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Activation, conversion from glycogen phosphorylase B to glycogen phosphorylase A

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The substrate of phosphorylase is glycogen. Phosphorylase is an enzyme that catalyzes the breakdown of glycogen into glucose-1-phosphate, which can then be used by cells for energy production.

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Glycogen phosphorylase can not cleave the alpha-1,6-glycosidic bonds at glycogen branch points

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the last step is ofcourse glycogen breakdown.......before that inactive glycogen phosphorylase-b is activated and phosphorylated to glycogen phosphorylase-a

by the help of activated phosphorylase kinase........

......phosphorylase kinase was activated by activated protien kinase..and activated protien kinase was activated by cyclic amp...........

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Phosphatase is an enzyme that removes phosphate groups from molecules, while phosphorylase is an enzyme that adds phosphate groups to molecules. Phosphatase acts by hydrolyzing phosphate ester bonds, while phosphorylase catalyzes the transfer of a phosphate group from a donor molecule to a substrate molecule.

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Chloroplasts and mitochondria both contain phosphorylase enzymes because these enzymes are involved in energy metabolism processes that occur in both organelles. Phosphorylase enzymes are responsible for catalyzing the breakdown of glycogen into glucose units in the cytoplasm, releasing energy in the form of ATP which is essential for cellular energy production.

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Starch phosphorylase is primarily involved in starch degradation by catalyzing the conversion of starch to glucose. In vivo starch anabolism involves the synthesis of starch molecules from glucose, which is carried out by enzymes like starch synthase and starch branching enzyme. Therefore, starch phosphorylase is not directly involved in the biosynthesis of starch in living systems.

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Phosphorylase and phosphatase are enzymes involved in regulating cellular processes by adding or removing phosphate groups from molecules. Phosphorylase adds phosphate groups to molecules, while phosphatase removes phosphate groups. This difference in function affects how these enzymes interact with other molecules and influence cellular activities.

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Phosphorylase is an enzyme that adds a phosphate group to a molecule, typically to activate it. Phosphatase is an enzyme that removes a phosphate group from a molecule, usually to deactivate it or regulate its activity. Essentially, phosphorylase adds a phosphate group while phosphatase removes a phosphate group.

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Phosphatase, phosphorylase, and kinase are enzymes involved in cellular processes. Phosphatase removes phosphate groups from molecules, phosphorylase adds phosphate groups to molecules, and kinase transfers phosphate groups from ATP to other molecules. Each enzyme has a specific function and mechanism of action in regulating cellular activities.

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Phosphorylase is an enzyme that adds phosphate groups to molecules, while kinase is an enzyme that transfers phosphate groups from ATP to other molecules. In cellular signaling pathways, phosphorylase helps activate or deactivate proteins by adding phosphate groups, while kinase helps transmit signals by transferring phosphate groups.

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glycogen phosphorylase, glycogen debranching enzyme, phosphoglutomutase

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Starch phosphorylase is important in metabolism as it helps break down starch into glucose units for energy production. This enzyme plays a key role in glycogen degradation in animals and starch degradation in plants, providing essential substrates for energy metabolism. Additionally, starch phosphorylase helps regulate blood glucose levels and is involved in various cellular processes related to energy balance.

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The cleavage of glycogen phosphorylase releases glucose-1-phosphate by breaking the glycosidic bond within glycogen. This glucose-1-phosphate can then be further processed to yield free glucose for energy production.

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Alpha 1,4 glucosidase helps break down complex carbohydrates into simpler sugars, while glycogen phosphorylase helps break down glycogen into glucose for energy. Essentially, alpha 1,4 glucosidase is involved in the initial breakdown of carbohydrates, while glycogen phosphorylase is involved in breaking down stored glycogen for energy production.

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The enzyme called glycogen phosphorylase breaks down glycogen in the body.

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I think you're referring to glycogen phosphorylase, which is an enzyme that catalyzes the reaction where glycogen is turned into a glucose-molecule, therefore making it available for transformation to energy.

Glycogen phosphorylase comes in two forms, A and B. Usually, the A form is considered the active form, whilst B is the inactive form. That is a modified truth, since both of these forms can exist in a T (tense) inactive state and R (relaxed) active state, depending on the presence of ADP (residue after phosphorylation of ATP). But usually, A is in its R state and B is in its T state. So for the sake of argument, we say A is active and B is inactive.

So the short answer would be 'No'. For example, hormones such as epinephrine, insulin, and glucagon regulate glycogen phosphorylase. Essentially, epinephrine and glucagon promotes the A form (by activating phosphorylase kinase, an enzyme that transforms A into B), and insulin promotes the B form (by inhibiting the phosphorylase kinase).

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Well this is a complicated question, one easy answer would be the salivary amylase, acetyl co enzyme A, B, C, D etc.

1) Each enzyme is specific : here are five out of 5,000 answers -

- pyruvate decarboxylase

- isocitrate lyase

- acetyl-CoA transferase

- phosphorylase kinase

- tryptophan 2-3-dioxygenase

2) note that all enzyme suffixes are -ase.

3) phosphorylase kinase has two -ases - a nested loop - is an ON switch -

phosphorylase phosphatase - also a nested loop - is an OFF switch.

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Michael Richard Dyson has written:

'The synthesis of potential nucleoside phosphorylase-resistant antiviral agents'

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well, its because too much starch in your diet makes you die a horribly painful death.

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Starch phosphorylase is primarily involved in starch catabolism, breaking down starch molecules into glucose units. It catalyzes the phosphorolytic cleavage of α-1,4 glycosidic bonds in starch. Starch anabolism, on the other hand, involves the synthesis of starch molecules from glucose monomers by enzymes like starch synthase and ADP-glucose pyrophosphorylase.

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Phosphorylase is an enzyme which joins with Glucose-1-phosphate together to make larger starch molecules. it is an example of synthesis (a joing together enzyme)

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William L Rumsey has written:

'Sex-related influences on exercise-induced myocardial phosphorylase conversion and associated glycogen depletion'

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Actually, three are the enzymes that intervene during glycogen breakdown (glycogenolysis).


  1. First, Glycogen phosphorylase (or simply phosphorylase) that catalyzes glycogen phosphorolysis (bond cleavage by the substitution of a phosphate group) to yield glucose-1-phosphate (G1P) releasing only one glucose residue that is at least five residues from a ramification point.
  2. The second enzyme is the Glycogen debranching enzymethat removes glycogen's branches, thereby permiting the glycogen phosphorylase reaction (see above) to go to completion. This enzymes also hydrolyzes alpha(1-6)-linked glucosyl units to yield glucose.
  3. Finally, Phosphoglucomutase that converts G1P to G6P which is also formed in the first step of glycolysis through the action of either hexokinase or glucokinase.

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No. Insulin converts glucose into glycogen for storage in the body. Glucagon converts glycogen into glucose.

(it's the various cells in the body that do the conversion in either case, insulin and glucagon are hormones that induce the shift in the metabolism.)

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Glycogen is broken down in the body through a process called glycogenolysis. This process involves the enzyme glycogen phosphorylase breaking down glycogen into glucose molecules, which can then be used for energy by the body.

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The enzyme that synthesizes starch from glucose-1-phosphate is starch synthase. This enzyme catalyzes the condensation reaction of glucose molecules to form the starch polymer.

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The main enzyme for breaking down glycogen is glycogen phosphorylase. This enzyme catalyzes the phosphorylytic cleavage of glucose residues from the glycogen polymer, releasing glucose-1-phosphate for energy production.

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DNA polymerase is an enzyme responsible for synthesizing new DNA strands during DNA replication. It catalyzes the formation of phosphodiester bonds between nucleotides to create a complementary strand of DNA based on a template strand.

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I, II, and III

  1. I. It is the rate-limiting enzyme of glycogenolysis
  2. II. It breaks alpha 1,4 glycosidic bonds
  3. III. It is activated by epinephrine

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The process of "glycogenolysis" is the splitting of glycogen in the liver, which in turn produces glucose. Glucagon can be administered in emergency diabetic situations where sugar can't be taken orally.

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The conversion of glycogen to glucose-1-phosphate is the first step in glycogen breakdown, also known as glycogenolysis. This process is catalyzed by the enzyme glycogen phosphorylase, which cleaves off a glucose molecule from the glycogen polymer. Glucose-1-phosphate is then further converted to glucose-6-phosphate for energy production.

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Yes, glycogen has more accessible cleavage sites than amylose because it is a highly branched polymer with multiple alpha-1,6-glycosidic bonds in addition to alpha-1,4-glycosidic bonds. This branching structure allows for more points of cleavage by enzymes like glycogen phosphorylase compared to the linear structure of amylose.

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root hair, the rhizoid of a vascular plant, is a tubular outgrowth of a trichoblast, a hair-forming cell on the epidermis of a plant root. As they are lateral extensions of a single cell and only rarely branched, they are invisible to the naked eye. They are found only in the region of maturation of the root. Just prior to the root hair cell development, there is a point of elevated phosphorylase activity

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ATP synthase is the enzyme that generates ATP using the concentration gradient of hydrogen ions. It is located in the inner mitochondrial membrane and uses the energy from the flow of hydrogen ions down their concentration gradient to convert ADP and inorganic phosphate into ATP.

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Kinases add phosphate groups to proteins, activating them in cellular signaling pathways. Phosphatases remove phosphate groups, deactivating proteins. Phosphorylases break down glycogen into glucose for energy. These enzymes play key roles in regulating cellular processes through their actions on protein phosphorylation.

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Kinases are enzymes that add phosphate groups to proteins, activating or deactivating them in cellular signaling pathways. Phosphorylases, on the other hand, are enzymes that catalyze the removal of phosphate groups from proteins, regulating their activity in signaling pathways. In summary, kinases add phosphate groups while phosphorylases remove them in cellular signaling pathways.

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Kinases are enzymes that add phosphate groups to proteins, activating or deactivating them in cellular signaling pathways. Phosphorylases are enzymes that catalyze the addition of phosphate groups to molecules, often involved in energy metabolism. Phosphatases are enzymes that remove phosphate groups from molecules, reversing the actions of kinases and phosphorylases in cellular signaling pathways.

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Glycogen is broken down through a process known as glycogenolysis, which involves the breakdown of glycogen into glucose molecules. This process is mainly controlled by enzymes such as glycogen phosphorylase and glucose-6-phosphatase. The resulting glucose is then available for energy production or storage in the body.

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The enzyme amylase breaks down starch into smaller sugar molecules such as maltose and glucose. Amylase is produced in saliva as well as in the pancreas and small intestine to aid in the digestion of starch.

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The precursors of glycogenolysis include hormonal signals like glucagon and epinephrine. These hormones trigger the activation of enzymes like glycogen phosphorylase and the release of glucose stored in glycogen for energy production. Stress and low blood glucose levels also stimulate the process of glycogenolysis.

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As in most of the enzymes, to perform its reactions it is necessary to be present certain cofactors and/or ion activators. Particularly, phosphorylases need the presence of either, monovalent (M+) or bivalent (M++) ions. In order to perform an enzymatic reaction in the lab, is crucial add the proper ion, otherwise the reaction wouldn't take place. A potassium phosphate salt, very soluble in water, will release K+ ions into the solution and to act as enzyme cofactor.

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Yes, when a cell needs energy, it can break down the chemical glycogen stored in the cytoplasm to release glucose. Glucose can then enter cellular respiration pathways to produce ATP, the energy currency of the cell.

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Yes, amylase can break down glycogen.

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The hormones epinephrine and glucagon control glycogen phosphorylase which is an enzyme that breaks down glycogen into glucose.
The Insulin helps in this process ...
Insulin
Glucagon
This hormone is called 'Glucagon'.

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Glycogen is broken down into glucose through a process called glycogenolysis. This process involves the release of glucose molecules from glycogen stores by the enzyme glycogen phosphorylase. These glucose molecules can then be used by the body for energy production.

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Introduction to glycogen metabolism is the process by which glycogen, a storage form of glucose, is synthesized and broken down in the body to maintain blood glucose levels within a healthy range. Glycogen is primarily stored in the liver and muscle tissues and serves as a readily available source of energy during periods of fasting or increased energy demands. The regulation of glycogen metabolism is tightly controlled by hormones such as insulin and glucagon to ensure proper energy balance.

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  1. Amylase- breaks bonds between carbohydrate molecules.
  2. Maltase- they target the sugars maltose, sucrose, and lactose to produce monosaccharides.
  3. Elastase- targets elastase to produce short-chain peptides.
  4. Trypsin- acts on proteins and polypeptides to produce short-chain peptides.
  5. Lipase- targets triglycerides to produce fatty acids and monoglycerides.

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adh controls the volume of urine by regulating the amount of water absorbed into the convoluted tubules. . At some point ,change in blood level activates the osmoreceptors in the hypothalamus which in turn activates the release of antidiuretic hormone(ADH). ADH is released into the blood stream, then it travels to the kidney's collecting ducts whilst in the kidney, ADH increase the number of water channels in the membrane of the collecting duct cells ADH binds to the cell membrane receptors to activate phosphorylase enzyme. This causes the vesicle containing aquaporins to fuse with the membrane. Therefore water is reabsorbed from the filtrated to produce concentrated urine which passes into the tubules, collects in the renal pelvis and flows through the ureters into the urinary bladder. The reabsorbed water increases the water potential of the blood, osmoreceptors are no longer activated and so ADH production stops. This is an example of negative feedback response consequently, their removal is accompanied by an unavoidable water loss

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