Function and biotechnology of extremophilic enzymes in low water
... diminishing the number of intermolecular hydrogen bonds [20-22]. High salt concentrations critically affect the solubility, binding, stability, and crystallization of proteins [23]. The interactions between proteins and protein subunits in solution are also altered by salts. The electrostatic intera ...
... diminishing the number of intermolecular hydrogen bonds [20-22]. High salt concentrations critically affect the solubility, binding, stability, and crystallization of proteins [23]. The interactions between proteins and protein subunits in solution are also altered by salts. The electrostatic intera ...
2 - Griffith Research Online
... diester, thereby acting as Lewis acid catalysts3. Reaction site specificity of FEN1 superfamily proteins was proposed to be explained by a double nucleotide unpairing (DNU) mechanism, which only allows the specific phosphate diester to access active site metal ions2,4-6 (Figure 1). This mechanism wa ...
... diester, thereby acting as Lewis acid catalysts3. Reaction site specificity of FEN1 superfamily proteins was proposed to be explained by a double nucleotide unpairing (DNU) mechanism, which only allows the specific phosphate diester to access active site metal ions2,4-6 (Figure 1). This mechanism wa ...
Metabolism - Glycolysis
... Reactions 2 and 5 are catalyzed by isomerases (carbonyl isomerization) ...
... Reactions 2 and 5 are catalyzed by isomerases (carbonyl isomerization) ...
BIOANALYTICAL/CLINICAL ANALYSIS
... URIC ACID + URICASE PEROXIDE + ALLANTOIN -Measure decrease in absorbance at 290nm of Uric Acid OR – Use o-dianisidine + Peroxide Red Color G. CREATININE ...
... URIC ACID + URICASE PEROXIDE + ALLANTOIN -Measure decrease in absorbance at 290nm of Uric Acid OR – Use o-dianisidine + Peroxide Red Color G. CREATININE ...
Bacterial transformation - BLI-Research-Synbio-2014-session-1
... • Restriction enzymes cut DNA by cleaving the sugar-phosphate backbone. • Restriction enzymes do not randomly cut, nor do they all cut DNA in the same location. • Like other enzymes they show specificity for certain sites. • Restriction enzymes recognize, bind to, and cut DNA within specific base se ...
... • Restriction enzymes cut DNA by cleaving the sugar-phosphate backbone. • Restriction enzymes do not randomly cut, nor do they all cut DNA in the same location. • Like other enzymes they show specificity for certain sites. • Restriction enzymes recognize, bind to, and cut DNA within specific base se ...
Proteins
... biological molecules. Their name is derived from the Greek word proteios which means first. Proteome is all the proteins in a living organism, while proteomics is the study of these proteins. ...
... biological molecules. Their name is derived from the Greek word proteios which means first. Proteome is all the proteins in a living organism, while proteomics is the study of these proteins. ...
Final
... Complete the following narrative by circling the word or phrase in each bold faced parenthesis that most accurately completes the statement. (1 point each). The study of variation in bacteria has several features that are distinct from the study of genetics in eukaryotic organisms. Bacteria typical ...
... Complete the following narrative by circling the word or phrase in each bold faced parenthesis that most accurately completes the statement. (1 point each). The study of variation in bacteria has several features that are distinct from the study of genetics in eukaryotic organisms. Bacteria typical ...
Structures of Proteins Primary structure
... It is transported around the body bound to specific a B12 binding protein (trans-cobalamin). It is stored mainly in the liver in amounts (3-5mg) sufficient to last a couple of years. ...
... It is transported around the body bound to specific a B12 binding protein (trans-cobalamin). It is stored mainly in the liver in amounts (3-5mg) sufficient to last a couple of years. ...
SHORT COMMUNICATION The Cellular Location of
... Cellular location of enzymes No proteinase ycaB was detected in concentrated culture filtrates from either yeast cells or germ-tube-forming cells. Pepstatin-sensitive proteinase activity in these preparations probably represents proteinase ycaA (Remold et al., 1968). Vacuole preparations were enrich ...
... Cellular location of enzymes No proteinase ycaB was detected in concentrated culture filtrates from either yeast cells or germ-tube-forming cells. Pepstatin-sensitive proteinase activity in these preparations probably represents proteinase ycaA (Remold et al., 1968). Vacuole preparations were enrich ...
SHORT COMMUNICATION The Cellular Location of
... Cellular location of enzymes No proteinase ycaB was detected in concentrated culture filtrates from either yeast cells or germ-tube-forming cells. Pepstatin-sensitive proteinase activity in these preparations probably represents proteinase ycaA (Remold et al., 1968). Vacuole preparations were enrich ...
... Cellular location of enzymes No proteinase ycaB was detected in concentrated culture filtrates from either yeast cells or germ-tube-forming cells. Pepstatin-sensitive proteinase activity in these preparations probably represents proteinase ycaA (Remold et al., 1968). Vacuole preparations were enrich ...
Class details
... Dye (Coomassie Brilliant Blue G-250) Dye binds protein, Abs increases (at 595nm) More protein = ? ...
... Dye (Coomassie Brilliant Blue G-250) Dye binds protein, Abs increases (at 595nm) More protein = ? ...
Pathways of Pyrimidine and Purine Metabolism in E.coli
... rihC is shown to hydrolyze multiple substrates and is the only hydrolase shown to act on purines ...
... rihC is shown to hydrolyze multiple substrates and is the only hydrolase shown to act on purines ...
Answer guide
... allow any sensible answer e.g. ethanol, carbon dioxide, citric acid, lactic acid, methane, penicillin, antibiotics ...
... allow any sensible answer e.g. ethanol, carbon dioxide, citric acid, lactic acid, methane, penicillin, antibiotics ...
Plasma enzyme
... LDH is a hydrogen transfer enzyme which catalyzes the interconversion of pyruvate and lactate. In the liver, it catalyzes the oxidation of L-lactate to pyruvate (L P) with the mediation of NAD as hydrogen acceptor. The reaction is reversible and the reaction equilibrium strongly favors the reverse ...
... LDH is a hydrogen transfer enzyme which catalyzes the interconversion of pyruvate and lactate. In the liver, it catalyzes the oxidation of L-lactate to pyruvate (L P) with the mediation of NAD as hydrogen acceptor. The reaction is reversible and the reaction equilibrium strongly favors the reverse ...
Disorders of phenylalanine and tyrosine metabolism
... cob(I) alamin (cblI) from 5,10-methylene tetrahydro folate which is regenerated in the folate cycle. The breakdown of homocysteine to cysteine is catalysed by the vit. B6-dependent enzymes cystathionine beta-synthase (CBS) und cystathionine gamma-lyase (CTH). Cysteine is further catabolised via cy ...
... cob(I) alamin (cblI) from 5,10-methylene tetrahydro folate which is regenerated in the folate cycle. The breakdown of homocysteine to cysteine is catalysed by the vit. B6-dependent enzymes cystathionine beta-synthase (CBS) und cystathionine gamma-lyase (CTH). Cysteine is further catabolised via cy ...
Discussion - AHCC Published Research
... induced liver injury mice prepared for this experiment. Regarding organ weight, AHCC significantly inhibit liver weight gain. Liver of mouse administered CCI4 is known to become fatty liver because of disorder of lipid metabolism, and olive oil used as a solubilizer is also a cause of adiposity in l ...
... induced liver injury mice prepared for this experiment. Regarding organ weight, AHCC significantly inhibit liver weight gain. Liver of mouse administered CCI4 is known to become fatty liver because of disorder of lipid metabolism, and olive oil used as a solubilizer is also a cause of adiposity in l ...
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 ...
BiochemReview
... • First AA is usually Methionine, as its sequence is AUG, the “start” codon. This has a formyl group in bacteria, but not in eukaryotes. • Hence, it’s called N-formyl Methionine. ...
... • First AA is usually Methionine, as its sequence is AUG, the “start” codon. This has a formyl group in bacteria, but not in eukaryotes. • Hence, it’s called N-formyl Methionine. ...
Structural Insights into Maize Viviparous14, a Key
... by multiple wavelength anomalous dispersion (MAD; Hendrickson, 1991), was refined to an Rwork/Rfree of 23.2/28.4% (Table 1; see Methods). VP14 folds as a seven-blade b-propeller with four a-helical inserts that form an a-helical domain on top of the b-propeller (Figure 2). Five of the seven blades o ...
... by multiple wavelength anomalous dispersion (MAD; Hendrickson, 1991), was refined to an Rwork/Rfree of 23.2/28.4% (Table 1; see Methods). VP14 folds as a seven-blade b-propeller with four a-helical inserts that form an a-helical domain on top of the b-propeller (Figure 2). Five of the seven blades o ...
- TestbankU
... to peptide bonds, a form of covalent bond, secondary is due to hydrogen bonds between amino acids that are not directly connected to each other, tertiary is typically due to hydrophobic interactions – hydrophobic residues on the inside and hydrophilic residues on the outside with some disulphide cov ...
... to peptide bonds, a form of covalent bond, secondary is due to hydrogen bonds between amino acids that are not directly connected to each other, tertiary is typically due to hydrophobic interactions – hydrophobic residues on the inside and hydrophilic residues on the outside with some disulphide cov ...
Authors` version - The Computable Plant
... for L-valine and L-isoleucine biosynthesis are catalyzed by a set of bi-functional enzymes that bind substrates from either pathway, L-valine inhibition of the first enzyme specific for its biosynthesis catalyzed by a single α-acetohydroxy acid synthase (AHAS) could compromise the cell for L-isoleuc ...
... for L-valine and L-isoleucine biosynthesis are catalyzed by a set of bi-functional enzymes that bind substrates from either pathway, L-valine inhibition of the first enzyme specific for its biosynthesis catalyzed by a single α-acetohydroxy acid synthase (AHAS) could compromise the cell for L-isoleuc ...
Enzymes
... • A protein’s secondary structure consists of regular, repeated patterns in different regions in the polypeptide chain. • This shape is influenced primarily by hydrogen bonds arising from the amino acid sequence (the primary structure). • The two common secondary structures are the a helix and the b ...
... • A protein’s secondary structure consists of regular, repeated patterns in different regions in the polypeptide chain. • This shape is influenced primarily by hydrogen bonds arising from the amino acid sequence (the primary structure). • The two common secondary structures are the a helix and the b ...
Enzyme
Enzymes /ˈɛnzaɪmz/ are macromolecular biological catalysts. Enzymes accelerate, or catalyze, chemical reactions. The molecules at the beginning of the process are called substrates and the enzyme converts these into different molecules, called products. Almost all metabolic processes in the cell need enzymes in order to occur at rates fast enough to sustain life. The set of enzymes made in a cell determines which metabolic pathways occur in that cell. The study of enzymes is called enzymology.Enzymes are known to catalyze more than 5,000 biochemical reaction types. Most enzymes are proteins, although a few are catalytic RNA molecules. Enzymes' specificity comes from their unique three-dimensional structures.Like all catalysts, enzymes increase the rate of a reaction by lowering its activation energy. Some enzymes can make their conversion of substrate to product occur many millions of times faster. An extreme example is orotidine 5'-phosphate decarboxylase, which allows a reaction that would otherwise take millions of years to occur in milliseconds. Chemically, enzymes are like any catalyst and are not consumed in chemical reactions, nor do they alter the equilibrium of a reaction. Enzymes differ from most other catalysts by being much more specific. Enzyme activity can be affected by other molecules: inhibitors are molecules that decrease enzyme activity, and activators are molecules that increase activity. Many drugs and poisons are enzyme inhibitors. An enzyme's activity decreases markedly outside its optimal temperature and pH.Some enzymes are used commercially, for example, in the synthesis of antibiotics. Some household products use enzymes to speed up chemical reactions: enzymes in biological washing powders break down protein, starch or fat stains on clothes, and enzymes in meat tenderizer break down proteins into smaller molecules, making the meat easier to chew.