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Cloning and expression of maize-leaf pyruvate, Pi dikinase
Cloning and expression of maize-leaf pyruvate, Pi dikinase

... means for cloning the RP gene. We sought to do this by identifying those sequences that were consistent with the known properties of the RP. These included plant proteins with (i) an estimated molecular mass of between 45 and 48 kDa, (ii) a chloroplast transit peptide, (iii) a threonine/ serine prot ...
Pavel Doležal
Pavel Doležal

Lecture 11 - Biosynthesis of Amino Acids
Lecture 11 - Biosynthesis of Amino Acids

... The ammonium ion is assimilated into an amino acid through glutamate and glutamine Most amino acids obtain their α–amino group from glutamate by transamination. The sidechain nitrogen of glutamine is the nitrogen source for the sidechain nitrogens of tryptophan and histidine. ...
CHAPTER 6
CHAPTER 6

... order that they can be regulated independently. Shown here are two possible arrangements of opposing catabolic and anabolic sequenced between A and P. (a) The parallel sequences proceed via independent routes. (b) Only one reaction has two different enzymes, a catabolic one (E3) and it’s anabolic co ...
Pavel Doležal
Pavel Doležal

... and newly characterized organelles, the mitosomes. These organelles were suggested to evolve either from a common pro-mitochondrial endosymbiont, or they represent highly modified or reduced mitochondria. Although the metabolic pathways in mitochondria and hydrogenosomes are rather different, and me ...
Introduction
Introduction

... How the FBS Standard is Used: Growth Curve Challenges: Cell Line, Cell Density, Cell Counting, Days in Culture • Three cell densities, determine viable cell counts on days 0,1,2,3,4, and 7. Select the cell density that exhibit a growth curve with 3 phases: Lag, Log, Stationary; and linear over 3 ti ...
Combining Rational and Evolutionary Approaches
Combining Rational and Evolutionary Approaches

... synthetic RNA switch to screen for improvements in enzymatic activity in vivo, I increased the activity of a model enzyme more than 30-fold. I then used a systems-level analysis of the host to identify a stress, heme depletion, that the enzyme placed on its host. Alleviating that stress increased th ...
Broad-Spectrum Peptide Inhibitors of Aminoglycoside Antibiotic
Broad-Spectrum Peptide Inhibitors of Aminoglycoside Antibiotic

... structures. Given this common binding site feature, positively charged molecules could be developed that interfere with this interaction with aminoglycosides and lead to broad-spectrum inhibition of resistance activity. Given that aminoglycoside resistance enzymes share this common binding strategy ...
3. Feedback mechanisms control cellular respiration
3. Feedback mechanisms control cellular respiration

... • Amino acids that will be catabolized must have their amino groups removed via deamination. • The nitrogenous waste is excreted as ammonia, urea, or another waste product. ...
Cloning and characterization of the
Cloning and characterization of the

... we cloned. Starting at position 40, the cDNA contains a complete 1605 bp long ORF that codes for a 534 amino acid long polypeptide (EMBL ID/accession no. SPO251329/AJ251329). This protein was named spPus1p (for S.pombe pseudouridine synthase 1), because of its sequence homology to two previously cha ...
Exonuclease active site: a more complete description
Exonuclease active site: a more complete description

... interacts with the hydroxyl of Y165, with the catalytic aspartate of the exonuclease III motif (D169), and with the scissile phosphate through a water-mediated hydrogen bond (Figure S1). The quality of the maps for the former conformation of copy B is extremely poor due to disorder, so only the mor ...
FORMATION OF AMMONIA
FORMATION OF AMMONIA

... results in a deficiency of one of the enzymes in the urea cycle. These enzymes are responsible for removing ammonia from the blood stream. Severe deficiency or total absence of activity of any of the first four enzymes (CPS1, OTC, ASS, ASL) in the urea cycle or the cofactor producer (NAGS) results i ...
Amino Acids, Proteins, and Enzymes
Amino Acids, Proteins, and Enzymes

... Enzyme Cofactors  A simple enzyme is an active enzyme that consists only of protein.  Many enzymes are active only when they combine with cofactors such as metal ions or small molecules.  A coenzyme is a cofactor that is a small organic molecule such as a vitamin. ...
Using antibody catalysis to study the outcome of multiple
Using antibody catalysis to study the outcome of multiple

... somatic mutation that placed a lysine residue in a deep, yet otherwise unrefined, hydrophobic pocket. We suggest that covalent chemistries may be as readily selected from the immune repertoire as the traditional noncovalent interactions that have formed the basis of immunochemistry until this time. ...
2 hours
2 hours

... overall free-energy change. Thus, a step that might not normally occur can be driven if it is coupled to a thermodynamically stable reaction. ...
Khoa hoc - Cong nghe
Khoa hoc - Cong nghe

Biochemical Patterns of Some Heterotrophic Marine
Biochemical Patterns of Some Heterotrophic Marine

... incubated in acetate+ammonium+phosphate ANSW medium at 18" for 72 hr with aeration were used. The bacteria were centrifuged at low temperatures, washed three times with ANSW and disintegrated for 10 min. in distilled water at 0" by ultrasonic treatment in a MSE 60 W. disintegrator. The suspension wa ...
Urea Cycle Defect: A Case Study
Urea Cycle Defect: A Case Study

... deficiency of the urea cycle enzyme ornithine transcarbamylase (OTC). The primary function of OTC is to catalyze the second reaction seen in the first figure of the urea cycle. In this reaction carbamylphosphate is coupled to the d-amino group of the amino acid ornithine, which together produces the ...
Document
Document

Nucleotide File
Nucleotide File

... pathways.[7] The components used in de novo nucleotide synthesis are derived from biosynthetic precursors of carbohydrate and amino acid metabolism, and from ammonia and carbon dioxide. The liver is the major organ of de novo synthesis of all four nucleotides. De novo synthesis of pyrimidines and pu ...
Skin fibroblast culture
Skin fibroblast culture

2, The Glyoxylate Pathway
2, The Glyoxylate Pathway

... intermediates. GAP and F6P are consumed through glycolysis and oxidative phosphorylation or recycled by gluconeogenesis to form G6P. In the latter case, 1 G6P can be converted, via 6 cycles of pentose phosphate pathway and gluconeogenesis, to 6 CO2 and 12 NADPH. • When R5P is needed more than NADPH, ...
hanan abas
hanan abas

... .Potassium Oxalate is always used as anticoagulants, by most ...
2.3 Carbon-Based Molecules
2.3 Carbon-Based Molecules

... • Proteins are polymers of amino acid monomers. – Twenty different amino acids are used to build proteins in organisms. – Amino acids differ in side groups, or R groups. – Amino acids are linked by peptide bonds. ...
glucose
glucose

... The most important amino acid for gluconeogenesis is alanin It is formed mainly in muscle by transamination of pyruvate and is transported by blood to the liver. ...
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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.
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