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Biochemistry
Midterm 2
Term | Definition |
---|---|
Serous Secretion | alpha amylase and lysozyme |
Mucus Secretion | mucin |
Characteristics of alpha amylase | hydrolyzes alpha-1-4-glycosidic bonds in starch produces maltose and isomaltose |
Characteristics of lysozyme | anti bacterial hydrolyzes the polysaccharides in cell membranes/walls |
Digestion Sequence | gastrin, histamine, HCL, acetylcholine, pepsinogen, then pepsin |
What is pepsin | protease that hydrolyzes peptide bonds |
What is acid TAG lipase | mostly used in short and medium chain fatty acids |
Characteristics of biliary secretion | bile salt make up emulsification and gall bladder contraction stimulated by CCK |
Characteristics of pancreatic secretion | aqueous bicarbonate and pancreatic enzymes (proteases, lipases, and alpha amylase) enzyme secretion stimulated by CCK and bicarbonate secretion stimulated by secretin |
Pancreatic Enzymes | pancreatic TAG lipase, cholesterol esterase, and phospholipase |
Characteristics of pancreatic TAG lipase | hydrolyzes fatty acyl groups from the 1 and 3 positions and produces 2-monoacylglycerol activated by colipase which is activated by trypsin |
Endopeptides | trypsinogen=trypsin chymotrypsinogen=chymotrypsin proelastase=elastase |
Exopeptidases | procarboxypeptidase A=carboxypeptidase A procarboxypeptidase B=carboxypeptidase B |
Brush Border Enzymes: Disaccharide | maltose, isomaltose, lactase, sucrase, trehalase |
Brush Border Enzymes: Peptides | dipeptidases and aminopeptidases |
What is digested by your colon bacteria | oligosaccharides: GOS, FOS, and XOS |
What is excreted by you colon bacteria | short-chain fatty acids |
What is secretin | peptide hormone released by intestinal mucosa and is proteolytically activated by lowered pH |
What is CCK | cholecystokinin, peptide hormone released by intestinal mucosa |
What is colipase | secreted by the pancreas as an inactive precursor, procolipase, and is activated by trypsin proteolysis |
What maltase | hydrolyzes alpha-1-4 glycosidic bonds in maltose to get two glucose molecules |
What is isomaltase | hydrolyzes alpha-1-6 glycosidic bonds in isomaltose to get two glucose molecules |
What is lactase | hydrolyzes beta-1-4 glycosidic bonds in lactose to get galactose and glucose molecules |
What is sucrase | hydrolyzes alpha-1-beta-2 glycosidic bonds in sucrose to get fructose and glucose molecules |
What is trehalase | hydrolyzes alpha-1-alpha-1 glycosidic bonds in trehalose to get two glucose molecules |
What is dipepetidase | hydrolyzes dipeptides into pairs of amino acids |
What is aminopeptidase | cleaves N-terminal residues |
Activated by trypsin | chymotrypsinogen, proelastase, procarboxypeptidase A, and procarboxypeptidase B |
Activates trypsin | proteolytic activator: enteropeptidase=enterokinase activated trypsin can cleave trypsinogen |
Simple Sugar and Amino Acid Pathway | Enterocyte, capillaries, hepatic vein, and then liver |
Fat and Lipid Pathway | Enterocyte, reassembly, chylomicron envelopment, lymph fluid, thoracic duct, heart, subclavian artery, and then body |
Location of Sodium Dependent Transporters | intestine and kidney all else are independent/facilitated |
Insulin Sensitive Tissue | striated muscle and adipose |
What is lipoprotein lipase | complex on the surface of fat that the chylomicron docks onto and is hydrolyzes it into free fatty acids into the fat or muscles |
What is the majority of cholesterol in your blood hours after your last meal (fast) | LDL LDL (3x-5x) of HDL |
What is atherosclerosis | Oxidative damage of LDL |
When you eat carbohydrates what enters the liver | glucose, galactose, and fructose (last two kept entirely by the liver) |
When you eat proteins what enters the liver | amino acids |
What are the SGLT2 specific inhibitors | forxiga, invokana, and jardiance |
Glucokinase | found in the liver increased kcat or vmax and km when compared to hexokinase |
Hexokinase | found everywhere else decreased kcat or vmax and km when compared to hexokinase |
Which enzymes in glycolysis consume ATP | hexokinase/glucokinase and phosphofructokinase |
Which enzymes in glycolysis produce ATP | phosphoglycerate kinase and pyruvate kinase |
How do you regenerate NAD from NADH (anaerobic) | lactate dehydrogenase |
What results from pyruvate kinase deficiency | hemolytic amenia |
New mother feeds baby juice and then the baby becomes ill, what does the baby most likely have? | aldolase B deficiency |
Galactokinase Deficiency | causes elevation in blood glucose treatment is dietary restriction |
Galactosemia | GALT deficiency and accumulation of galactose 1-phosphate and galactitol |
Substrate-level Phosphorylation | the formation of ATP from ADP and a phosphorylated intermediate |
Fructosuria | lack of fructokinase |
What are the substrates of the PDH complex | pyruvate, CoA, and NAD+ |
What are the products of the PDH complex | CO2, Acetyl CoA, and NADH |
What is the classification of the PDH complex | oxidative decarboxylation |
In resting well-fed muscle what do you expect | PDH kinase to phosphorylate and inactivate the PDH complex |
In exercising muscles what do you expect | increased calcium levels to activate PDH phosphatase (dephosphorylates PDH) |
What are the five coenzymes and their vitamin deratives | TPP (B1), lipoamide, CoA (B5), FAD (B2), and NAD (B3) |
What is malate | alpha hydroxy succinate 4 carbon alpha-hydroxy carboxylic acid |
What enzyme produces NADH and CO2 | isocitrate dehydrogenase and alpha-ketoglutarate dehydrogenase |
Which enzymes produce FADH2 | succinate dehydrogenase |
Which enzymes produce NADH | malate dehydrogenase, isocitrate dehydrogenase, and alpha-ketoglutarate dehydrogenase |
Which enzymes produce CO2 | isocitrate dehydrogenase and alpha-ketoglutarate dehydrogenase |
Which enzymes produce GTP | succinate thiokinase |
ETC complexes | complex 1: NADH dehydrogenase complex 3: cytochrome bc1 complex 4: cytochrome c oxidase |
Enzymes that transport electrons | 1-3: CoQ 3-4: cytochrome c |
Pumps for NADH | 1, 3, 4 |
Pumps for FADH2 | 2, 3, 4 |
How do you regulate NAD+ | glycerol 3-P shuttle and malate shuttle |
Pentose - P Reaction | ribose-5-phosphate and NADPH |
First two dehydrogenase enzymes for Pentose - P Reaction | glucose 6-phosphate dehydrogenase and g-phosphate gluconate dehydrogenase |
A student on a mission trip taking anti-malarias passes out, what is the likely cause | glucose 6-phosphate dehydrogenase deficiency |
Second cause of hemolytic anemia | glucose 6-phosphate dehydrogenase deficiency |
Other uses of NADPH | reductive biosynthesis, cytochrome P450 reductase, steroid hormone synthesis, phagocytosis, nitric oxide synthase |
What is a porphyrin ring | 4 pyrrole rings joined through methenyl bridges |
What is heme | composed of a porphyrin ring with iron |
The enzyme that starts heme synthesis | aminolevulinic acid synthase (ALA synthase) |
ALA synthase inhibitors | high concentrations of heme iron |
What is porphyria | a group of disease that describes a deficiency in any enzyme involved in heme biosynthesis |
What is the pathophysiological explanation for porphyyria | enzyme deficiency in the heme pathway makes it so that heme doesn't accumulate to the point that it can turn off ALA synthase |
What is the process of heme breakdown | heme, biliverdin, bilirubin, conjugated bilirubin, bile secretion, colon (stercobilin) or kidney (urobilin) |
Hemolytic Jaundice | excessive red blood cell death leads to excessive bilirubin, liver normal but just needs time |
Obstructive Jaundice | gallstones blocks bile from coming out, no bile out=no bilirubin out |
Hepatocellar Jaundice | liver disease |
Neonatal Jaundice | bilirubin glucuronide enzyme not produced yet |
What form of cofactor binds oxygen in both myoglobin and hemoglobin | heme-iron 2+ |
What is the structure of myoglobin | single folded polypeptide globular structure, globular protein |
What is the structure of hemoglobin | heterotetramer dimer of heterodimers. |
What facilitates oxygen binding in the lungs | decrease proton (increased pH), decrease CO2, decrease 2,3-BPG |
What facilitates oxygen binding in the peripheral tissue | increase proton (decreased pH), increase CO2, increase 2,3-BPG |
What brings on a pain crisis | low oxygenation |
How would someone with SCD avoid a pain crisis | be well oxygenated |
Qualitative Hemoglobinopathies | sickle cell disease |
Quantitative Hemoglobinopathies | thalassemia |
T vs R Structure | T=taut R=relaxed |
What effects T-R equilibrium? Stabilizes T/facilitates O2 release | increase proton, increase CO2, increase 2,3-BPG |
FADH Complex | succinate dehydrogenase |
Oxaloactate | alpha=ketosuccinate or 4-alpha-ketodicarboxylic acid |