is threonine a protein

What is threonine (th)?

Threonine or thr or th is also known as thr amino acid. Thr amino acid (essential amino acid) is used in the biosynthesis or biological synthesis of proteins. Also, we know that amino acids are the building blocks of the body utilized to make proteins.

Is threonine polar or nonpolar?

Threonine (symbol Thr or T) is an amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated −NH +. 3 form under biological conditions), a carboxyl group (which is in the deprotonated −COO − form under biological conditions), and a side chain containing a hydroxyl group, making it a polar, ...

Is threonine a chiral amino acid?

Threonine is one of two proteinogenic amino acids with two chiral centers, the other being isoleucine. Threonine can exist in four possible stereoisomers with the following configurations: (2 S ,3 R ), (2 R ,3 S ), (2 S ,3 S) and (2 R ,3 R ).

Where is threonine found in a protein?

Role in structure: Being a fairly indifferent amino acid, Threonine can reside both within the interior of a protein, or on the protein surface. Threonine has an additional property that is frequently overlooked.

What type of amino acid is threonine?

Threonine, an essential amino acid, is a hydrophilic molecule. Threonine is an other hydroxyl-containing amino acid. It differs from serine by having a methyl substituent in place of one of the hydrogens on the β carbon and it differs from valine by replacement of a methyl substituent with a hydroxyl group.

What is threonine known for?

L-Threonine is an essential amino acid that helps to maintain the proper protein balance in the body. It is important for the formation of collagen, elastin, and tooth enamel, and aids liver and lipotropic function when combined with aspartic acid and methionine.

Is threonine a vitamin?

Threonine is an essential amino acid. Amino acids are the building blocks the body uses to make proteins. The "essential" amino acids are those that cannot be made by the body and must be obtained from the diet.

What is threonine made from?

In plants and microorganisms, threonine is synthesized from aspartic acid via α-aspartyl-semialdehyde and homoserine. Homoserine undergoes O-phosphorylation; this phosphate ester undergoes hydrolysis concomitant with relocation of the OH group.

What functional group is threonine?

hydroxyl groupIt contains an α-amino group (which is in the protonated −NH+3 form under biological conditions), a carboxyl group (which is in the deprotonated −COO− form under biological conditions), and a side chain containing a hydroxyl group, making it a polar, uncharged amino acid.

Why is threonine important to the body?

Threonine, pronounced three-uh-neen is one of nine essential amino acids your body needs to function properly. Aiding in maintaining healthy skin, teeth, collagen, elastin, and muscle tissue, it also helps with digestion, metabolism and preventing fat buildup in the liver.

How do you get threonine?

Animal sources of threonine include lean beef, lamb, pork, collagen, gelatin, cheese. For every 100g of lean beef or lamb there's about 165% of your recommended dietary intake. Plant based sources include tofu, sunflower seeds, flaxseeds, wheat germ, cashews, almonds, lentils, and pistachios.

Is threonine essential amino acid?

Essential amino acids cannot be made by the body. As a result, they must come from food. The 9 essential amino acids are: histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine.

Where is threonine found in the body?

Threonine helps keep connective tissues and muscles throughout the body strong and elastic, including the heart, where it is found in significant amounts. It also helps build strong bones and tooth enamel, and may speed wound healing or recovery from injury.

What causes threonine deficiency?

Deficiency Symptoms and Causes Threonine deficiency is rare, as most people get enough of the amino acid in the foods they eat. However, people with an unbalanced diet, vegans and vegetarians, may not consume enough threonine foods, which can cause low levels of the amino acid.

What causes high threonine?

High levels of Threonine can be due to excessive dietary intake or possible insufficient metabolism of threonine. The initial step requires B6, and zinc is needed to phosphorylate B6 to its active coenzyme form. So supplementation with B6 and zinc can be helpful.

Is threonine Glucogenic or ketogenic?

Threonine is both ketogenic and glucogenic because of acetaldehyde/acetyl CoA formation.

Is threonine an essential amino acid?

Essential amino acids cannot be made by the body. As a result, they must come from food. The 9 essential amino acids are: histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine.

Which amino acids are aromatic?

Tyrosine, phenylalanine and tryptophan are the three aromatic amino acids (AAA) involved in protein synthesis.

What type of amino acid is serine?

Serine is generally classified as a nutritionally nonessential (dispensable) amino acid, but metabolically, serine is indispensible and plays an essential role in several cellular processes. Serine is the major source of one-carbon units for methylation reactions that occur via the generation of S-adenosylmethionine.

Q1: Explain the Two Best Threonine-Rich Foods.

Ans: the two threonine-rich foods are:TurkeyA chunk of protein-rich meat, for example, turkey has known to enough enhancement the body with threoni...

Q2: Explain the Role of Threonine on the Digestive System.

Ans: Threonine assumes a significant part in improving generally stomach related soundness of a person. It is related to delivering mucous gel laye...

Q3: List the Threonine Deficiency Disorders.

Ans: The deficiency of threonine must be treated with consuming a proper diet otherwise it may become very fatal and cause the following health iss...

When was threonine discovered?

Threonine was the last of the 20 common proteinogenic amino acids to be discovered. It was discovered in 1936 by William Cumming Rose, collaborating with Curtis Meyer. The amino acid was named threonine because it was similar in structure to threonic acid, a four-carbon monosaccharide with molecular formula C 4 H 8 O 5.

How much threonine is needed for human body?

Adult humans require about 20 mg/kg body weight/day. In plants and microorganisms, threonine is synthesized from aspartic acid via α-aspartyl-semialdehyde and homoserine. Homoserine undergoes O -phosphorylation; this phosphate ester undergoes hydrolysis concomitant with relocation of the OH group.

How many potential coordination sites does phosphothreonine have?

Phosphothreonine has three potential coordination sites (carboxyl, amine and phosphate group) and determination of the mode of coordination between phosphorylated ligands and metal ions occurring in an organism is important to explain the function of the phosphothreonine in biological processes.

What is the role of threonine in the biosynthesis of cobalamin?

Threonine is used to synthesize glycine during the endogenous production of L-carnitine in the brain and liver of rats.

What are the most common small motifs formed by interactions with serine?

Threonine sidechains are often hydrogen bonded; the most common small motifs formed are based on interactions with serine: ST turns, ST motifs (often at the beginning of alpha helices) and ST staples (usually at the middle of alpha helices).

Is threonine a stereoisomer?

Stereoisomers. Threonine is one of two proteinogenic amino acids with two stereogenic centers, the other being isoleucine. Threonine can exist in four possible stereoisomers with the following configurations: (2 S ,3 R ), (2 R ,3 S ), (2 S ,3 S) and (2 R ,3 R ). However, the name L -threonine is used for one single stereoisomer, ...

Is threonine a posttranslational modification?

The threonine residue is susceptible to numerous posttranslational modifications. The hydroxyl side-chain can undergo O -linked glycosylation. In addition, threonine residues undergo phosphorylation through the action of a threonine kinase. In its phosphorylated form, it can be referred to as phosphothreonine. Phosphothreonine has three potential coordination sites (carboxyl, amine and phosphate group) and determination of the mode of coordination between phosphorylated ligands and metal ions occurring in an organism is important to explain the function of the phosphothreonine in biological processes.

What is Threonine?

Threonine fills in as the sole source of carbon and nitrogen for the development of a wide assortment of creatures.

Why is threonine named threonine?

Threonine amino acid was named threonine because it familiarizes with the structure of threonic acid. A threonic acid is a four-carbon monosaccharide with a molecular formula of C4H8O5.

What is the amino acid that makes up elastin?

Threonine is a fundamental amino acid in people (given by food), Threonine is a significant buildup of numerous proteins, for example, tooth veneer, collagen, and elastin.

What is the amino acid that is used in the biosynthesis of proteins?

Threonine is an amino acid that we use in the biosynthesis of proteins. It involves an α-amino group (a protonated − NH3+ structure under organic conditions), a carboxyl group (a deprotonated − COO− form under biological conditions), and a side chain containing a hydroxyl group (OH), making it a polar, uncharged amino acid.

How does threonine work?

Threonine works the accompanying way: it consolidates with aspartic corrosive and Methionine to together assistance liver summary fats and unsaturated fats. This cycle decreases the amassing of fat in the liver, which would some way or another influence the liver capacity.

Why is threonine important?

Threonine is considered a significant fundamental amino acid, which is needed for advancing the general wellbeing status of the central nervous system. It additionally assists with improving the movement of the cerebrum.

What is the role of threonine in the body?

Threonine amino acid is an essential amino acid that plays a significant role in regulating protein balance in the human body. Also, it a little-known amino acid, but plays a major role in the immune system. In general, our body cannot synthesize an essential threonine directly, so we obtain it from dietary sources.

What is threonine used for?

Threonine is an essential amino acid. Amino acids are the building blocks the body uses to make proteins. The "essential" amino acids are those that cannot be made by the body and must be obtained from the diet. People use threonine for conditions such as a muscle control disorder marked by involuntary movements and muscle tightness ( spasticity ), ...

How long can you take threonine?

Doses of up to 4 grams of threonine daily have been used safely for up to 12 months. Some people experience minor side effects such as stomach upset, headache, nausea, and skin rash. Special Precautions and Warnings.

Is threonine safe to take?

Side Effects. When taken by mouth: Threonine is LIKELY SAFE when used in food amounts. It's been proposed that people need to get about 0.5 to 1 gram of threonine from their diet per day. This amount is considered to be safe. Threonine is POSSIBLY SAFE when used as a medicine.

Does NMDA interact with threonine?

Medications used for Alzheimer's disease (NMDA antagonists) interacts with THREONINE. There is some concern that threonine might decrease how well a medication used for Alzheimer's disease works. This medication is called memantine (Namenda). Dosing.

Is threonine safe for pregnant women?

Pregnancy and breast -feeding : There isn't enough reliable information to know if threonine is safe to use when pregnant or breast-feeding. Stay on the safe side and avoid use. Amyotrophic lateral sclerosis (Lou Gehrig's disease) :There is some concern that threonine might decrease lung function in patients with ALS.

What is threonine?

Threonine is an essential amino acid. It is important for regulating protein balance in the body. This amino acid is a precursor to serine and glycine. These are two other amino acids necessary for muscle tissue production. L-threonine has many uses in the body. It supports:

What is the role of threonine in the body?

In summary, threonine is an important essential amino acid. It has a range of roles in the human body. It helps to support the immune system and healthy digestion. This amino acid is also essential for tissue development and maintenance. Therefore, it plays a key role in heart and liver health.

What amino acid protects the digestive tract?

Here this amino acid protects the digestive tract. Threonine is needed to produce the mucus gel layer that covers the digestive tract. This mucus is a barrier to digestive enzymes that can damage the intestines. Threonine is also used in other endogenous secretions.

What are the symptoms of threonine deficiency?

Symptoms of threonine deficiency. Common symptoms of threonine deficiency include digestive difficulties, emotional agitation, confusion and a fatty liver. This amino acid is usually abundant in a balanced diet. Consequently, deficiencies are rare. However, vegans and strict vegetarians may want to consider a supplement.

Why is threonine important for the immune system?

Ensuring that the body has enough threonine to support immune function is important to safeguard against a host of diseases.

What amino acids are involved in the liver?

Threonine works together with the amino acids methionine and aspartic acid to support the liver. These amino acids help to facilitate lipotropic function. In this process the body digests fats. Therefore in the absence of sufficient threonine the liver would become overwhelmed by fats.

What foods contain threonine?

Nuts, beans, seeds and other vegetables also contain threonine but in lower concentrations. Adults need approximately 15mg of this amino acid per kilogram of body weight daily for optimal functioning 9.

Why is threonine important?

It is important for the formation of collagen, elastin, and tooth enamel, and aids liver and lipotropic function when combined with aspartic acid and methionine. Threonine is an essential amino acid in humans (provided by food), Threonine is an important residue of many proteins, such as tooth enamel, collagen, and elastin.

What is threonine used for?

Useful with intestinal disorders and indigestion, threonine has also been used to alleviate anxiety and mild depression.

How many people were exposed to threonine in 1981?

NIOSH (NOES Survey 1981-1983) has statistically estimated that 18,524 workers (13,980 of these were female) were potentially exposed to threonine in the US (1).

How much threonine is in infant formula?

The threonine content of most of the infant formulas currently on the market is approximately 20% higher than the threonine concentration in human milk. Due to this high threonine content the plasma threonine concentrations are up to twice as high in premature infants fed these formulas than in infants fed human milk. To study the effect of different threonine intakes on plasma and tissue amino acid concentrations, 24 young male Wistar rats were fed three experimental diets based on a mixture of bovine proteins with a whey protein/casein ratio of 60/40 with different threonine contents [group A, 0.86 g of threonine/100 g (n = 8); group B, 1.03 g of threonine/100 g (n = 8); group C, 2.21 g of threonine/100 g (n = 8)]. Eight animals were fed a typical rat diet based on bovine casein as controls. After a feeding period of 15 d, amino acids were measured in plasma and in homogenates of the cerebral cortex, brain stem, liver, and muscle. There was a significant correlation between threonine intake and plasma threonine levels (r = 0.687, p < 0.001). The plasma threonine concentration correlated significantly with the threonine concentration in the cortex (r = 0.821, p < 0.01) and the brain stem (r = 0.882, p < 0.01). There was a positive significant correlation between threonine and glycine concentrations in the cortex (r = 0.673, p < 0.01), and the brain stem (r = 0.575, p < 0.01), whereas the glycine concentration decreased with increasing threonine intakes in the liver and muscle. The presented data indicate that increasing the threonine in plasma leads to increasing brain glycine and thereby affects the neurotransmitter balance in the brain. This may have consequences for brain development during early postnatal life. Therefore, excessive threonine intake during infant feeding should be avoided.

What is the excess threonine converted to?

The evidence indicates that excess threonine is converted to carbohydrate, liver lipids, and carbon dioxide.

What is the role of L-threonine?

l-Threonine. More... L-threonine is an optically active form of threonine having L-configuration. It has a role as a nutraceutical, a micronutrient, a Saccharomyces cerevisiae metabolite, a plant metabolite, an Escherichia coli metabolite , a human metabolite, an algal metabolite and a mouse metabolite. It is an aspartate family amino acid, ...

What is L-tetrahedronine?

L-Threonine makes up collagen, elastin, and enamel protein. It aids proper fat metabolism in the liver, helps the digestive and intestinal tracts function more smoothly, and assists in metabolism and assimilation.

What is the name of the enzyme that phosphorylates the OH group of serine or threon?

A serine/threonine protein kinase ( EC 2.7.11.-) is a kinase enzyme that phosphorylates the OH group of serine or threonine (which have similar sidechains). At least 125 of the 500+ human protein kinases are serine/threonine kinases (STK). In enzymology, the term serine/threonine protein kinase describes a class of enzymes in the family ...

What are the functions of mitogens in the cell?

respond to extracellular stimuli (mitogens) and regulate various cellular activities, such as gene expression, mitosis, differentiation, and cell survival/apoptosis.

What is the process of phosphorylation of serine kinase?

In enzymology, the term serine/threonine protein kinase describes a class of enzymes in the family of transferases, that transfer phosphates to the oxygen atom of a serine or threonine sidechain in proteins. This process is called phosphorylation. Protein phosphorylation in particular plays a significant role in a wide range ...

What is the V-Akt gene?

The v-akt gene was identified as the oncogene of retrovirus AKT8. The gene codes for a protein kinase. Human homologs of the AKT8 oncogenic protein were identified in 1987.By 1995 it had been found that Akt kinases function as mitogen-activated kinases downstream from cell surface receptors that activate phosphoinositide 3-kinase. Three human akt genes exist. All three Akt kinases regulate cell proliferation and Akt2 is particularly important for insulin actions in cells. A major target of Akt kinases is glycogen synthase kinase-3 .

Which kinase regulates cell proliferation?

All three Akt kinases regulate cell proliferation and Akt2 is particularly important for insulin actions in cells. A major target of Akt kinases is glycogen synthase kinase-3 . EC 2.7.1.37. Pelle. is a serine/threonine kinase that can phosphorylate itself, and also Tube and Toll.

What is the EC number of a serine kinase?

Many serine/threonine protein kinases do not have their own individual EC numbers and use "2.7.11.1". These were formerly included in EC number " 2.7.1.37", which was a general EC number for any enzyme that phosphorylates proteins while converting ATP to ADP (i.e., ATP:protein phosphotransferases.)

Do kinases phosphorylate serine?

While serine/threonine kinases all phosphorylate serine or threonine residues in their substrates, they select specific residues to phosphorylate on the basis of residues that flank the phosphoacceptor site, which together comprise the consensus sequence. Since the consensus sequence residues of a target substrate only make contact with several key amino acids within the catalytic cleft of the kinase (usually through hydrophobic forces and ionic bonds ), a kinase is usually not specific to a single substrate, but instead can phosphorylate a whole "substrate family" which share common recognition sequences. While the catalytic domain of these kinases is highly conserved, the sequence variation that is observed in the kinome (the subset of genes in the genome that encode kinases) provides for recognition of distinct substrates. Most kinases are inhibited by a pseudosubstrate that binds to the kinase like a real substrate but lacks the amino acid to be phosphorylated. When the pseudosubstrate is removed, the kinase can perform its normal function.

Which hormone binds to a thyroid receptor?

Fig. 3. Nongenomic regulation of CPT by thyroid hormone. Thyroid hormone binds to a thyroid hormone receptor, which may initiate one or both signaling pathways to disinhibit CPT1. Both the AMPK and the PI3K/Akt signaling cascades have been implicated in the T3-mediated increase in CPT1 activity.

Which protein kinases have domains that interact with other proteins?

Forty-six protein kinases have domains that interact with other proteins such as SH3, 55 tyrosine and serine kinases have lipid interaction domains such as PH, 38 have domains linked to small GTPase signaling, and 28 serine kinases have domains linked to calcium signaling.

What are the mitogen-activated protein kinases?

The mitogen-activated protein kinases (MAPKs) are a group of serine/threonine-specific protein kinases regulating gene expression, mitosis, proliferation, differentiation, cell survival, and death in response to a wild array of stimuli-including mitogens, osmotic stress, HS, and pro-inflammatory cytokines (Pearson et al., 2001 ). It has been shown that numerous members of the MAPK superfamily phosphorylate Tau at several SP/TP sites in vitro ( Shulman and Feany, 2003; Augustinack et al., 2002 ). One of the characterized candidates from the cell stress response pathway, the c-jun N-terminal kinase (JNK), has been reported in regulating Tau phosphorylation ( Goedert et al., 1997; Reynolds et al., 2000; Zhu et al., 2000, 2001 ). In the Drosophila tauopathy model, overexpression of hTau V337M and a stress-activated kinase, Hemipterous (Hep), the Drosophila homolog of JNK kinase, exacerbates hTau-induced rough eye phenotype ( Shulman and Feany, 2003 ). In addition, it has been implicated that this synergistic interaction between Hep/JNK and hTau toxicity is mediated via hTau phosphorylation ( Steinhilb et al., 2007b ). A recent study using mouse and Drosophila models has shown that reducing axonal transport activates the JNK pathway, increases hTau hyperphosphorylation, and aggravates hTau-mediated neurotoxicity ( Falzone et al., 2010 ). However, it has also been shown that oxidative stress plays a causal role in hTau-induced neurotoxiciy via the activation of the JNK signaling pathway. In this model, oxidative stress acts to enhance hTau-induced cell cycle activation, not to promote hTau phosphorylation ( Dias-Santagata et al., 2007 ). In addition to the JNK pathway, other members of the MAPK pathway have recently been identified as novel modifiers of hTau-induced neurotoxicity in a genetic screen ( Ambegaokar and Jackson, 2011 ).

What is the catalytic domain of protein kinases?

The catalytic domains of eukaryotic serine/threonine- and tyrosine-specific protein kinases are related in sequence, and belong to the eukaryotic protein kinase (ePK) superfamily, which in turn is a subset of protein-kinase like (PKL) kinases that share a common fold and catalytic mechanism. The major control functions of protein kinases are reflected in their involvement in disease. Thirty-five percent of the kinome (175 genes) has been directly implicated in human disease, through mutation, mis-expression, or copy number changes, and 121 protein kinases are implicated in cancer, including 51 of the 90 tyrosine kinases. Many more protein kinases are weakly implicated and are emerging from genome-scale studies, including recent efforts to re-sequence the entire kinome in a wide variety of human cancers to derive driver mutations involved in carcinogenesis. Protein kinase catalytic function is often dependent on additional domains in the protein, which regulate activity, localize, and recruit regulatory proteins/second messengers and substrates. About half the protein kinases are predicted to have additional domains, many of which are implicated in signaling. Of the tyrosine kinases, 25 have P.Tyr binding SH2 domains that play a cardinal role in establishing tyrosine-phosphorylation based signaling networks. Forty-six protein kinases have domains that interact with other proteins such as SH3, 55 tyrosine and serine kinases have lipid interaction domains such as PH, 38 have domains linked to small GTPase signaling, and 28 serine kinases have domains linked to calcium signaling. Most members of a protein kinase family have the same set of ancillary domains, but there are some exceptions, and alternative splicing is often used to generate distinct domain combinations from a single gene.

What is the function of protein kinase?

Protein kinase catalytic function is often dependent on additional domains in the protein, which regulate activity, localize, and recruit regulatory proteins/second messengers and substrates. About half the protein kinases are predicted to have additional domains, many of which are implicated in signaling.

Which kinases are intracellular?

The serine–threonine kinases are almost all intracellular and include key mediators of carcinogenesis such as raf, Akt/protein kinase B, and MEK.

Do protein kinases have the same domains?

Most members of a protein kinase family have the same set of ancillary domains, but there are some exceptions, and alternative splicing is often used to generate distinct domain combinations from a single gene. View chapter Purchase book. Read full chapter.

Overview

Modifications

History

Stereoisomers

Biosynthesis

Metabolism

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