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Kanamycin Kinase
Aminoglycoside-3'-phosphotransferase (APH(3')), also known as aminoglycoside kinase, is an enzyme that primarily catalyzes the addition of phosphate from ATP to the 3'-hydroxyl group of a 4,6-disubstituted aminoglycoside, such as kanamycin. However, APH(3') has also been found to phosphorylate at the 5'-hydroxyl group in 4,5-disubstituted aminoglycosides, which lack a 3'-hydroxyl group, and to diphosphorylate hydroxyl groups in aminoglycosides that have both 3'- and 5'-hydroxyl groups. Primarily positively charged at biological conditions, aminoglycosides bind to the negatively charged backbone of nucleic acids to disrupt protein synthesis, effectively inhibiting bacterial cell growth. APH(3') mediated phosphorylation of aminoglycosides effectively disrupts their mechanism of action, introducing a phosphate group that reduces their binding affinity due to steric hindrances and unfavorable electrostatic interactions. APH(3') is primarily found in certain species of gram-positive b ...
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Enzyme
An enzyme () is a protein that acts as a biological catalyst by accelerating chemical reactions. The molecules upon which enzymes may act are called substrate (chemistry), substrates, and the enzyme converts the substrates into different molecules known as product (chemistry), products. Almost all metabolism, metabolic processes in the cell (biology), cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme, pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts include Ribozyme, catalytic RNA molecules, also called ribozymes. They are sometimes descr ...
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Disulfide Bonds
In chemistry, a disulfide (or disulphide in British English) is a compound containing a functional group or the anion. The linkage is also called an SS-bond or sometimes a disulfide bridge and usually derived from two thiol groups. In inorganic chemistry, the anion appears in a few rare minerals, but the functional group has tremendous importance in biochemistry. Disulfide bridges formed between thiol groups in two cysteine residues are an important component of the tertiary and quaternary structure of proteins. Compounds of the form are usually called '' persulfides'' instead. Organic disulfides Structure Disulfides have a C–S–S–C dihedral angle approaching 90°. The S–S bond length is 2.03 Å in diphenyl disulfide, similar to that in elemental sulfur. Disulfides are usually symmetric but they can also be unsymmetric. Symmetrical disulfides are compounds of the formula . Most disulfides encountered in organosulfur chemistry are symmetrical disulfides. ...
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Magnesium
Magnesium is a chemical element; it has Symbol (chemistry), symbol Mg and atomic number 12. It is a shiny gray metal having a low density, low melting point and high chemical reactivity. Like the other alkaline earth metals (group 2 of the periodic table), it occurs naturally only in combination with other elements and almost always has an oxidation state of +2. It reacts readily with air to form a thin Passivation (chemistry), passivation coating of magnesium oxide that inhibits further corrosion of the metal. The free metal burns with a brilliant-white light. The metal is obtained mainly by electrolysis of magnesium Salt (chemistry), salts obtained from brine. It is less dense than aluminium and is used primarily as a component in strong and lightweight magnesium alloy, alloys that contain aluminium. In the cosmos, magnesium is produced in large, aging stars by the sequential addition of three Helium nucleus, helium nuclei to a carbon nucleus. When such stars explo ...
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Metaphosphate
A metaphosphate ion is an oxyanion that has the empirical formula . It was first postulated in 1955 but was not observed until 1979, when it was detected by mass spectrometry. Metaphosphate is an intermediate in the hydrolysis of phosphate esters but it is difficult to isolate, as it readily hydrolyses to from a dihydrogen phosphate Dihydrogen phosphate is an inorganic ion with the formula 2PO4sup>−. Phosphates occur widely in natural systems. Perhaps the most common salt of dihydrogen phosphate is sodium dihydrogen phosphate. It is used in animal feed, fertilizer, ... ion () and tends to self-react in the absence of water to form rings or infinite chains: These species are also called metaphosphates and are generally stable, with some such as sodium trimetaphosphate being produced on an industrial scale. Metaphosphates can be used as an alternative of white phosphorus in organic syntheses. See also * Sodium trimetaphosphate * Sodium hexametaphosphate References ...
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Dissociative Substitution
In chemistry, dissociative substitution describes a reaction pathway by which compounds interchange ligands. The term is typically applied to coordination and organometallic complexes, but resembles the SN1 mechanism in organic chemistry. This pathway can be well described by the ''cis'' effect, or the labilization of CO ligands in the ''cis'' position. The opposite pathway is associative substitution, being analogous to SN2 pathway. Pathways that are intermediate between the pure dissociative and pure associative pathways are called interchange mechanisms. Complexes that undergo dissociative substitution are often coordinatively saturated and often have octahedral molecular geometry. The entropy of activation is characteristically positive for these reactions, which indicates that the disorder of the reacting system increases in the rate-determining step. Kinetics Dissociative pathways are characterized by a rate determining step that involves release of a ligand from t ...
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Stem-loop
Stem-loops are nucleic acid Biomolecular structure, secondary structural elements which form via intramolecular base pairing in single-stranded DNA or RNA. They are also referred to as hairpins or hairpin loops. A stem-loop occurs when two regions of the same nucleic acid strand, usually Complementarity (molecular biology), complementary in nucleotide sequence, base-pair to form a double helix that ends in a loop of unpaired nucleotides. Stem-loops are most commonly found in RNA, and are a key building block of many RNA biomolecular structure#Secondary structure, secondary structures. Stem-loops can direct RNA folding, protect structural stability for messenger RNA (mRNA), provide recognition sites for RNA-binding protein, RNA binding proteins, and serve as a Substrate (chemistry), substrate for Enzyme catalysis, enzymatic reactions. Formation and stability The formation of a stem-loop is dependent on the stability of the helix and loop regions. The first prerequisite is the p ...
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Antiparallel (biochemistry)
In biochemistry, two biopolymers are antiparallel if they run parallel (geometry), parallel to each other but with opposite directionality (molecular biology), directionality (alignments). An example is the two complementarity (molecular biology), complementary strands of a DNA nucleic acid double helix, double helix, which antiparallel vectors, run in opposite directions alongside each other. Nucleic acids Nucleic acid molecules have a phosphoryl (5') end and a hydroxyl (3') end. This notation follows from IUPAC nomenclature of organic chemistry, organic chemistry nomenclature, and can be used to define the movement of enzymes such as DNA polymerases relative to the DNA strand in a non-arbitrary manner. G-quadruplexes G-quadruplexes, also known as G4 DNA are secondary structures found in nucleic acids that are rich in guanine. These structures are normally located at the telomeres (the ends of the Chromosome, chromosomes). The G-quadruplex can either be parallel or antiparallel ...
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Amino Acid
Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. Only these 22 appear in the genetic code of life. Amino acids can be classified according to the locations of the core structural functional groups ( alpha- , beta- , gamma- amino acids, etc.); other categories relate to polarity, ionization, and side-chain group type ( aliphatic, acyclic, aromatic, polar, etc.). In the form of proteins, amino-acid '' residues'' form the second-largest component (water being the largest) of human muscles and other tissues. Beyond their role as residues in proteins, amino acids participate in a number of processes such as neurotransmitter transport and biosynthesis. It is thought that they played a key role in enabling life on Earth and its emergence. Amino acids are formally named by the IUPAC- IUBMB Joint Commi ...
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C-terminus
The C-terminus (also known as the carboxyl-terminus, carboxy-terminus, C-terminal tail, carboxy tail, C-terminal end, or COOH-terminus) is the end of an amino acid chain (protein Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residue (biochemistry), residues. Proteins perform a vast array of functions within organisms, including Enzyme catalysis, catalysing metab ... or polypeptide), terminated by a free carboxyl group (-COOH). When the protein is translated from messenger RNA, it is created from N-terminus to C-terminus. The convention for writing peptide sequences is to put the C-terminal end on the right and write the sequence from N- to C-terminus. Chemistry Each amino acid has a carboxyl group and an amine group. Amino acids link to one another to form a chain by a dehydration reaction which joins the amine group of one amino acid to the carboxyl group of the next. Thus polypeptide chains have an end with an ...
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Alpha-helix
An alpha helix (or α-helix) is a sequence of amino acids in a protein that are twisted into a coil (a helix). The alpha helix is the most common structural arrangement in the secondary structure of proteins. It is also the most extreme type of local structure, and it is the local structure that is most easily predicted from a sequence of amino acids. The alpha helix has a right-handed helix conformation in which every backbone N−H group hydrogen bonds to the backbone C=O group of the amino acid that is four residues earlier in the protein sequence. Other names The alpha helix is also commonly called a: * Pauling–Corey–Branson α-helix (from the names of three scientists who described its structure) * 3.613-helix because there are 3.6 amino acids in one ring, with 13 atoms being involved in the ring formed by the hydrogen bond (starting with amidic hydrogen and ending with carbonyl oxygen) Discovery In the early 1930s, William Astbury showed that there were d ...
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N-terminus
The N-terminus (also known as the amino-terminus, NH2-terminus, N-terminal end or amine-terminus) is the start of a protein or polypeptide, referring to the free amine group (-NH2) located at the end of a polypeptide. Within a peptide, the amine group is bonded to the carboxylic group of another amino acid, making it a chain. That leaves a free carboxylic group at one end of the peptide, called the C-terminus, and a free amine group on the other end called the N-terminus. By convention, peptide sequences are written N-terminus to C-terminus, left to right (in LTR writing systems). This correlates the translation direction to the text direction, because when a protein is translated from messenger RNA, it is created from the N-terminus to the C-terminus, as amino acids are added to the carboxyl end of the protein. Chemistry Each amino acid has an amine group and a carboxylic group. Amino acids link to one another by peptide bonds which form through a dehydration reaction that ...
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