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Amino acids nonstandard

The vast majority of research focused on selenium in biology (primarily in the fields of molecular biology, cell biology, and biochemistry) over the past 20 years has centered on identification and characterization of specific selenoproteins, or proteins that contain selenium in the form of selenocysteine. In addition, studies to determine the unique machinery necessary for incorporation of a nonstandard amino acid (L-selenocysteine) during translation also have been central to our understanding of how cells can utilize this metalloid. This process has been studied in bacterial models (primarily Escherichia colt) and more recently in mammals in vitro cell culture and animal models). In this work, we will review the biosynthesis of selenoproteins in bacterial systems, and only briefly review what is currently known about parallel pathways in mammals, since a comprehensive review in this area has been recently published. Moreover, we summarize the global picture of the nonspecific and specific use of selenium from a broader perspective, one that includes lesser known pathways for selenium utilization into modified nucleosides in tRNA and a labile selenium cofactor. We also review recent research on newly identified mammalian selenoproteins and discuss their role in mammalian cell biology. [Pg.122]

The second reaction also occurs in the mitochondria and involves the transfer of the carbamoyl group from carbamoyl phosphate to ornithine by ornithine transcarbamoylase. This reaction forms another nonstandard amino acid citrulline which then has to be transported out of the mitochondrion into the cytosol where the remaining reactions of the cycle take place. [Pg.381]

It is not clear whether alterative nucleotides and amino acids were available prebiotically. Studies of the Murchison meteorite (see Chapter 5) have revealed a large number of nonstandard amino acids many are accepted by terran machinery. It is clear that advanced organisms, such as those found in modem life, are fully capable of synthesizing extra nucleotides for RNA and DNA and extra amino acids for proteins. [Pg.63]

Ornithine (C) is a nonstandard amino acid that occurs in metabolic processes. Which amino acid does it most closely resemble Estimate pKa values and p/ for ornithine, and draw the major form present at pH = 2, pH = 6, and pH = 11. If ornithine were a component of proteins, how would it affect the tertiary structure of a protein ... [Pg.748]

No structure is assigned a peptide name unless it contains at least two standard amino acid residues. A standard amino acid residue is any amino acid that can stand alone as a stereoparent (e.g., glycine or tryptophan), plus asparagine and glutamine. 2-Aminobutanoic acid and 2,4-diaminobutanoic acid are now considered nonstandard amino acids. [Pg.93]

The aaRS have enormous potential as tools to incorporate novel amino acids into proteins (15). Modified proteins that contain one or more nonstandard amino acids could confer unique chemical, physical, and/or biologic properties. These custom-designed proteins could be adapted as medicinal therapeutics and as biotechnology tools. [Pg.35]

Nonstandard amino acids can be either incorporated globally at multiple sites within a protein or inserted at specific locations (1, 15). Global misincorporation of nonstandard amino acids can produce protein polymers with altered physical properties that confer, for example, varied tensile strengths and elasticities (16). These unique biomaterials can be used in many medical applications, such as altering properties associated with cell adhesion. In other applications, routine replacement of methionine by selenomethionine aids in X-ray crystal structure determination. [Pg.35]

FIGURE 14 The GTR graph and RTG graph of cyclosporin A. Mbt, Abu, Sar, Ninl, and Nmv are the names of nonstandard amino acids. Data adopted from the paper of Xu, Weber, and Borer. ... [Pg.269]

Figure 2. Chromatographic separation of amino acids after derivatization with phenylisothiocyanate (PITC) A. Separation of 200 picomole standard amino acid mix H containing 18 amino acids. B. Separation of an extended amino acid mix containing 28 amino acids. The standard one-letter abbreviations are used for the usual amino acids. Nonstandard amino acids are Sp, phosphoserine Hp, hydroxyproline Citr, citrulline Tau, taurine aAba, a-amino butyric acid HKl HK2, hyi oxylysines Om, ornithine , artifacts from reagents. Figure 2. Chromatographic separation of amino acids after derivatization with phenylisothiocyanate (PITC) A. Separation of 200 picomole standard amino acid mix H containing 18 amino acids. B. Separation of an extended amino acid mix containing 28 amino acids. The standard one-letter abbreviations are used for the usual amino acids. Nonstandard amino acids are Sp, phosphoserine Hp, hydroxyproline Citr, citrulline Tau, taurine aAba, a-amino butyric acid HKl HK2, hyi oxylysines Om, ornithine , artifacts from reagents.
In addition to the twenty standard amino acids, many nonstandard amino acids are also found in almost all proteins. Generally, these amino acids arise as a consequence of various chemical modifications after they have been incorporated into protein. Posttranslational modification of amino acids is one basis of the regulation of protein activity, specificity, and stability. [Pg.254]

Nonstandard amino acids consist of amino acid residues that have been chemically modified after they have been incorporated into a polypeptide or amino acids that occur in living organisms but are not found in proteins. [Pg.113]

Several standard and nonstandard amino acids act as metabolic intermediates. For example, arginine, citrulline, and ornithine (Figure 5.6) are components of the urea cycle (Chapter 15). The synthesis of urea, a molecule formed in vertebrate livers, is the principal mechanism for the disposal of nitrogenous waste. [Pg.118]

Many amino acids, such as citrulline and ornithine (which are found in the urea cycle), are not building blocks of proteins. Other nonstandard amino acids, such as hydroxyproline, are formed after translation by posttranslational modification. When discussing amino acids and translation, the magic number was always 20. Only 20 standard amino acids were put onto tRNA molecules for protein synthesis. In the late 1980s, another amino acid was found in proteins from eukaryotes and prokaryotes alike, including humans. It is selenocysteine, a cysteine residue in which the sulfur atom has been replaced by a selenium atom. [Pg.348]

Explicit sequences in a PDB hie are provided in lines starting with the keyword SEQRES. Unlike other sequence databases, PDB records use the three-letter amino acid code, and nonstandard amino acids are found in many PDB record sequence entries with arbitrarily chosen three-letter names. Unfortunately, PDB records seem to lack sensible, consistent rules. In the past, some double-helical nucleic acid sequence entries in PDB were specihed in a 3 -to-5 order in an entry above the complementary strand, given in 5 -to-3 order. Although the sequences may be obvious to a user as a representation of a double helix, the 3 -to-5 explicit sequences are nonsense to a computer. Fortunately, the NDB project has hxed many of these types of problems, but the PDB data format is still open to ambiguity disasters from the standpoint of computer readability. As an aside, the most troubling glitch is the inability to encode element type separately from the atom name. Examples of where... [Pg.89]

Hong, S.H., Ntai, I., Haimovich, A.D., Kelleher, N.L. et al. (2014) Cell-free protein synthesis from a release factor 1 deficient Escherichia coli activates efficient and multiple site-specific nonstandard amino acid incorporation. [Pg.817]

The feasibility of incorporating nonstandard amino acids into peptides/ proteins offers valuable options to modulate the functionality and reactivity of the produced molecular structures. Novel amino acids can be introduced in either a residue-specific or site-specific fashion. Integrating these engineered peptides into biomimetic scaffolds facilitates the construction of biomaterials with tunable chemical and mechanical properties. [Pg.217]

For every PDB entry for which the structure was solved by X-ray diffraction, ligands were automatically extracted from the PDB file by identifying distinct molecules of 5-100 non-hydrogen atoms with different chain IDs to the remaining protein sequence, discontinuous residue numbers, or nonstandard amino acid residue IDs. Each putative ligand was converted to a SMILES string by deriving bond information... [Pg.168]

Nonstandard Amino Acids Peptides sometimes contain an amino acid different from the 20 shown in Table 25.1. Dehydroalanine, for example, is a component of a toxic substance produced by a strain of cyanogenic bacteria, and hydroxyproline is a component of the collagen in connective tissue. [Pg.1034]

Like most nonstandard amino acids, dehydroalanine and hydroxyproline are formed by modification of one of the standard amino acids that has already been incorporated into a peptide. Two nonstandard amino acids—selenocysteine and pyrrolysine—Ae so-called twenty-first and twenty-second amino acids, however, are coded for by DNA. [Pg.1034]

The next section deals with amino acid stereochemistry. You can prepare for it by locating all of fhe chirality centers in the four nonstandard amino acids just shown and specifying their configuration using the Cahn-Ingold-Prelc R,S notation. [Pg.1035]

Some nonstandard amino acids are not found in proteins. Examples include lanthionine, 2-aminoisobutyric acid, dehydroalanine and the neurotransmitter gamma-aminobutyric acid. Nonstandard amino acids often occur as intermediates in the metabolic pathways for standard amino acids — for example ornithine and citrulline occur in the urea cycle, part of amino acid catabolism (see below). A rare exception to the dominance of a-amino acids in biology is the P-amino acid beta alanine (3-aminopropanoic acid), which is used in plants and microorganisms in the synthesis of pantothenic acid (vitamin B5), a component of coenzyme A. [Pg.40]

Nonstandard amino acids are usually formed through modifications to standard amino acids. For example, homocysteine is formed through the transsulfuration pathway or by the demethylation of methionine via the intermediate metabolite S-adenosyl methionine, while hydroxyproline is made by a posttranslational modification of proline. [Pg.45]


See other pages where Amino acids nonstandard is mentioned: [Pg.37]    [Pg.42]    [Pg.14]    [Pg.126]    [Pg.360]    [Pg.90]    [Pg.800]    [Pg.90]    [Pg.238]    [Pg.428]   
See also in sourсe #XX -- [ Pg.110 ]




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