Term
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Definition
Tissues, especially skeletal muscle, contain this -When ATP synthesis exceeds immediate needs
(high energy charge), creatine is converted to phosphocreatine. When energy is needed (e.g., for a burst of activity), phosphocreatine is used to convert ADP to ATP. Phosphocreatine has a high energy
phosphate bond (~10.3 kcal/mol). |
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Term
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Definition
One or two high-energy electrons
can be captured by FAD, forming FADH• (a free
radical) or FADH2. FADH2 is oxidized by O2 in
mitochondria to yield 1.5 ATP. |
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Term
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Definition
Two high energy electrons in the
form of hydride ion (H- = H:) can be captured by
NAD+, forming NADH. Reoxidation of NADH by O2
in mitochondria ultimately yields 2.5 ATP. |
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Term
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Definition
A central metabolic intermediate and a high
energy species that can transfer acetyl groups (CH3-C(=O)-) to other biological molecules or to
water. Other acyl groups can also be attached to CoASH to yield high energy thioesters |
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Term
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Definition
When enzymes for sequential steps are grouped so that the intermediates do not diffuse away. -Such physically associated enzymes
are called a metabolon. |
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Term
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Definition
Responsible for basal glucose uptake and are therefore found in nearly all mammalian tissues, particularly in neuronal cells and RBCs (GLUT1 only). Their Km for
glucose is 1 mM, so they are always saturated. |
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Term
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Definition
Expressed in liver, pancreatic β-cells and the basolateral side of intestinal cells. -It has a high Km for glucose (15-20 mM), which means glucose uptake will be proportional to plasma concentration. This property causes glucose uptake to increase when blood glucose levels increase. |
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Term
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Definition
Has a Km of 5 mM and transports glucose into skeletal muscle and fat cells. Insulin increases GLUT4 translocation to plasma membrane, accounting in part for the hormone’s effect on glucose uptake into those tissues. |
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Term
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Definition
Present on the apical side of small intestine cells and functions mainly for fructose uptake. |
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Term
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Definition
The sodium, glucose cotransporter (sodium/glucose permease), is expressed on the apical side of intestine cells and is responsible for glucose and galactose uptake. |
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Term
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Definition
This catalyzes the phosphorolytic cleavage of the α(1-4)
bonds of glycogen. - The enzyme works only on non-reducing ends that are > 4 residues away from a branch point. - Glycogen phosphorylase contains an active site
pyridoxal phosphate (PLP) residue that acts as a general acid-base catalyst (this is an atypical use of PLP). |
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Term
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Definition
Located on the luminal surface of the endoplasmic reticulum (ER), so G-6-P is transported out to it, and glucose is then transported back into the cytosol and
then out into the plasma. -this reaction occurs in liver, but not in skeletal muscle |
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Term
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Definition
Transfers a block of 3 glucose units from a α(1-6) branch from one outer branch to another (4-α-D-glucanotransferase activity) and (ii) hydrolyzes (no Pi) the remaining α(1-6)-linked glucose unit (α-1,6-glucosidase activity). |
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Term
Phosphofructokinase-1 (PFK-1) |
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Definition
Catalyzes the committed and rate-determining
step of the pathway -catalyzes the conversion of fructose-6-phosphate to
fructose-1,6-bisphosphate (FBP) -ATP acts as an inhibitor of the enzyme, its affect is to change the Km of the enzyme for F6P, its substrate. -Citrate, a central intermediate in the tricarboxylic acid (TCA) cycle, also serves as a feedback inhibitor in a manner similar to that of ATP -AMP, ADP, and inorganic phosphate (Pi) act as allosteric activators (signaling a need for more ATP production) by competing with ATP for binding to the allosteric ATP site.
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Term
Fructose-2,6-bisphosphate |
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Definition
Most important allosteric activator of PFK-1 -The concentration of fructose-2,6-bisphosphate is hormonally regulated by the balance between insulin and
glucagon (in the liver). -The effect of fructose-2,6-bisphosphate is to modulate the Km of PFK-1 for its substrate fructose-6-phosphate and its inhibition by ATP. |
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Term
Phosphofructokinase-2 (PFK-2) |
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Definition
This enzyme forms fructose-2,6-bisphosphate from a small amount of fructose-6-phosphate -shares a polypeptide chain with FBPase-2 -regulated allosterically by fructose-6-phosphate
and covalently by phosphorylation of a single serine residue within the regulatory domain by a protein kinase. It is activated in its unphosphorylated form |
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Term
Fructose bisphosphatase-2 (FBPase-2) |
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Definition
F-2,6,-bP broken down to fructose-6-phosphate and Pi by the action of this enzyme, which is on the same polypeptide chain as PFK-2 -activities are reciprocally regulated allosterically by fructose-6-phosphate and covalently by phosphorylation of a single serine residue within the regulatory domain
by a protein kinase. -activated in its phosphorylated form |
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Term
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Definition
Glucose is converted to a metabolically active form not recognized by GLUT transporters (G-6-P) in most cells by this kinase -occurs in several tissue-specific isoforms but all are active toward a broad range of hexose sugars have a low Km for glucose (~0.1 mM), use Mg-ATP as the true nucleotide substrate, and are inhibited by
glucose-6-phosphate (an example of product inhibition). |
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Term
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Definition
In the mitochondrion pyruvate is converted to oxaloacetate by this enzyme -an ATP dependent enzyme -used in gluconeogenesis to bypass the pyruvate kinase step of glycolysis, which is irreversible -an allosterically regulated biotin-dependent enzyme -Oxaloacetate cannot cross the mitochondrial membrane and must be reduced to malate by
mitochondrial malate dehydrogenase or converted to aspartate by aspartate aminotransferase (AAT). |
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Term
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Definition
-during gluconeogenesis, this is synthesized by pyruvate carboxylase in the mitochondira to bypass the pyrukate kinase step of glycolysis -cannot cross the mitochondrian membrane & must be reduced to malate by mitochondrial malate dehydrogenase or converted to aspartate by aspartate aminotransferase (AAT). -Once in the cytosol, malate is reoxidized to
oxaloacetate by cytosolic malate dehydrogenase or Asp is reconverted to OAA by cytosolic AAT. |
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Term
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Definition
Glucose is converted to G-6-P in liver and in pancreatic β-cells by this enzyme. -has a higher Vmax and also a higher Km for glucose than hexokinase (~10 mM). -It is not inhibited by glucose-6-phosphate.
-Glucokinase expression is increased by insulin. |
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Term
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Definition
Glycogen phosphorylase releases glucose-1-phosphate (G-1-P), but further metabolism requires glucose-6-phosphate (G-6-P). Phosphoglucomutase makes this
conversion. -also used in the synthetic process, where it converts the opposite reaction of G-6-P to G-1-P |
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Term
UDP-glucose pyrophosphorylase |
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Definition
Converts G-1-P to an activated UDP-glucose in the gluconeogenesis pathway. -utilizes a UTP to activate G-1-P -reaction is readily reversible but the reaction is driven forward by the subsequent hydrolysis of pyrophosphate by pyrophosphatase. |
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Term
Phosphoprotein phosphatase |
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Definition
Dephosphorylates pyruvate kinase in the liver to reactivate it after its phosphorylation by protein kinase. |
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Term
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Definition
Increased in liver cells by glucagon signaling. -cAMP increases which binds to the regulatory units of PKA and releases active PKA from them. -PKA then phosphorylates pyruvate kinase to inhibit glycolysis |
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Term
Glycogen Phosphorylase Regulation |
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Definition
Phosphorylase is a dimer that exists in two conformations, a T state (inactive) and an R state (active). -conformation of phosphorylase b (inactive, phosphorylated) is mostly controlled by the metabolites ATP, G6P, & AMP. It is most often in T state physiologically. -high AMP levels will convert it to the R state -phosphorylase a (active, unphosphorylated) is most often in the R state & is unresponsive to ATP & G6P physiologically. It remains in the R state unless there is a high glucose level. |
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Term
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Definition
Phosphorylation of glycogen phosphorylase is controlled by this enzyme, which is under the influence of insulin & glucagon. -glucagon stimulates phosphorylation of phosphorylase kinase, which activates it. Phosphorylase kinase then phosphorylates glycogen phosphorylase, activating it. -Ca2+ also activates this in muscle -also phosphorylates glycogen synthase, inactivating it -insulin stimulates phosphoprotein phosphatase, which dephosphorylates glycogen phosphorylase & phosphorylase kinase |
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Term
Phosphoprotein Phosphatase |
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Definition
Activated by insulin -dephosphorylates glycogen synthase & phosphorylase kinase, inactivating both -also dephosphorylates glycogen synthase, activating it |
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