Biology and Biochemistry Flashcards
competitive inhibition
binding site: active site
impact on Km: increases
impact on Vmax: none
*can be overcome by increasing the substrate concentration, so Km will increase (more substrate needed to reach 1/2 Vmax)
noncompetitive inhibition
binding site: allosteric site
impact on Km: no change
*active enzyme still has same affinity for substrate
impact on Vmax: decreases
*less enzyme available to react due to allosteric site
mixed inhibition
binding site: allosteric site
impact on Km: increases or decreases
impact on Vmax: decreases
uncompetitive enzyme
binding site: enzyme-substrate complex
impact on Km: decreases
impact on Vmax: decreases
catalytic efficiency
kcat/Km
lower Km means
higher enzyme affinity for a substrate
order of circulation
superior and inferior vena cava right atrium (tricuspid valve) right ventricle pulmonary arteries lungs pulmonary veins left atrium (bicuspid/mitral valve) left ventricle aorta body
blood buffer equation
CO2 + H2O ⇌ H2CO3 ⇌ H+ + HCO3-
veins
carry blood low in oxygen to the heart
arteries
carry oxygen rich blood to body
Vmax is limited
if all active sites of enzyme are occupied, adding more substrate does not increase the reaction rate
prokaryote cell wall (gram positive or gram negative)
gram positive –> purple : thick layer of peptidoglycan
gram negative –> pink/red : thin, less peptidoglycan
plasmids
carry DNA that is no necessary for the survival of prokaryote
binary fission
asexual reproduction in prokaryotes
genetic recombination
transformation, transduction, and conjugation
integration DNA into genome
-antibiotic resistance
-virulence factors
transformation
integration of foreign genetic material into the host genome
gram negative rods
conjugation
2 cells form a conjugation bridge to transfer genetic material donor male (+) and recipient female (-)
transduction
virus transfers genetic material from one bacterium to another
ex: bacteriophages
viruses
DNA or RNA
do not have the ribosomes
must express and replication genetic info within the host cell
bacteriophages
viruses that target bacteria by injecting their genetic material
positive sense
genome may be directly translated to functional proteins by ribosomes of host cell (like mRNA)
negative sense
template
*carry RNA replicase so complementary strand can be synthesized
retroviruses
single stranded RNA viruses
reverse transcriptase –> synthesizes DNA from SS RNA –> integrated into host genome –> replicated and transcribed
lytic life cycle
virulent
maximize cell’s functions, no regard for host cell survival
lysogenic cycle
viral genes integrated into host genome
prion
infectious protein
causes misfolding of protein
viroids
small pathogens with short circular SS RNA
no protein
glucogenic amino acid
all but leucine and lysine
can be converted into glucose through gluconeogenesis
ketogenic amino acids
leucine, lysine, isoleucine, phenylalanine, threonine, tryptophan, tyrosine
converted into acetyl CoA and ketone bodies
ketone bodies
transportable forms of acetyl CoA
produced by liver
used by other tissues during prolonged starvation
ketolysis
breakdown of ketone bodies
when: during prolonged fast (brain!!)
(pyruvate dehydrogenase is inhibited so glycolysis and glucose uptake decreases to spare essential proteins)
acetyl CoA and oxaloacetate form …
citrate
when: beginning of citric acid cycle
Beta oxidation
reverse of fatty acid synthesis
*oxidizing and releasing molecules of acetyl CoA
each 4 step cycle releases 1 acetyl CoA and reduces NAD+ and FAD
importance of acetyl CoA (B oxidation producing it)
- it enters the citric acid cycle in muscle
- in the liver, it stimulates gluconeogenesis by activating pyruvate carboxylase
- use it to synthesize ketone bodies
types of enzymes
LIL’ HOT
Lyase
Isomerase
Ligase
Hydrolase
Oxidoreductase
Transferase
lyases
cleavage of single molecule into two products
NO WATER
isomerases
rearrangement of bonds
ligases
addition or synthesis reactions, requires ATP
hydrolase
breaking with water
phosphatase, cleaves phosphate group
oxidoreductase
redox reactions
“dehydrogenase”