least
Compounds that are the most oxidized have the _____ energy
catabolism
reactions which breakdown complex molecules into simpler ones, usually done to release energy for work (respiration)
anabolsim
reactions which use simpler molecules to build more complex ones, usually require an input of energy (photosythesis)
multiple steps
cells do not have an effective means of transforming and storing an explosive amount to energy, so metabolims is done in _____
most
Compounds that are reduced have the _____ energy
activation energy, we capture energy, step regulation
Animal cells do not combust because_____
cAMP
formed by ATP activation of epinephrine or glucagon, activates a PKA
PKA
Turns glycogen synthase off and phosphorylase on
insulin
Bonds to its receptors to produce PDE, which deactivates cAMP
glycolysis
Occurs in cytoplasm, doesn’t require oxygen, starting pathway in all organisms, produces little ALP
glycolysis
Is very thermodynamically favorable due to large negative G and [reactants] >>> [products]
phosphofructokinase
uses ATP to catalyze the conversion of fructose-6-phosphate to fructose-1,6-bisphosphate by adding a phosphate in step 3, ends energy investment phase
TCA/Kreb’s/citric acid
Occurs in mitochondria, requires oxygen indirectly, ATP from GTP
hexokinase
uses ATP convert glucose and remove it from the reactant pool in the 1st step of glycolysis
NAD+
Important cofactor/coenzyme that accepts electrons and becoms reduced, adds a 2nd phosphate in glycolysis
allosteric activator
binds to a site on an enzyme other than the active site, typically sensitive indicators of the cells needs.
allosteric inhibitor
binds to a site on an enzyme other than the active site, typically downstream products
pyruvate kinase
makes the product 2 ATP and 2 pyruvate in the 10th step of glycolysis
anarobic metabolism
another word for fermentation, occurs in the cytosol, returns NADH to NAD+ which is recycled in the glycolysis pathway
High NAD+
_____ = low energy
Low NAD+
____ = high energy
electron transport chain
glucose, pyruvate
Glycolysis starts with _____ and ends with ………
outer
the _____ membrane of the mitochondria is more permeable, a 1:1 protein:lipid ratio, and is homologous to bacterial membranes
inner
the _____ membrane of the mitochondria is less permeable, 3:1 protein:lipid ratio, and required special transport proteins
water
a pH gradient inside of the mitochondria is maintained by _____ and used to bring H+ ions inside to produce ATP
ubiquinone
small, mobile, carbon ring, e- transporter, lipid-soluble, travels by lateral diffusion in the lipid bilayer, accepts/donates 2 H+ and 2 e- from complex I or II
oxygen
terminal electron acceptor (highest affinity) in aerobic respiration
cytochrome c
mobile carrier that is small and soluble, transport electrons to complex IV
complex II
can shuttle electrons between complexes, gather electrons from FADH2 or NADH
complex IV
collects 4 e- and then uses them to reduce oxygen and produce water
3 ways to contribute to gradient
electron pumps (complexes 1, 3, 4), ubiquinone, Oxygen removing H+ from the solution
ATP synthases
enzyme consisting of F1 and F0, the F1 (orange has alpha/beta subunits) (bannana is stalk)
ADP
most important factor controlling respiration rate
beta
catalytic domains that cause ADP to turn into ATP
gamma
as _____ subunit turns, it interacts with the beta subunits differently
open, loose, tight
the three positions of the beta subunits which are caused by the gamma subunit
c
intermembrane subunit that acts as a water wheel for the H+ gradients
proton-motive force
energy provided by the H+ gradient, can:
1.Make ATP via ATP synthase
2.Exchange ADP for ATP (antiport).
3.Bring in Pi with H+ (symport)
4.Bring in pyruvic acid with H+ (symport)
rotenone
poison that blocks e- flow at complex 1
antimycin
poison that blocks e- flow at complex 3
cyanide
poison that blocks e- flow at complex 4
CO
poison that blocks e- flow at complex 4
uncouplers
allow H+ ions to diffuse through membrane and never reach high concentrations of ATP
chloroplast
large organelle with 3 membranes (2 outer 1 inner) containing stacks (granum) of thylakoids (pennies)
light dependent
reactions that occur in thylakoid membranes, uses sunlight and water to make NADPH and ATP
calvin cycle
reaction that turns CO2 into a carbohydrate using energy from the light reactions, recycles ADP and NADP+ to begining of cycle
NADP+
terminal electron acceptor (highest affinity) in photosynthesis
chlorophyll
pigment within the membrane of thylakoid that is excited by light and releases energy by (a.) fluorescence (b.) resonance energy transfer (c.) e- transfer
photosystem II
system where light is absorbed by reaction center and starts e- transport through the plastoquinone
photosystem I
system that makes NADPH from the e- transport
rubisco
ribose biphosphate carboxylase (RuBP), fixes CO2 in the Calvin cycle to make carboxylkase intermediates, start with 6 of them
stroma
where light independent rxn/Calvin cycle occurs
thylakoid membrane
where light dependent rxn occurs
regulated secretion
Type of secretion where proteins are stored in secretory granules and released upon a specific signal. Examples include insulin and digestive enzymes.
constitutive secretion
Type of secretion by cells where secretory products are continuously released into the extracellular space without any specific stimulus.
pathway of secreted proteins and IMPs
what is the picture?
rough ER
functions: production, folding, quality control and secretion of some proteins
smooth ER
functions: synthesis of steroid hormones, detoxification, and sequestration of calcium ions
cytosolic ribosome
all translation starts in the ______
cytosolic
cytoplasmic proteins imported mitochondrial proteins , and nuclear proteins are made by _____ ribosomes
exocytosis
vesicle fusion for secretion outside the cells (e.g. RER to cis Golgi at PM)
endocytosis
vesicle formation for intake of molecules at the plasma membrane (also called budding at organelles)
cisternae
part of the ribosome where proteins are synthesized
golgi complex
stack of flattened cisternae divided into functional groups, including a cis and trans face
functions: process proteins from the RER for secretion or the lysosome
signal hypothesis
signal codons in the mRNA cause a signal peptide, which causes insertion into the RER, where it is cleaved off. allows for certain proteins to be secreted
pellet 1
contains: nuclei, mitochondria, and other big stuff
pellet 2
contains: microsomes (ER and Golgi)
lysate
in vitro translation: the supernatant containing soluble proteins, ribosomes, tRNA, initiation & elongation factors (all the good stuff for protein synthesis)
gel autoradiograph
using a SDS page, is labeled with a radiocactive ion
sufficient
adding a 28 aa signal pathway is _____ to turning a regular protein into a secretory one
signal recognition particle (SRP)
G protein that (regulated by GTP or GDP) binds to the signal peptide, binds ribosome (stopping translation) and binds SRP receptor (docking station)
SRP-receptor
an IMP resident in RER membrane. cytoplasmic domain binds to SRP-GTP
stop transfer sequence
stretch of 20 hydrophobic AAS after a signal sequence, causes a cytosolic C terminus and a luminal N terminus
start transfer sequence
stretch of ~20 hydrophobic AAs not at N terminus, causes a cytosolic N terminus and luminal C terminus
translocon
protein complex that forms pore for passage of nascent polypeptide. Sec61 = main protein compenent
binding protein
an RER lumenal protein that helps seal the translocon and functions as a chaperone.
signal peptidase
will cut peptide bind connecting signal sequence to the remainder of the protein
NLS
sequence marking a protein for insertion into the nucleus
motif of ML
K (K/L) X (K/L)
initial or core glycosylation of glycoproteins
addition of oligosaccharides onto asp, 3 of which are cut off to help with folding
inside
proteins stay _____ the RER during folding in order to esure proper function
UGGT
functions as a folding sensor in the RER, if improperly folded, UGGT adds a glucose onto a protein
Calnexin
in the RER, modifies folding proteins by removing a glucose molecule
ubiquination
in the RER, addition of ubiquinone to a protein that fails to fold, marks for destruction in the cytoplasm
co-immunoprecipitation
determins if and how proteins interact by observint the pellet in an SDS page and immunoblotting the protein of interest (not the target of the antibody)
transmembrane proteins
have cytoplasmic sorting signals that bind to adapter proteins
coat proteins
assemble onto adapters, forming a sphere and making a pinch-off bud
adapter proteins
binds to transmembrane proteins with sorting signals and allows for binding of coat proteins
COPII-coated vesicles
coat protein that move materials friom the RER to Golgi
COPI-coated vesicles
coat protein that recycle materials back to precious Golgi
Clathrin coated vesicles
coat protein that uses AP2 for plasma membrane and AP1 for golgi
SNARE
(1) Tethering: Rab G-proteins on the vesicle and target surface each bind to tethering proteins that \n mediate the first connection between vesicle and target. \n (2) Docking: v-SNARES on the vesicle and t-SNARES on the target surface interact in a specific \n manner to allow docking of the vesicle at the target surface. \n (3) Fusion: the v- and t-SNARES are helical and they coil around one another and twist which \n physically pulls on the vesicle and target membranes and allows them to become one
CIS & CGN
modification in the Golgi: Sorting for RER retrieval, PO4 addition on mannose, mannose removal
medial
modification in the Golgi: further mannose removal, N-acetylglucosamine addition,
trans
modification in the Golgi: Fucose, glucose and galactose addition
TGN
modification in the Golgi: sialic acid addition, sorting
asp-x-x-leu-leu
used for transport from the TGN to the lysosome via clathrin
lys-lys-X-X (kkxx)
used for transport back to the RER through Arf 1by COP I
DXE, or FF, FY, or YY
used for transport from RER to the golgi by COP II through Sar 1