific propensity ... iHyd-PseAAC: predicting hydroxyproline and hydroxylysine in proteins by incorporating dipeptide position-specific propensity ... iHyd-PseAAC: predicting hydroxyproline and hydroxylysine in proteins by incorporating dipeptide position-specific propensity ...
Galactosylation of collagen propeptide hydroxylysines by PLOD3 (Homo sapiens) * PLOD3:Fe2+ dimer:Galactosyl-hydroxylysyl ... Glucosylation of collagen propeptide hydroxylysines (Homo sapiens) * PLOD3:Fe2+ dimer:Galactosyl-hydroxylysyl collagen ... Galactosylation of collagen propeptide hydroxylysines by procollagen galactosyltransferases 1, 2. (Homo sapiens) * COLGALT1, ... A protein modification that effectively converts an L-lysine residue to O5-galactosyl-L-hydroxylysine. ...
Natural Amino Acids From Peptides Collagen Specific Hydroxyproline and Hydroxylysine. Essential Lysine, Leucine, Valine, ...
Also acts on protein 5-hydroxylysine. *Catalyzes the final known enzymic step required for collagen and elastin cross-linking ...
The isolation of hydroxylysine from a gelatin hydrolysate. 1950, Vol. 15, pp. 288-294 [Abstract] ...
  • Natural Amino Acids From Peptides Collagen Specific Hydroxyproline and Hydroxylysine. (vitaminlife.com)
  • 5-Hydroxylysine is a hydroxylated derivative of the amino acid L-Lysine that is present in certain collagens . (nutrawiki.org)
  • To allow proper folding in triple-helices and organization in quaternary super-structures, collagen molecules require essential post-translational modifications (PTMs), including hydroxylation of proline and lysine residues, and subsequent attachment of glycan moieties (galactose and glucose) to specific hydroxylysine residues on procollagen alpha chains. (unipv.it)
  • lysine, hydroxylysine, and tryptophan. (medlineplus.gov)
  • A shortage (deficiency) of this enzyme allows lysine, hydroxylysine and tryptophan and their intermediate breakdown products to build up to abnormal levels, especially at times when the body is under stress. (medlineplus.gov)
  • The intermediate breakdown products resulting from incomplete processing of lysine, hydroxylysine, and tryptophan can damage the brain, particularly the basal ganglia, causing the signs and symptoms of glutaric acidemia type I. (medlineplus.gov)
  • GA-1 is an autosomal recessive disorder caused by deficiency of glutaryl-CoA dehydrogenase, a mitochon- drial enzyme involved in the metabolism of lysine, hydroxylysine and tryptophan. (who.int)
  • Glutaric aciduria type 1 is an autosomal-recessive disorder resulting from a deficiency of mitochondrial glutaryl-CoA dehydrogenase (EC 1.3.99.7, GCDH) which is involved in the metabolism of lysine, hydroxylysine, and tryptophan. (loinc.org)
  • Hydroxylysine is an amino acid and is most widely known as a component of collagen . (nutrawiki.org)
  • The resulting galactosyl-hydroxylysine (Gal-Hyl) and less abundant glucosyl-galactosyl-hydroxylysine (Glc-Gal-Hyl) are amongst the simplest glycosylation patterns found in nature and are essential for collagen and ECM homeostasis. (unipv.it)
  • Galactosylation of collagen propeptide hydroxylysines by procollagen galactosyltransferases 1, 2. (reactome.org)
  • Alkenes from unsaturated fatty acids and ceramides can also be converted to glycols by osmium tetroxide and then oxidized by periodate to aldehydes, and periodate will oxidize certain β-aminoethanol derivatives such as the hydroxylysine residues in collagen, as well as methionine (to its sulfoxide) and certain thiols (usually to disulfides). (thermofisher.com)
  • Hydroxylysine (Hyl) is an amino acid with the molecular formula C6H14N2O3. (wikipedia.org)
  • Also acts on protein 5-hydroxylysine. (expasy.org)
  • While intracellular functions have been reported for LOX proteins, the primary role of this family of enzymes is the remodeling of the extracellular matrix (ECM), due to their capacity to convert lysine and hydroxylysine residues in collagens and elastin into highly reactive aldehydes, which eventually condense with other oxidized groups or intact lysines to form a variety of inter- and intrachain cross-linkages. (nature.com)
  • The enzyme catalyzes oxidative deamination of the epsilon-amino group in certain lysine and hydroxylysine residues of collagens and lysine residues of elastin. (origene.com)
  • LOXL2 catalyzes the oxidative deamination of lysine and hydroxylysine residues in extracellular matrix (ECM) proteins to promote crosslinking of these proteins, and thereby plays a major role in ECM remodeling. (ku.edu)
  • Here we outline the type of information that ssNMR can provide and describe the procedures involved in a ssNMR structural study, with particular focus on using dynamic nuclear polarization to enhance sensitivity for detecting hydroxylysine residues by ssNMR. (nih.gov)
  • Beta-galactosyltransferase that transfers beta-galactose to hydroxylysine residues of collagen. (nih.gov)
  • Reducible crosslinks in hydroxylysine-deficient collagens of a heritable disorder of connective tissue. (nih.gov)
  • lysine, hydroxylysine, and tryptophan. (medlineplus.gov)
  • A shortage (deficiency) of this enzyme allows lysine, hydroxylysine and tryptophan and their intermediate breakdown products to build up to abnormal levels, especially at times when the body is under stress. (medlineplus.gov)
  • The intermediate breakdown products resulting from incomplete processing of lysine, hydroxylysine, and tryptophan can damage the brain, particularly the basal ganglia, causing the signs and symptoms of glutaric acidemia type I. (medlineplus.gov)
  • Glutaric acidemia type I is an inherited disorder characterized by inadequate levels of an enzyme that helps break down the amino acids lysine, hydroxylysine, and tryptophan. (nih.gov)
  • GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. (nih.gov)
  • GA-1 is an autosomal recessive disorder caused by deficiency of glutaryl-CoA dehydrogenase, a mitochon- drial enzyme involved in the metabolism of lysine, hydroxylysine and tryptophan. (who.int)
  • Hydroxylysine (Hyl) is an amino acid with the molecular formula C6H14N2O3. (wikipedia.org)
  • Jointace Collagen provides a high-grade collagen which is hydrolysed to improve absorption and unlike some sources of collagen it contains high levels of the key amino acid hydroxylysine. (vitabiotics.com)
  • This relative decrease in hydroxylysine was not caused by cytotoxicity or changes in total collagen content, which were found to remain constant as measured by Alamar Blue metabolism and Sircol dye binding assays. (nih.gov)
  • Hydroxylysine" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (umassmed.edu)
  • A protein modification that effectively converts an L-lysine residue to O5-glucosylgalactosyl-L-hydroxylysine. (reactome.org)
  • This graph shows the total number of publications written about "Hydroxylysine" by people in this website by year, and whether "Hydroxylysine" was a major or minor topic of these publications. (umassmed.edu)