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  Encyclopedia of Keywords > Aspartic > Asparagine   Michael Charnine

Keywords and Sections
CIRCULATING ASPARAGINE
AMIDATION
CARBOXAMIDE GROUP
ASPARAGINE RESIDUE
ASPARAGINE SYNTHETASE
SURFACE
TRANSFORMATION
PLACE
ESSENTIAL
ABILITY
NAME
EQUILIBRIUM
CONVERSION
EXPRESSION
BRAIN
CENTRAL NERVOUS SYSTEM
POLYPEPTIDE CHAIN
POLYSACCHARIDES
HIGH CONCENTRATIONS
CAPSID
SEQUENCE
MUTATED
PRODUCTION
DEPLETION
FORMATION
ACRYLAMIDE
AMINO ACIDS
REDUCING SUGARS
TRANSAMINATION
ASX
ADDITION
AMIDE GROUP
AMIDE
ASPARAGINASE
AMMONIA
ASPARAGUS
LEUCINE
CELLS
PROTEINS
NON-ESSENTIAL AMINO
HISTIDINE
ARGININE
RESIDUES
ASN
GLUTAMIC
THREONINE
Review of Short Phrases and Links

    This Review contains major "Asparagine"- related terms, short phrases and links grouped together in the form of Encyclopedia article.

Definitions

  1. Asparagine is an amino acid required by cells for the production of protein. (Web site)
  2. Asparagine is a nonessential amino acid, meaning that it can be synthesized from central metabolic pathyway intermediates in humans.
  3. Asparagine is a nonessential amino acid, which means that it is manufactured from other amino acids in the liver. (Web site)
  4. Asparagine is a common site for attachment of carbohydrates in glycoproteins. (Web site)
  5. Asparagine is a fairly significant amino acid, composing an average of 4.4 percent of most proteins. (Web site)

Circulating Asparagine

  1. These leukemic cells depend on circulating asparagine. (Web site)

Amidation

  1. The amino acid asparagine is synthesized from aspartate by an amidation reaction.
  2. A final, therapeutically useful amino acid-related reaction is the amidation of aspartic acid to produce asparagine.

Carboxamide Group

  1. In addition, a side reaction that occurs at the carboxamide group of asparagine (N) is studied. (Web site)

Asparagine Residue

  1. In addition, the two lysine residues and the asparagine residue are exposed to solvent as they ought to be. (Web site)

Asparagine Synthetase

  1. Amino acid control of asparagine synthetase: relation to asparaginase resistance in human leukemia cells.
  2. Asparagine synthetase as a causal, predictive biomarker for L-asparaginase activity in ovarian cancer cells. (Web site)

Surface

  1. Like asparagine, glutamine is almost always found at the protein surface. (Web site)

Transformation

  1. Amino acid transformation and ammonia synthesis are largely dependent on asparagine.

Place

  1. Asparagine It is an amino acid which is located close to the TCA cycle (place of energy generation) together with aspartic acid. (Web site)
  2. Neither asparagine nor glutamine could sustain cell growth in place of the essential His682 side chain.

Essential

  1. Asparagine is not essential to the human diet, since it can be synthesized from aspartic acid. (Web site)

Ability

  1. The ability of AnsR to regulate ansZ expression in response to asparagine availability was examined.

Name

  1. As its name indicates, aspartic acid is the carboxylic acid analog of asparagine.

Equilibrium

  1. The nervous system needs asparagine to maintain the equilibrium, as well as in amino acid transformation. (Web site)

Conversion

  1. Family members that contain this domain catalyse the conversion of aspartate to asparagine. (Web site)

Expression

  1. Expression of the ansAB operon is repressed by AnsR, and the activity of AnsR has been proposed to be regulated by either asparagine or aspartate (26).
  2. Expression of the ornithine decarboxylase gene in response to asparagine in intestinal epithelial cells. (Web site)
  3. The expression of the ansA gene, which encodes the second L -asparaginase, was found to be induced by asparagine. (Web site)

Brain

  1. As it is converted back into aspartic acid, asparagine releases energy that brain and nervous system cells use for metabolism.
  2. Asparagine acid controls metabolic activity in the brain and nerves, and is used in the treatment of damages in these areas.
  3. Asparagine is of therapeutic use in brain and neurological imbalances.

Central Nervous System

  1. In the central nervous system, asparagine is needed to maintain a balance, preventing over nervousness or being overly calm.
  2. Asparagine helps maintain an equilibrium of the central nervous system and has therapeutic properties, but is toxic when used in excess. (Web site)

Polypeptide Chain

  1. For N -linked oligosaccharides, a 14-sugar precursor is first added to the asparagine in the polypeptide chain of the target protein.

Polysaccharides

  1. Also, polysaccharides linked at the amide nitrogen of asparagine in the protein confer stability on some secreted glycoproteins.

High Concentrations

  1. Asparagine acid is found in high concentrations everywhere in the body.

Capsid

  1. Optionally, the capsid protein has asparagine (N) at amino acid position 394, wherein the asparagine (N)includes a glycosylation site. (Web site)

Sequence

  1. The asparagine is in a specific amino acid sequence. (Web site)

Mutated

  1. Alternatively, one or more asparagine (N) residues have been mutated to glutamine (Q). (Web site)
  2. Thus, in one embodiment, the asparagine residue in position 23 of the sequence defined in SEQ ID NO: 2 has been mutated, for example to a threonine residue. (Web site)
  3. In one embodiment, the asparagine residue in position 3 is not mutated. (Web site)

Production

  1. Asparagine synthetase and glutamine synthetase, catalyze the production of asparagine and glutamine from their respective a -amino acids. (Web site)

Depletion

  1. Depletion of asparagine, which results from treatment with the enzyme L-asparaginase, kills the leukemic cells. (Web site)
  2. Normal cells, however, are less affected by the depletion due to their ability to synthesize asparagine. (Web site)

Formation

  1. Glutamine Much as asparagine resembles ASP, Glutamine resembles GLU. Again the carboxyl group has been neutralized by formation of an amide bond. (Web site)

Acrylamide

  1. We find that asparagine, a major amino acid in potatoes and cereals, is a crucial participant in the production of acrylamide by this pathway. (Web site)

Amino Acids

  1. The amino acid mimetic monomers are selected to mimic the side chain of the amino acids asparagine or glutamine. (Web site)
  2. Two amino acids, asparagine and glutamine, have a carboxamide group in them. (Web site)

Reducing Sugars

  1. Acrylamide also is formed as an intermediate in the Maillard reaction between the amino acid asparagine and reducing sugars.

Transamination

  1. Asparagine is very active in converting one amino acid into another (amination and transamination) when the need arises. (Web site)

Asx

  1. Asparagine or aspartic acid B Asx A placeholder when either amino acid may occupy a position.

Addition

  1. In addition, a novel Asn696Ser (asparagine converted to serine in codon 696) substitution was found in one HCM patient. (Web site)
  2. Asparagine also provides key sites for N-linked glycosylation, modification of the protein chain with the addition of carbohydrate chains. (Web site)
  3. In Eukaryotes, most N -linked oligosaccharides begin with addition of a 14-sugar precursor to the asparagine in the polypeptide chain of the target protein.

Amide Group

  1. For asparagine, either product results in the loss of the amide group, hence "deamidation". (Web site)
  2. A 14 residue sugar is first built on a dolichol carrier and then attached to the amide group of an asparagine of a nascent polypeptide chain. (Web site)

Amide

  1. Asparagine is the amide of aspartic acid. (Web site)

Asparaginase

  1. Asparaginase (EC 3.5.1.1) is an enzyme that catalyzes the hydrolysis of asparagine to aspartic acid. (Web site)
  2. Asparagine loses the amino group from its R-group by hydrolysis catalyzed by Asparaginase.
  3. Monitoring of asparaginase activity and asparagine levels in children on different asparaginase preparations.

Ammonia

  1. Asparaginase is also widely distributed within the body, where it converts asparagine into ammonia and aspartate. (Web site)
  2. Accordingly, microbial cells assimilate ammonia via reactions leading to the formation of either glutamate, glutamine, asparagine, or carbamoyl phosphate. (Web site)
  3. It is biosynthesized from ASPARTIC ACID and AMMONIA by asparagine synthetase.

Asparagus

  1. The amino acid asparagine gets its name from asparagus, the asparagus plant being rich in this compound. (Web site)
  2. Asparagine was first discovered in asparagus, which has a high concentration of the amino acid.

Leucine

  1. The analysis of variance result for asparagine + aspartate (Asx), serine (Ser), and leucine (Leu) was P < 0.0001.

Cells

  1. To determine the production of asparagine and other amino acids by MSCs, we cultured 2 × 10 4 cells into 96-well plates.
  2. Depletion or deprivation of asparagine to such cells can be partial or substantially complete, so long as the desired therapeutic benefit is achieved. (Web site)
  3. When cells are grown in the presence of inducing amounts of asparagine, AnsR repression of the ansAB operon is relieved and AnsA is expressed at high levels.

Proteins

  1. On a per-mole basis, asparagine is incorporated into proteins and enzymes at a rate of 4.4 percent with respect to the other amino acids. (Web site)
  2. Asparagine is essential to all living cells for the production of many proteins. (Web site)
  3. Story and Nomenclature of Amino Acids Asparagine is the earliest amino acid to be discovered in proteins as early as 1806.

Non-Essential Amino

  1. Asparagine is a non-essential amino acid that the body can manufacture in the liver.
  2. In mammals, asparagine is a non-essential amino acid, meaning it does not need to be present in the diet.

Histidine

  1. The second, eluting at 400 mM KCl, used histidine and, to a lesser extent, asparagine. (Web site)

Arginine

  1. For example, substitution of valine for leucine, arginine for lysine, or asparagine for glutamine may not cause a change in functionality of the polypeptide. (Web site)
  2. Histidine, leucine, asparagine, and arginine were also functional amino donors but to a lesser extent. (Web site)

Residues

  1. The polypeptide may be glycosylated on asparagine residues with monosaccharides, disaccharides, oligosaccharides, or polysaccharides. (Web site)
  2. Predicting which asparagine residues will be prone to deamidation in a new therapeutic protein can also be difficult.
  3. The asparagine residues, and also one glycine residue in the B domain, which were replaced, are underlined in the figure. (Web site)

Asn

  1. Asparagine (Asn, N) and glutamine (Gln, Q) are the amides of the side chain carboxyl groups of Asp and Glu respectively.
  2. The side-chains of the amino acids asparagine (Asn) and glutamine (Gln) terminate by an amide group. (Web site)

Glutamic

  1. UV absorption) Asparagine and Glutamine are converted to Aspartic acid and Glutamic acid by treatment with acid.

Threonine

  1. For example, d - O - H d +, d - NH 2 d + or d + C=O d - groups in the side chains of serine, threonine, asparagine and glutamine. (Web site)
  2. O-linked glycosylation occurs at the hydroxyl group of threonine or serine and N-linked glycosylation occurs at the amino group of asparagine. (Web site)
  3. Thus, for example, the mutation of an asparagine in position 23 to a threonine is denoted N23T. (Web site)

Categories

  1. Aspartic
  2. Chemistry > Biochemistry > Amino Acids > Glutamine
  3. Aspartate
  4. Amino
  5. Chemistry > Biochemistry > Amino Acids > Serine

Related Keywords

    * Amino * Aspartate * Aspartic * Glutamine * Serine
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  Short phrases about "Asparagine"
  Originally created: February 05, 2007.
  Links checked: April 11, 2013.
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