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hormone that increases intracellular concentration of cAMP |
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changes conformation of catalytic site to increase affinity of enzyme for substrate |
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compounds bind to allosteric site & cause conformational change (activator or inhibitor) |
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two or more subunits w/ binding sites, one for substrate & one for activator or inhibitor |
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changes conformation of catalytic site to decrease affinity of enzyme for substrate |
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original signal activates numerous bindings, each of which in turn activates numerous bindings, each of which activates numerous bindings (and so on), with the net impact of geometrically increasing the influence of the original signal by creating a cascade effect. |
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hormonal 2nd regulatorbinds to regulatory subunits of protein kinase A |
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modulator proteinbinds to number of proteins & regulates their functions |
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turns glycogen phosphorylase b into glycogen phosphorylase a so muscles are ready w/ energy |
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regulation of certain pathways thru increased substrate (i.e. those in disposal of toxic compounds) |
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control enzyme found in liver and beta cells of pancreas to remove glucose and store as glycogen for later use |
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converted to glucose 6-phosphate through feedback inhibition, leads to glycogen synthesis or glycolysis |
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catalyzed from glucose by hexokinasewill proceed to glycolysis or glycogen synthesis |
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rate-limiting enzyme in glycogen degradationglycogen to glucose 1-phosphate |
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control enzyme found in muscle tissue that catalyzes glucose into glucose-6-phosphate, 1st step of glycolysis |
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the initial velocity of a reactionVi |
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two enzymes that catalyze the same reaction in a different manner |
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another way of stating substrate concentration at ½ Vmax |
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substrate concentration at ½ Vmaxallows us to know how enzyme will function at given substrate concentr. |
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bind to other proteins & regulate activity by conformational changes @ allosteric site |
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ester w/ phosphorous @ carbonyl carbonin glycolysis, used to store available energy in body |
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sequence of events in which one kinase phosphorylates another kinase |
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allosteric activator regulated by positive feedback system |
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decrease in rate of enzyme caused by accumulation of its own product |
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kinase enzyme that modifies other proteins by chemically adding phosphate groups to them |
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family of enzymes whose activity is dependent on level of cyclic AMP (cAMP) in cell. Has several functions in cell including regulation of glycogen, glucose and lipid metabolism. |
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enzymes that remove a phosphate group from a protein through hydrolyzing phosphoric acid monoesters into a phopshate ion and a molecule with a free hydroxyl group. (Opposite function of a kinase) |
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the process of breaking peptide bonds between amino acids in proteins. Carried out by enzymes called peptidases, proteases or proteolytiic cleavage enzymes. Proteins often undergo proteolytic cleavage before final maturation of the protein. It is irreversible. |
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relaxed state of the enzyme where allosteric activators more likely to bindsubstrates bind very well |
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Michaelis-Menten enzymes are all this type of curve (i.e. hexokinase) |
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sigmoidal curve - same as Km - substrate concentration at ½ Vmax |
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an enzyme that phosphorylates the OH group of serine or threonine. At least 125 of the 500+ human protein kinases are serine/threonine kinases. |
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molecule that is acted upon by an enzyme |
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tense or taut statedoes not bind to substrate, allosteric inhibitors more likely to bind |
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part of the complex of 3 regulatory proteins integral to muscle contraction in skeletal and cardiac muscles but not smooth muscle. Contains 4 calcium binding domains. Ca2+ binds to troponin-C which then removes inhibition between actin & myosinmuscle contracts |
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enzyme that can transfer phosphate group from ATP to a tyrosine residue in a protein |
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speed @ which reaction takes placedependent on concentration of substrate & product levels |
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maximum velocity that can be achieved @ infinite concentration of substrate |
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precursor proteins of proteasesactivated by proteolytic cleavage (i.e. chymotrypsinogen to chymotrypsin) |
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