Chapter 17 - Amino Acid Metabolism
... Maple syrup urine disease - the disorder of the oxidative decarboxylation of -ketoacids derived from valine, isoleucine, and leucine caused by the missing or defect of branched-chain dehydrogenase. The levels of branched-chain amino acids and corresponding -ketoacids are markedly elevated in both ...
... Maple syrup urine disease - the disorder of the oxidative decarboxylation of -ketoacids derived from valine, isoleucine, and leucine caused by the missing or defect of branched-chain dehydrogenase. The levels of branched-chain amino acids and corresponding -ketoacids are markedly elevated in both ...
Proteins
... Another major compound of living things is protein. Proteins make up the bulk of all solid material within your body and other living organisms. Proteins are the most structurally sophisticated molecules known. They vary extensively in structure with each type of protein having a unique three-dimens ...
... Another major compound of living things is protein. Proteins make up the bulk of all solid material within your body and other living organisms. Proteins are the most structurally sophisticated molecules known. They vary extensively in structure with each type of protein having a unique three-dimens ...
Review - Columbus Labs
... pKa Values of the Amino Acid Side Chains • Arginine, Arg, R: pKa(guanidino group) = 12.5 • Lysine, Lys, K: pKa = 10.5 ...
... pKa Values of the Amino Acid Side Chains • Arginine, Arg, R: pKa(guanidino group) = 12.5 • Lysine, Lys, K: pKa = 10.5 ...
Amino Acids
... hydrophobicity. The side chain of proline and its α-amino group form a ring structure. Proline gives the fibrous structure of collagen, and interrupts the α-helices found in globular proteins. ...
... hydrophobicity. The side chain of proline and its α-amino group form a ring structure. Proline gives the fibrous structure of collagen, and interrupts the α-helices found in globular proteins. ...
Chapter 4: Amino Acids General Features of Amino Acids
... • D-amino acids in peptides and proteins (excluding proline) consist of a carboxylic acid (-COOH) and an amino (-NH2) functional group attached to the same tetrahedral carbon atom. • Distinct R-groups, that distinguish one amino acid from another, also are attached to the alpha-carbon (except in the ...
... • D-amino acids in peptides and proteins (excluding proline) consist of a carboxylic acid (-COOH) and an amino (-NH2) functional group attached to the same tetrahedral carbon atom. • Distinct R-groups, that distinguish one amino acid from another, also are attached to the alpha-carbon (except in the ...
Amino acid lecture(1) by Prof.Dr.Moaed Al
... The metabolism of amino acids will be described in the following sequence: 1 The most simple AA that give pyruvate – Ala, Ser, Gly, Thr 2 Amino acids containing sulfur – Met, Cys 3 Sources of one-carbon units and use of those units in syntheses 4 Aspartic acid 5 Glutamic acid and its relation to Arg ...
... The metabolism of amino acids will be described in the following sequence: 1 The most simple AA that give pyruvate – Ala, Ser, Gly, Thr 2 Amino acids containing sulfur – Met, Cys 3 Sources of one-carbon units and use of those units in syntheses 4 Aspartic acid 5 Glutamic acid and its relation to Arg ...
Dan`s poster - The University of Sheffield
... Nitrogen, a key resource for plants, is required for the synthesis of proteins and many other important types of molecule. Amino acids are the major ‘nitrogen currency’ of plants, being translocated between different cells and to different organs in response to the needs of the plant. This places gr ...
... Nitrogen, a key resource for plants, is required for the synthesis of proteins and many other important types of molecule. Amino acids are the major ‘nitrogen currency’ of plants, being translocated between different cells and to different organs in response to the needs of the plant. This places gr ...
Prezentace aplikace PowerPoint
... A serious disease results from the inability to oxidize phenylalanine by a defective phenylalanine hydroxylase. This results in high levels of phenylpyruvate developing (phenylpyruvate is the result of transamination of phenylalanine with an amino acid). The disease is phenylketonuria (PKU), and res ...
... A serious disease results from the inability to oxidize phenylalanine by a defective phenylalanine hydroxylase. This results in high levels of phenylpyruvate developing (phenylpyruvate is the result of transamination of phenylalanine with an amino acid). The disease is phenylketonuria (PKU), and res ...
Dionex AminoPac Columns for the Analysis of Amino Acids
... Proteins and peptides are large macromolecules consisting of covalently bonded amino acids. Proteins commonly exist as folded structures, while peptides are shorter linear polymers consisting of only a few amino acids. Amino acid analysis refers to the methodology used to determine the individual am ...
... Proteins and peptides are large macromolecules consisting of covalently bonded amino acids. Proteins commonly exist as folded structures, while peptides are shorter linear polymers consisting of only a few amino acids. Amino acid analysis refers to the methodology used to determine the individual am ...
Proteins
... Amino Acids They are classified as , , , etc. amino acids according the carbon that bears the nitrogen. ...
... Amino Acids They are classified as , , , etc. amino acids according the carbon that bears the nitrogen. ...
Session #31: homework Solution
... The structure of cysteine at pH = 7 shows that the side group is protonated. So we must conclude that even though the pKa is 8.33, the sulfhydryl (−SH) is acting as an acid. The isoelectric point, pI, is the pH at which the zwitterion is the dominant species. Let’s start with extreme acid conditions ...
... The structure of cysteine at pH = 7 shows that the side group is protonated. So we must conclude that even though the pKa is 8.33, the sulfhydryl (−SH) is acting as an acid. The isoelectric point, pI, is the pH at which the zwitterion is the dominant species. Let’s start with extreme acid conditions ...
2- All essential amino acids are glucogenic. False
... 1- An increase in gluconeogenesis from amino acids results in a decrease in urea formation. False An increase in the availability of gluconeogenic amino acids from the catabolism of body protein is associated with increased ammonia and results in increased urea production. ...
... 1- An increase in gluconeogenesis from amino acids results in a decrease in urea formation. False An increase in the availability of gluconeogenic amino acids from the catabolism of body protein is associated with increased ammonia and results in increased urea production. ...
Biosynthesis of the nutritionally nonessential amino acids
... hydroxylase of skin, skeletal muscle, and granulating wounds. But only after these amino acids have been incorporated into peptides. Requires: substrate, molecular O2, ascorbate, Fe2+, and α ketoglutarate . One atom of O2 is incorporated into proline or lysine, the other into succinate. A deficiency ...
... hydroxylase of skin, skeletal muscle, and granulating wounds. But only after these amino acids have been incorporated into peptides. Requires: substrate, molecular O2, ascorbate, Fe2+, and α ketoglutarate . One atom of O2 is incorporated into proline or lysine, the other into succinate. A deficiency ...
Protein structure - Manning`s Science
... The monomers that join together to make the polymer are the amino acids. Proteins are known as polypeptides because the bonds that join the amino acids together are called PEPTIDE bonds. ...
... The monomers that join together to make the polymer are the amino acids. Proteins are known as polypeptides because the bonds that join the amino acids together are called PEPTIDE bonds. ...
Lh6Ch18AAOxid
... carbamoyl phosphate and passed into the urea cycle 4. Amino acids are degraded to pyruvate, acetyl-CoA, αketoglutarate, succinyl-CoA, and/or oxaloacetate 5. Amino acids yielding acetyl-CoA are ketogenic. 6. Amino acids yielding other end products are glucogenic. 7. Genetic defects in amino degradati ...
... carbamoyl phosphate and passed into the urea cycle 4. Amino acids are degraded to pyruvate, acetyl-CoA, αketoglutarate, succinyl-CoA, and/or oxaloacetate 5. Amino acids yielding acetyl-CoA are ketogenic. 6. Amino acids yielding other end products are glucogenic. 7. Genetic defects in amino degradati ...
Amino acid
Amino acids (/əˈmiːnoʊ, ˈæmənoʊ, əˈmaɪnoʊ/) are biologically important organic compounds containing amine (-NH2) and carboxylic acid (-COOH) functional groups, usually along with a side-chain specific to each amino acid. The key elements of an amino acid are carbon, hydrogen, oxygen, and nitrogen, though other elements are found in the side-chains of certain amino acids. About 500 amino acids are known and can be classified in many ways. They can be classified according to the core structural functional groups' locations as alpha- (α-), beta- (β-), gamma- (γ-) or delta- (δ-) amino acids; other categories relate to polarity, pH level, and side-chain group type (aliphatic, acyclic, aromatic, containing hydroxyl or sulfur, etc.). In the form of proteins, amino acids comprise the second-largest component (water is the largest) of human muscles, cells and other tissues. Outside proteins, amino acids perform critical roles in processes such as neurotransmitter transport and biosynthesis.In biochemistry, amino acids having both the amine and the carboxylic acid groups attached to the first (alpha-) carbon atom have particular importance. They are known as 2-, alpha-, or α-amino acids (generic formula H2NCHRCOOH in most cases, where R is an organic substituent known as a ""side-chain""); often the term ""amino acid"" is used to refer specifically to these. They include the 22 proteinogenic (""protein-building"") amino acids, which combine into peptide chains (""polypeptides"") to form the building-blocks of a vast array of proteins. These are all L-stereoisomers (""left-handed"" isomers), although a few D-amino acids (""right-handed"") occur in bacterial envelopes and some antibiotics. Twenty of the proteinogenic amino acids are encoded directly by triplet codons in the genetic code and are known as ""standard"" amino acids. The other three (""non-standard"" or ""non-canonical"") are selenocysteine (present in many noneukaryotes as well as most eukaryotes, but not coded directly by DNA), pyrrolysine (found only in some archea and one bacterium) and N-formylmethionine (which is often the initial amino acid of proteins in bacteria, mitochondria, and chloroplasts). Pyrrolysine and selenocysteine are encoded via variant codons; for example, selenocysteine is encoded by stop codon and SECIS element. Codon–tRNA combinations not found in nature can also be used to ""expand"" the genetic code and create novel proteins known as alloproteins incorporating non-proteinogenic amino acids.Many important proteinogenic and non-proteinogenic amino acids also play critical non-protein roles within the body. For example, in the human brain, glutamate (standard glutamic acid) and gamma-amino-butyric acid (""GABA"", non-standard gamma-amino acid) are, respectively, the main excitatory and inhibitory neurotransmitters; hydroxyproline (a major component of the connective tissue collagen) is synthesised from proline; the standard amino acid glycine is used to synthesise porphyrins used in red blood cells; and the non-standard carnitine is used in lipid transport.Nine proteinogenic amino acids are called ""essential"" for humans because they cannot be created from other compounds by the human body and, so, must be taken in as food. Others may be conditionally essential for certain ages or medical conditions. Essential amino acids may also differ between species.Because of their biological significance, amino acids are important in nutrition and are commonly used in nutritional supplements, fertilizers, and food technology. Industrial uses include the production of drugs, biodegradable plastics, and chiral catalysts.