catalyze
(verb)
To accelerate a process.
Examples of catalyze in the following topics:
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Types and Functions of Proteins
- Enzymes are proteins that catalyze biochemical reactions, which otherwise would not take place.
- The substrates are the reactants that undergo the chemical reaction catalyzed by the enzyme.
- These enzymes include amylase, which catalyzes the digestion carbohydrates in the mouth and small intestine; pepsin, which catalyzes the digestion of proteins in the stomach; lipase, which catalyzes reactions need to emulsify fats in the small intestine; and trypsin, which catalyzes the further digestion of proteins in the small intestine.
- These biosynthetic enzymes include DNA Polymerase, which catalyzes the synthesis of new strands of the genetic material before cell division; fatty acid synthetase, which the synthesis of new fatty acids for fat or membrane lipid formation; and components of the ribosome, which catalyzes the formation of new polypeptides from amino acid monomers.
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Enzyme Active Site and Substrate Specificity
- Enzymes catalyze chemical reactions by lowering activation energy barriers and converting substrate molecules to products.
- This dynamic binding maximizes the enzyme's ability to catalyze its reaction.
- One of the important properties of enzymes is that they remain ultimately unchanged by the reactions they catalyze.
- After an enzyme is done catalyzing a reaction, it releases its products (substrates).
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The Energy-Releasing Steps of Glycolysis
- In the seventh step, catalyzed by phosphoglycerate kinase (an enzyme named for the reverse reaction), 1,3-bisphosphoglycerate donates a high-energy phosphate to ADP, forming one molecule of ATP.
- The enzyme catalyzing this step is a mutase (isomerase).
- Enolase catalyzes the ninth step.
- The last step in glycolysis is catalyzed by the enzyme pyruvate kinase (the enzyme in this case is named for the reverse reaction of pyruvate's conversion into PEP) and results in the production of a second ATP molecule by substrate-level phosphorylation and the compound pyruvic acid (or its salt form, pyruvate).
- Many enzymes in enzymatic pathways are named for the reverse reactions since the enzyme can catalyze both forward and reverse reactions (these may have been described initially by the reverse reaction that takes place in vitro, under non-physiological conditions).
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The Energy-Requiring Steps of Glycolysis
- The first step in glycolysis is catalyzed by hexokinase, an enzyme with broad specificity that catalyzes the phosphorylation of six-carbon sugars.
- An enzyme that catalyzes the conversion of a molecule into one of its isomers is an isomerase.
- The third step is the phosphorylation of fructose-6-phosphate, catalyzed by the enzyme phosphofructokinase.
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Control of Catabolic Pathways
- Enzymes, proteins, electron carriers, and pumps that play roles in glycolysis, the citric acid cycle, and the electron transport chain tend to catalyze non-reversible reactions.
- This enzyme catalyzes the phosphorylation of glucose, which helps to prepare the compound for cleavage in a later step.
- The last step in glycolysis is catalyzed by pyruvate kinase.
- The citric acid cycle is controlled through the enzymes that catalyze the reactions that make the first two molecules of NADH .
- Enzymes, isocitrate dehydrogenase and α-ketoglutarate dehydrogenase, catalyze the reactions that make the first two molecules of NADH in the citric acid cycle.
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Nitrogenous Waste in Terrestrial Animals: The Urea Cycle
- The urea cycle utilizes five intermediate steps, catalyzed by five different enzymes, to convert ammonia to urea.
- The enzyme ornithine transcarbamylase catalyzes a key step in the urea cycle.
- The urea cycle converts ammonia to urea in five steps that include the catalyzation of five different enzymes.
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Metabolic Pathways
- Each reaction step is facilitated, or catalyzed, by a protein called an enzyme.
- Enzymes are important for catalyzing all types of biological reactions: those that require energy as well as those that release energy.
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Regulatory Mechanisms for Cellular Respiration
- Reactions that are catalyzed by only one enzyme can go to equilibrium, stalling the reaction.
- A number of enzymes involved in each of the pathways (in particular, the enzyme catalyzing the first committed reaction of the pathway) are controlled by attachment of a molecule to an allosteric (non-active) site on the protein.
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Elongation and Termination in Eukaryotes
- Consequently, RNA Polymerase II does not need as many accessory proteins to catalyze the synthesis of new RNA strands during transcription elongation as DNA Polymerase does to catalyze the synthesis of new DNA strands during replication elongation.
- However, RNA Polymerase II does need a large collection of accessory proteins to initiate transcription at gene promoters, but once the double-stranded DNA in the transcription start region has been unwound, the RNA Polymerase II has been positioned at the +1 initiation nucleotide, and has started catalyzing new RNA strand synthesis, RNA Polymerase II clears or "escapes" the promoter region and leaves most of the transcription initiation proteins behind.
- All RNA Polymerases travel along the template DNA strand in the 3' to 5' direction and catalyze the synthesis of new RNA strands in the 5' to 3' direction, adding new nucleotides to the 3' end of the growing RNA strand.
- Once the addition of a new nucleotide to the 3' end of the growing strand has been catalyzed, the RNA Polymerase moves to the next DNA nucleotide on the template below it.
- The Poly(A) Polymerase enzyme which catalyzes the addition of a 3' poly-A tail on the pre-mRNA is part of the complex that forms with CPSF and CstF.
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Plasma Membrane Hormone Receptors
- Adenylyl cyclase catalyzes the conversion of ATP to cAMP. cAMP, in turn, activates a group of proteins called protein kinases, which transfer a phosphate group from ATP to a substrate molecule in a process called phosphorylation.
- Further amplification occurs as protein kinases, once activated by cAMP, can catalyze many reactions.