Wednesday, August 14, 2013

Knee Joint



Additional Links:

Phosphoglycerate Mutase

Glycolysis - (3PG) into (2PG)
Enzymes Enzymes Clinical Significance

Moves the phosphate position from 3C to 2C

Lyases
  • 3-phosphoglycerate Substrate
  • Reversible

Additional Links:

Lipid Phosphatases

Require removal of phosphoryl groups of inositol lipids that had been phosphorylated as a part of signaling

Digestive System

Organ System
Cellular Metabolism CH13

Function:

  • Digestion of biomolecules, vitamins and inorganic minerals

Components/Anatomy:

Organs/Anatomy:

Accessory Organs

Concepts:

Biomolecule Absorption

Terminology:

  • Digestion: breaking down food into progressively smaller particles and absorbed in the small intestine
  • Biomolecules

Additional Information:

Pepsin

Digestive System

Proteolytic enzyme in the stomach converting polypeptdies into oligopeptides

Hydrolases

Characteristics:

  • Optimal activity in pH 1-2

LOC:

  • Stomach

Concepts:

Additional Information:

Protease


Enzymes that degrade proteins by breaking peptide bonds

Proteins Enzymes

Protease/Peptidase/Proteinase

Function/Purpose:

Stratificaiton:

  • Serine
  • Threonin
  • Cysteine
  • Aspartate
  • Metalloprotease
  • Glutamic acid

Concepts:

Salient Examples:

Additional Information:

Stomach

Digestive System

Primary organ of digestion that chemically processes biomolecules

Stomach

Fundamentals:

Characteristics/Specs:

  • Located in the URQ
  • Capacity for 2 L
  • Gastric and pyloric glands
  • Respond to signals from the brain activated by the sight, taste and smell of food

Function/Purpose:

  • Processes biomolecules into chyme
    • Combined mechanical and chemical digestive activities INC significantly Surface area of the food particles
      • WHY? Optimize absorption
  • 1)Proteins are denatured and degredation
  • pH 1-2
  • 2)Lipids are initially emulsified

Types of Secretions:

  • Mucus

Salient Enzymes and Function Tests:

Enzymes:

  • Pepsinogen - Pepsin
    • Pepsin will digest proteins by cleaving peptide bonds near the aromatic rings resulting in short polypeptide fragments
    • pepsin which is most active at pH of 2

Stomach Function Tests and Assessment:

Anatomy:

Gross Anatomy:

  • Cardia/Cardiac/Gastroesophageal Sphincter
  • Fundus
  • Body
  • Pylorus
  • Pyloric Sphincter

Micro Anatomy:

Molecular
  • ATP dependent proton pump similar to Na K ATPase
Cellular
  • Mucus/Surface cells - secrete mucus
  • Endocrine cells/Pyloric glands - secretes Gastrin
    • Gastrin - stimulates secretion of HCl and Pepsinogen
      • Activates Parietal cells and Chief Cells
  • Gastric pits
  • Parietal cells - secretes HCl (pH 1)
    • Activates acid initially activates Pepsinogen-Pepsin:ZYM for autocatalysis
    • Prevents most known bact
  • Chief cells - secretes Pepsinogen

Concept:

  • Surface Area - MATH
  • Enzymes - Zymogens/Proenzymes

Terminology:

  • Gastric Pit: region where parietal cells and chief cells are located
  • Chyme: acidic semifluid mixture

Additional Information:


Secretin

Digestive System Small Intestine

Stimulates the pancreas to release of sodium bicarbonate

Pancreas

Secretin


Fundamnetals:

  • Stimulated by from low duodenal pH (2-4.5)
    • Also the secretion of secretin is increased by the products of protein digestion bathing the mucosa
    • Also bile salts and fatty acids
    • Oligopeptide stimulated

Function/Purpose:

  • Target organ Pancreas
    • Secrete bicarbonate
  • Enhances CCK's function

LOC:

  • Small intestine - duodenum

Additional Information:

    Secretin is a hormone that causes pancreatic juice to be excluded from the pancreas
        When hydrochloric acid passes from the stomach into the duodenum, secretin is released into the bloodstream and stimulates the acinar cells of the pancreas to secrete water and bicarbonate into the pancreatic ducts that drain into the duodenum. By this mechanism, hydrochloric acid secreted by the stomach, which can be damaging to the intestinal lining, is promptly diluted and neutralized. Secretin also inhibits the secretion of gastrin, which triggers the initial release of hydrochloric acid into the stomach, and delays gastric emptying.
''Molecular basis''
    Secretin increases watery bicarbonate solution from pancreatic duct epithelium. Pancreatic acinar cells have secretin receptors in their plasma membrane. As secretin binds to these receptors, it stimulates adenylate cyclase activity and converts ATP to cyclic AMP. Cyclic AMP acts as second messenger in intracellular signal transduction and leads to increase in release of watery carbonate. It is known to promote the normal growth and maintenance of the pancreas.
    It counteracts blood glucose concentration spikes by triggering increased insulin release from pancreas, following oral glucose intake.
  
    Although secretin releases gastrin from gastrinomas, it inhibits gastrin release from the normal stomach. It reduces acid secretion from the stomach by inhibiting gastrin release from G cells. This helps neutralize the pH of the digestive products entering the duodenum from the stomach, as digestive enzymes from the pancreas (e.g., pancreatic amylase and pancreatic lipase) function optimally at slightly basic pH.[citation needed]
    In addition, secretin stimulates pepsin secretion from chief cells, which can help break down proteins in food digestion. It also stimulates release of glucagon, pancreatic polypeptide and somatostatin.

Small Intestine

Digestive System

Secretes chemicals and primary location of absorbing biomolecules

Small Intestine

Fundamentals:=

  • Bulk of chemical digestion
  • Chemicals (Intest&Panc) are the key to proper digestion and absorption
  • Important in mechanical digestion of lipids

Function/Purpose:

  • Biomolecule Absorption
  • Secretion of CCK
  • Biomolecule Synthesis
    • Lipid resynthesis of triacylglycerides from fatty acids and monoacylglycerols

Salient Enzymes and Function Tests:

Enzymes:

  • Enteropeptidase/Enterokinase/Master Switch
    • Activates trypsiogen and trypsin
Enterogastrones - slow the movement of chime and allow a greater time to digest the fat
Disaccharidases
  • Maltase - converts maltose into glucose
    • Surface of intestinal cells
  • alpha-Glucosidase - digests maltotriose and other oligosaccharides
    • Surface of intestinal cells
  • Sucrase - digests sucrose (GLU and FRU) disaccharide
    • Surface of intestinal cells
  • Lactase - converts lactose into GAL and GLU
Peptidases
  • Dipeptidase - cleave the peptide bond of dipeptides to release the AA’s

Stomach Function Tests and Assessment:

Anatomy:

Gross Anatomy:

  • Duodenum - most digestion occurs
  • Illeum
  • Jejunum

Micro Anatomy:

  • Inner Wall
    • Villi
      • Microvilli
  • Epithelial Cells
  • Blood Vessels
  • Lymphatics
  • Circular Muscle
  • Longitudinal Muscle
  • Smooth Muscle

Regulation:

  • PNS-ANS inhibits the digestion

Concept:

Terminology:

  • Peristalisis: quick and unconscious gastrointestinal contractions of Smooth Muscle

Additional Information:


Cholecystokinin

Digestive System - Small Intestine

Stimulates pancreas and gall bladder to secrete digestive enyzmes and bile salts

Pancreas Gall Bladder

Cholecystokinin (CKK)/Gastrin

  • Clincal values

Function/Purpose:

  • Stimulated by initial digestion products in stomach

Tissue source:

Diagnostic significance:

Assay for enzyme activity:

Source of error:

Additional Information:

Zymogens

[[Enzymes]]

==Precursors of enzymes==

====Function/Purpose:====
====Salient Examples:====
*[[Pepsinogen]]
*[[Chymotrypsinogen]]
*[[Trypsinogen]]
*[[Procarboxypeptidase]]
*[[Proelastase]]
====Additional Information:====

Pepsinogen

Cellular Metabolism

Zymogen of Pepsin

Pepsin

Pepsinogen

  • Clinical values

Function/Purpose:

  • Small amount of enyzme activity to activate itself to some degree in acidic environment

Tissue source:

Diagnostic significance:

Assay for enzyme activity:

Source of error:

] Temp: ENZ

simplefunction

((links))

Name

  • Clincal values

Function/Purpose:

  • Substrate
  • Product

Salient Information:

Tissue Source:

Regulation:=

Clinical Significance:

Chemistry of Enzyme:

Assay Source of error:

Additional Information:

] Temp: Organ

Medical Science - back

asdf

links

Organ

Function/Purpose:

Salient Enzymes and Function Tests:

Enzymes:

Organ Function Tests and Assessment:

Anatomy:

Gross Anatomy:

Micro Anatomy:

Concept:

Additional Information:

Enteropeptidase

Enzymes
Digestive System

Enteropeptidase/Enterokinase

  • Clincal values

Function/Purpose:

Tissue source:

Diagnostic significance:

Assay for enzyme activity:

Source of error:

Additional Information:

Trypsin

Digestive System

Along with Enteropeptidase, activates Trypsinogen to form Trypsin

Trypsinogen

Trypsin

  • Clincal values

Function/Purpose:

  • Master switch of the pancreatic zymogens

Tissue source:

Diagnostic significance:

Assay for enzyme activity:

Source of error:

Additional Information:

Gall Bladder

Digestive System


Secretes bile salts produced in the liver

Liver

Function/Purpose:

Salient Enzymes and Function Tests:

Enzymes:

Organ Function Tests and Assessment:

Anatomy:

Gross Anatomy:

Micro Anatomy:

Concept:

Diseases:

Procedures:

Additional Information:

Snake Venom Poisoning

ConditionsDiseases List

Snake Venom Poisoning

Fundamentals:

  • 50-60 proteins that vary from species to species
    • Enzymes that digest cell membranes
  • EX: Phospholipases
  • Brake phospholipids and destroy phospholipids of skeletal muscles exposing insides of cells
    • ER, mitochondria, nuc env membrane, plasma membrane all contain phospholipids
  • Target the RBCs = hemolysis
  • EX: Collagenases
  • Digest collagen - connective tissue
  • EX: hyaluronidase
  • DIgest glycosaminoglycan - connective tissue
  • Both destroy tissue at the site of the bite enabling the venom to spread more readily throughout the victim
  • EX: Proteases
  • Degrade basement membranes and components of extracellular matrix = severe tissue damage
  • Stimulate formation of blood clotts as well as digest blood clots
  • Neurotoxic activities
    • Immobilize prey while the digestive enzymes take effect

Concepts:

Additional Information:

Med School

So here is the start of yet another project...

Essay Samples

Medical Schools

United States
  • Allopathic Medicine - MD
    • Roughly 130+ schools
  • Osteopathic Medicine - DO
    • Roughly 30 schools
bygons be bygons
FYI DO NOT BOTHER APPYING TO PUERTORICAN SCHOOLS
  • They maybe cheap but that's because of their preference for PR residents
Example #1 University of San Juan - From Gladys H. Gonzalez Navarrete MD JD
  • pic comming soon
  • "We appreciate your interest in our school, however, we must inform you that as a state-supported school, priority is given to residents of Puerto Rico. Due to this fact, we are unable to consider your application."
    • Does not specify any out of state slots in the letter, will have to dig the MSAR.
    • It states a "mr/NonResRejCta" in the very bottom of the letter so im not sure if there is a "mr/NonResAccCta" for acceptances but thats my 2 cents
Canada
 
Carribean/Mexico
Philippines
  • http://www.iime.org/database/pacific/philippines.htm
  • http://www.upcm.ph/2007/admission.html -UP
  • http://officialweb.upm.edu.ph/schoolsandcolleges.php
  • http://www.flinders.edu.au/medicine/sites/medical-course/international-applicants/
  • http://www.internationaldoc.com/
  • http://nmatfordummies.blogspot.com/2010/03/frequently-asked-questions.html
http://www.mededpath.org/faq.php

Australia
 
United Kingdom
  • - uk schools
  • [1]
  • http://www.google.com/#sclient=psy&hl=en&q=admissions+test+BMAT&aq=f&aqi=g-m1g-v1&aql=&oq=&pbx=1&bav=on.1,or.&fp=6ec3191c2b79d4d0
  • http://www.ucl.ac.uk/medicalschool/mbbs-admissions
  • http://www.ukcat.ac.uk/
  • http://www.ukcat.ac.uk/pages/details.aspx?page=ukCatUniversities
  • http://www.iime.org/database/europe/uk.htm

Regulation of Enzymes

Enzymes - back

Molecular perspective in the involuntary control of our biological catalysts

Regulation of Enzymes

Fundamentals

  • Enzymes produce a product

Types of Inhibition:

Reversible Covalent Modificaiton
Irreversible
  • Suicide Inhibition
  • Transition State Analog

Concepts:

  • Bufers - Chemistry
The energy charge of most cells ranges form .8 to .95

Regulation of Metabolism

Cell Metabolism

Involuntary control of our body's energy functions

Regulation of Metabolism:

Function/Purpose:

  • Products or reactants need to be in balance for our well being

Types of Regulation:

Coupled Reaction
  • a spontaneous reaction provides the energy needed by a nonspontaneous one
Regulation of Enzymes
Compartamentalizaiton
  • Hormonal
  • Segregates opposed reactions
Energy Status
  • Energy Charge - ADP Buffer
    • (ATP + .5ADP)/(ATP + ADP + AMP)
      • 1= all ATP
      • 0= all AMP
  • Phosphorylation Potential
    • ATP/(ADP + Pi)
THINK Buffers Human Buffers Buffered like pH, ATP fluctuates
Controling Flux

Concepts:

Additional Information:

Cell Metabolism

Cellular Metabolism - CH14

The body's involuntary functions of vital energy reactions (anabolism and catabolism)

  • Daily reactions we take for granted but necessary to function properly

Fundamentals:

Regulation of Metabolism

General Types of Pathways

  • Linear: continuous series of reactions in which the product of one reaction is the reactant in the next
  • Circular: series of reactions where the final product is an initial reactant
  • Spiral: series of repeated reactions used to break down or build up a molecule

Biomolecule Metabolism/Intermediary/Central Metabolism:

Complex Carbohydrate Metabolism
Carbohydrate Metabolism
Amino Acid Metabolism
Nucelotide Metabolism
Complex Lipid Metabolism
Lipid Metabolism
Energy Metabolism
Cofactor Vitamin Metabolism
Other Amino Acid Metabolism
Other Substances Metabolism

Concepts:

Terminology:

  • Orthophosphate
  • Anabolism: build up of chemicals to synthesize new products
  • Catabolism: breakdown of chemicals to degrade into new products
  • Intermediary/Central Metabolism: discrete pathways of one function

Additional Information:

GLC t G6P

Glycolysis

Glucose + ATP <-(Hexokinase)->>> Glucose 6-phosphate + ADP + H

Hexokinase

Fundamentals:

  • Glucose is transported by specific transport proteins into the cell
  • Glucose is phosphorylated by ATP to form Glucose 6-phosphate
    • Phosphorylation changes polarity of glucose
      • keeps the molecule inside the cell, does now allow the passage out of the membrane
    • Phosphoryl groups destabilize glucose
      • sets up an isomerization of the 6C structure

Specifics

  • Hexokinase has two lobes that move toward each other
  • Removal of water form the active site enhances the specificity of the enzyme
  • Binding site could attack the gamma phosphoryl group of ATP forming ADP and Pi

Hexokinase

Glycolysis - GLC into (G-6P)

Phosphorylates glucose

Transferases

Hexokinase

  • Requires Mg
  • Glucose substate
  • Reversible reaction (favors product)
  • Requires ATP

Additional Information:

G6P t F6P

Glycolysis

Glucose 6-phosphate <-(Phosphoglucose isomerase)-> Fructose 6-phosphate

Phosphoglucose isomerase

Fundamentals:

  • Glucose (aldose) is changed into Fructose (ketose)
    • Only three carbon molecuels are metabolized and this makes it easier to cleave into the 3C fragments
Entry Points

Specifics

  • Galactose is funelled through this step in Glycolysis

Additional Information:

G6P t F1,6BP

[[Glycolysis]]

==Glucose 6-phosphate <-(Phosphoglucose isomerase)-> Fructose 1-6-bisphosphate==
[[Phosphoglucose isomerase]]
====Fundamentals:====
*Glucose (aldose) is changed into Fructose (ketose)
**Only three carbon molecuels are metabolized and this makes it easier to cleave into the 3C fragments
====Specifics====

PG Iase

Glycolysis - (G-6P) into (F-6P)

Isomerizes phosphoglucose

Isomerases

Phosphoglucose Isomerase

Fundamentals:

Additional Information:

GLC t G6P

[[Glycolysis]]

==Glucose + ATP <-(Hexokinase)-> Glucose 6-phosphate + ADP + H==
[[Hexokinase]]
====Fundamentals:====
*Glucose is transported by specific transport proteins into the cell
*Glucose is phosphorylated by ATP to form Glucose 6-phosphate
**Phosphorylation changes polarity of glucose
***keeps the molecule inside the cell, does now allow the passage out of the membrane
**Phosphoryl groups destabilize glucose
====Specifics====
*Hexokinase has two lobes that move toward each other
*Removal of water form the active site enhances the specificity of the enzyme
*Binding site could attack the gamma phosphoryl group of ATP forming ADP and Pi

G6P t F1,6BP

[[Glycolysis]]

==Glucose 6-phosphate <-(Phosphoglucose isomerase)-> Fructose 1-6-bisphosphate==
[[Phosphoglucose isomerase]]
====Fundamentals:====
*Glucose (aldose) is changed into Fructose (ketose)
**Only three carbon molecuels are metabolized and this makes it easier to cleave into the 3C fragments
====Specifics====
====Additional Information:====
*[http://en.wikipedia.org/wiki/Fructose_1,6-bisphosphate Wikipedia]

PFKase

Glycolysis - (F-6P) into (F-1,6BP)

Phosphorylates fructose

Transferases

Phosphofructokinase (PFK)

KEY ENZYME IN GLYCOLYSIS

  • Requires Mg or Mn?
  • Fructose 6-phosphate Substate
  • Reversible reaction (favors product)
  • Requires ATP
  • Allosteric enzyme

Concepts:

Additional Information:

F6P t F1,6BP

Glycolysis

Fructose 6-phosphate + ATP <-(Phosphofructokinase)->>> Fructose 1-6-bisphosphate + ADP + Pi

Phosphofructokinase (PFK)

Fundamentals:

  • ATP required
    • This addition of another ATP sets up enough energy to allow to cleave the 6C structure
Entry Points

Specifics

Additional Information:

F1,6BP t GAP + DHAP

Glycolysis

Fuctose 1,6-bisphosphate <-(Aldolase A)-> Glyceraldehyde 3-phosphate and Dihydroxyacetone phosphate

Aldolase A

Fundamentals:

  • Reverse Aldol Reaction - OCHM!

Concepts:

  • Aldol Chemistry]] - OCHM

Specifics:

Aldolase

Glycolysis - (F-1,6BP) into (GAP) + (DHAP)
Enzymes

Cleaves aldols

Lyases

Aldolase

  • Fructose 1,6-bisphosphate Subtrate
  • Reversible

Types:

  • Aldolase A, B, C

Aldolase A

Aldolase B

Additional Information:

DHAP t GAP

Glycolysis

Dihydroxyacetone phosphase <-(Triose phospahte isomerase)-> Glyceraldehyde 3-phosphate

Triose phosphate isomerase

3PIase

Glycolysis - (DHAP) into (GAP)

Converts the three sugar ketose into an aldose

Isomerases

Triose phosphate isomerase (TPI/TIM)

  • Dihydroxyacetone phosphate Substatrate
  • Reversible

GAP t 1,3BPG

Glycolysis - Gluconeogenesis


Glyceraldehyde 3-phosphate + NAD <-(Glyceraldehyde 3-phosphate dehydrogenase)-> 1,3,bisphosphoglycerate + NADH + H

Glyceraldehyde 3-phosphate dehydrogenase (GAPDH)

General:

  • Aldehyde is oxidized to COOH
  • COOH is phosphorylated as NAD is reduced
  • This sets up the molecule to generate ATP
    • Unfavorable formation of a mixedanhydride - phosphorylated carboxylic acid

Specifics:


GA3PDHase

Glycolysis - (GAP) into (1,3BPG)
Enzymes - Enzymes Clinical Significance

Oxidizes Glyceraldehyde 3-phosphate

Oxidoreductases

Glyceraldehyde 3-phosphate dehydrogenase (GAPDH)

  • Glyceraldehyde 3-phosphateSubstrate
  • Needs NAD+
  • Reversible
  • Product has a high phosphoryl transfer potential
    • Mixed anhydride of phosphoric acid and carboxilic acid

Coupled RXN Specifics:

  • Oxidation of aldehyde to COOH by NAD
    • Farovarble dG(o') -50kJ
Thioester Intermediate - more stable than reactant but less stable tha product
  • Joining of COOH and orthophosphate to form acyl-phosphate product
    • Unfavorable

Concepts:

Additional Links:

Oxidoreductases

[[Enzymes]] - back

==catalyze an oxidation reduction between two substrates==

==EC1: Oxidoreductases==

====Salient Examples:====
*[[Drug Metabolizing Enzymes]] Cytochrome P450
*[[(GAPDH)]]

Orthophosphate

Cell Metabolism

Pi/Inorganic phosphate/Orthophosphate

1,3BPG t 3PG

Glycolysis

1,3-bisphosphoglycerate <-(Phosphoglycerate Kinase)-> 3-phosphoglycerate

Phosphoglycerate Kinase

Phosphoglycerate Kinase

Glycolysis - (1,3BPG) into (3PG)
Enzymes

Dephosphorylates 1,3BPG and creates ATP

Transferases
  • 1,3-bishposphoglycerate Substrate
  • Reversible
  • Creates ATP
  • Substrate level phosphorylation

Additional Links:

Pyruvate Decarboxylation

Cell Metabolism

Combustion of pyruvate into Acetyl-CoA


LOC:

Summary:

  • Pyruvate + CoA into AcCoa
    • Pyruvic acid + Coenzyme A into Acetyl-CoA
      • Requires NAD
      • Produces CO2 and NADH

Steps:

  • Pyruvate is brought into the mitochondrial matrix
    • Transporter protein
      • Commits pyruvate to become Acetyl-CoA
  • Pyruvate Dehydrogenase Complex (3 enzymes + 5 coenzymes)

3PG to 2PG

Glycolysis - Gluconeogenesis
Phosphoglycerate Mutase

3-phosphoglycerate <-(Phosphoglycerate Mutase)-> 2-phosphoglycerate

Glycolysis

2-phosphoglycerate <-Phosphoglycerate Mutase)-> 3-phosphoglycerate

Gluconeogenesis

Mechanism:

General
  • Phosphorylation and dephosphorylation
    • NOT an intermolecular attack of the alcohol with the phosphate
      • WHY? - educated guesses
        • Enzyme holds the molecue at a particular shape
        • Enzyme has an affinity = rate that revents intermolecular attack
        • Steric hindrance of the 2O(-)s means that there is an extra electron (6 total) repelling
          • Environment is slighlty basic pH of 7.3-ish so this allows the Os on the phoshate to remain deprotonated
          • To me since there is resonance, it seems like the steric hindrance is further intensified by the "swatting" of the O atom as it converts from a singe tetrahedral configuration to a planar carbonyl.
            • Imagine that the three Os are all in resonance periodically "swatting" away the chances for an intermolecular attack
            • MAYBE the concept of a feris wheel and mini golf put puts
              • each O as it swats away the chance of OH intermolecular attack

PGate Mase

Glycolysis - (3PG) into (2PG)
Enzymes Enzymes Clinical Significance

Moves the phosphate position from 3C to 2C

Lyases
  • 3-phosphoglycerate Substrate
  • Reversible

Additional Links:

Enolase

Glycolysis - (2PG) into (PEP)
Enzymes Enzymes Clinical Significance

Dehydrates to 3C to form a double bond or the enol of the soon to be keto

Lyases
  • 2-phosphoglycerate Substrate
  • Reversible

Additional Information:

2PG t PEP

Glycolysis - Gluconeogenesis
Enolase

2-phosphoglycerate <-(Enolase)-> phosphoenolpyruvate

Glycolysis

Phosphoenolpyruvate <-(Enolase)-> 2-phosphoglycerate

Gluconeogenesis

Details:

  • Phosphoryl traps PEP in its unstable enol form

OAA t PEP

Gluconeogenesis
  • Addition of phosphoryl group is highly unfavorable, Glycolysis
  • Carboxylation and decarboxylation are much more favorable, Gluconeogenesis
    • Decarboxylations often drive reactions that are otherwise highly endergonic

Heme Synthesis

Glycine and Succinyl-CoA to create heme

Mitochondria, Cytoplasm


  • Alanine (5-aminolaevulinic acid) synthesis – Glycine and Succinyl-CoA condensation
    • Alanine Synthase – controls of porphyrins and heme synthesis rate, controlling enzyme
  • Porphobilinogen (PBG) subunit synthesis – Two alanines combine to form monopyrrole ring PBG
  • Hydroxymethylbilane synthesis – Four PBGs combine to form linear tetrapyrrole—four monopyrroles strung together end to end
“The open section on the left of the structure above – where two pyrrole rings lie adjacent to each other but not joined—is then closed, producing a tetrapyrrole ring. This produces the first porphyrin on the pathway, uroporphyrinogen. This step is catalysed by uroporphyrinogen lll cosynthase, which also tweaks the ring into a particular orientation called the lll isomer. This enzyme is defective in congenital erythropoietic protoporphyria.  

Uroporphyrinogen lll Four of the carboxylic acid side chains (COOH) are successively knocked off by the enzyme uroporphyrinogen decarboxylase (UROD), producing the heptacarboxylic, hexacarboxylic and pentacarboxylic porphyrinogen intermediates (not shown), ending in coproporphyrinogen lll. This enzyme is defective in porphyria cutanea tarda (PCT).  

Coproporphyrinogen lll A further two carboxylic acid side chains are knocked off by the enzyme coproporphyrinogen oxidase, which is defective in hereditary coproporphyria (HCP).  

Protoporphyrinogen lX This molecule is then oxidised from protoporphyrinogen lX to protoporphyrin lX by the enzyme protoporphyrinogen oxidase, which is defective in variegate porphyria.  

Protoporphyrin lX An iron atom (Fe2+) is inserted into the centre of the tetrapyrrole ring to form heme. This is catalysed by the enzyme ferrochelatase, which is defective in erythropoietic protoporphyria.  

HEME BREAKDOWN

The tetrapyrrole ring is broken open (See the gap between the O atoms at the top of the structure below).

This step is catalysed by the enzyme heme oxygenase.  

Biliverdin This is further reduced to bilirubin by the enzyme biliverdin reductase  

Bilirubin Bilirubin is the form in which the breakdown products of heme are excreted from the body: in the bowel, it is further broken down to urobilinogen and stercobilinogen by bacteria.” – from additional info Capetown

Salient Chemicals:

  • Glycine
  • Succinyl-CoA
  • Alanine synthase
  • Alanine


Additional Information:

Tuesday, August 13, 2013

PEP t Pyruvate

Glycolysis

Phosphoneolpyruvate + ADP <-(Pyruvate Kinase)->Pyuvate + ATP

Pyruvate KinasePyruvate

Additional Information:

Pyruvate Kinase

Transfers Pi from sugar to ATP

Glycolysis - (2PG) into (PEP)
Enzymes Enzymes Clinical Significance
Kinases
  • Phosphoenolpyruvate Substrate
  • Ireversible

Additional Information:

Pyruvate

Pyruvate/Pyruvic Acid


Cell Metabolism

Function/Purpose:

  • Variable and verastile compound

Fundamentals:

Fate of pyruvate is variable:

Concepts:

Terminology:

  • Fermentations are ATP generating process in which organic compounds act as both donors and acceptors of electrons

FRU 1P Path

Fructose 1-phosphate Pathway

Conversion of Fructose in the liver to be metabolized by Glycolysis


Liver
Fructose

Glycolysis


  • Fructose into Fructose 1-phosphate
  • Fructose 1-phosphate into 1)Dihydroxyacetone Phosphate (DHAP) and 2)Glyceradehyde
    • Fructose 1-phosphate Aldolase/Aldolase B
    • Mechanism is via the formation of a Schiff Base
  • 2)Glyceraldehyde into Glyceraldehyde 3-phosphate

Concepts:

FRU

Fructose

Ketose sugar


Carbohydrates - Carbohydrate List
Cell Metabolism

Fructose Metabolism:

Additional Information:

GAL

Galactose

Aldose sugar

Carbohydrates - Carbohydrate List
Cell Metabolism


Galactose Metabolism:

Conditions/Diseases:

Additional Information:

GAL-GLC Int Path

Galactose

Galatcose-Glycose Interconversion Pathway:

Specifics:

Note that UDP-GLC is regenerated

Lactase

Beta galactosidase of Lactose (GLU and GAL) disaccharide

Small Intestine
Lactose
Hydrolases

Specifics:

  • Lactase activity normally declines to 5-10% of what it was at birth

LOC:

  • Surface of intestinal cells

Terminology:

  • Beta galactosidase - cleaves the beta bond between GLC and GAL

Diseases/Conditions:

Lactose Intolerance

Lactose Intolerance/Hypolactasia

Deficiency in lactase


Carbohydrates - Lactose
ConditionsDiseases List

Fundamentals:

  • Lactose is good energy source for intestinal flora
    • Anaerobic fermenters
  • Lactate is produced by these microorganisms
    • Lactate draws water into the intestine as well as lactose
      • Sufficient accumulation of water = diarrhea
  • Severe accumulation hinders the absorption of other nutrients

Treatment:

  • Avoid consumption of lactose
  • Adding lactase to milk products

Carbohydrate List

Pertinent Carbohydrates
Monosaccharides
Disaccharide
Polysaccharides

Glucose

Carbohydrates - Carbohydrate List

Cell Metabolism

Ketose sugar

Funciton/Purpose

  • Glucose is vital to certain organs that do not have the equipment to create glucose

Vital LOC:

  • Brain - no gluconeogenesis but has mitochondria
  • Skeletal muscle
  • Red blood cells - no mitochondria

Glucose Metabolism:

Catabolism
Anabolism
Interlinking Pathways

Conditions/Diseases:

Additional Information:

Conditions and Disease List

Medical Science

As it gets populated it will be further segregated into organ systems. It will be sweet, promise. 

Additional Information:

] Temp: Conditions & Diseases

ConditionsDiseases List

ConDis

desc
  • Frequency

Fundamentals:


LOC:


Causes:


1)Genetic:


2)Pathogenic:


3)Biochemical:


4)Anatomical:


Route Of Transmission ROT:


Pathogenesis:


1)Genetic:


2)Pathogenic:


3)Biochemical:


4)Anatomical:


Symptoms:


Diagnosis:


Treatment:


Prevention:


Additional Information:

Diabetes

ConditionsDiseases List
  • Two Main Types:
Type 1: insulin deficiency - insulin dependent
Type 2: insulin resistance - insulin nondependent

Causes:

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Genetic:

Route Of Transmission ROT:

LOC:

Pathogenesis:

Type 2
  • Insulin fails to inhibit the expression of a gene that encodes PEPCK and other genes of gluconeogenesis
    • Increased output for glucose by the liver
  • Without treatment type 2 may progress to type 1

Symptoms:

  • Excessive thirst
  • Frequent urination
  • Blurred vision
  • Fatigue
  • Frequent/slow healing infections
Type 2
  • Hyperglycemia

Diagnosis:

Treatment:

  • Weight loss
  • Healthy diet
  • Exercise
  • Drug treatment
    • enhance sensitivity to insulin

Prevention:

Additional Information:

Galactosemia

ConditionsDiseases List
  • Disruption of galactose metabolism
    • Deficiency in galactose 1-phosphate uridyl transferase activity

Causes:

Genetic:

Route Of Transmission ROT:

LOC:

Pathogenesis:

Symptoms:

  • Vomit or diarrhea after consuming milk
  • Hepatomegaly
  • Jaundice
  • Cirrhosis
  • Cataracts
  • Lethargy
  • Retarded mental development
  • Blood galactose elevated
  • Galactose in urine

Diagnosis:

  • Absence of transferase in red blood cells

Treatment:

  • Remove galactose from the diet
    • Prevents liver disease and cataract development
    • BUT CNS malfunction/delayed acquisition of language skills
      • Females = ovarian failurs

Prevention:

Additional Information:

Cataracts

ConditionsDiseases List

crystaline lens/anterior chamber becomes opaque decreasing vision

Fundamentals:

  • Clouding of the normally clear lens of the eye
    • If galactose 1-phosphate uridyl transferase is not active
    • Aldose reductase converts Galactose into Galactitol
      • Galactitol is osmotically active, water will difffuse into the lens forming cataracts

Causes:

  • Aging process
  • Trauma
  • Glaucoma
  • Medications

Genetic:

Route Of Transmission ROT:

LOC:

Pathogenesis:

Symptoms:

Diagnosis:

Treatment:

Prevention:

  • Milk Moderation: NOTE THERE IS A HIGH INCIDENCE OF CATARAC FORMATION WITH AGE POPULATIONS THAT CONSUME SUBSTANTIAL AMOUNTS OF MILK INTO ADULTHOOD
    • Too much of ANYTHING IS BAD theory 

Additional Information:

Glycerol

Cell Metabolism

Glycerol Metabolism

Glycolytic and Gluconeogenic Pathway Glycolysis,Gluconeogenesis
Links with DAH Glycolytic/Gluconeogenic Enzyme

Additional Information: