Biochemistry Flashcards
oxidoreductase
catalyzes transfer of e-, often using a cofactor such as NAD+
- dehydrogenase
transferase
catalyzes movement of functional group from one molecule to another
- kinases
hydrolase
breaking of a molecule using H2O
Lyase
breaks/form C-C, C-O, C-N bonds without being oxidoreductase or hydrolase
isomerase
creates isomer of original molecule
Ligase
catalyzes addition or synthesis reactions
- usually uses ATP
lock and key theory
suggest enzyme’s active site (lock) is already in appropriate conformation for substrate (key) to bind
induced fit theory
substrate causes enzyme’s active site to conformationally change (induce fit) upon binding
enzymes without cofactors are called _____ and then become ______ with a cofactor; define prosthetic group
apoenzymes; holoenzymes
- tightly bound cofactors/coenzymes necessary for enzyme function
name B vitamins
B1 - thiamine B2 - riboflavin B3 - niacin B5 - pantothenic acid B6 - pyridoxal phosphate B7 - biotin B9 - folic acid B12 - cyanocobalamin
relationship with Km and dissociation and Km and affinity
Greater Km = Greater dissociation
Greater Km = Lower affinity
michaelis menten equation
V = Vmax[S]/Km+[S]
Vmax equation; what is Kcat?
Vmax = Kcat[E]
- Kcat is the turnover number (# of substrates converted to products)
Describe Hill’s coefficient if greater than, less than, or equal to 1
- > 1 = positively cooperative, after one ligand binds affinity increases
- <1 = negatively cooperative, after one ligand binds affinity decreases
- =1 = enzyme does not exhibit cooperative binding
competitive vs noncompetitive vs uncompetitive (and how each affects Vmax and Km)
- competitive inhibitors compete with substrate for the active site (Km increases, Vmax unchanged)
- noncompetitive inhibitors bind in spot that is not active site, changing conformation of binding site (Vmax decreases, Km unchanged)
- uncompetitive inhibitors bind only to E-S complex and lock substrate in enzyme, effectively increasing affinity (Km and Vmax decrease)
what is a zymogen?
an inactive enzyme that must be activated in order to be functional
collagen vs elastin vs keratin
ALL part of extracellular matrix
- collagen is in connective tissue; provides strength/flexibility
- elastin is in connective tissue; stretches/recoils, restoring original tissue shape
- keratin is in epithelial cells; contributes to mechanical integrity of cell and is a regulatory protein; makes up hair and nails
actin vs tubulin
- Actin is in myofibrils, is the most abundant protein in eukaryotic cells; they have a + and - side, can travel unidirectionally
- Tubulin makes up MTs, provide structure and chromosome separation in mitosis/meiosis; also polar, - side adjacent to nucleus and + side in periphery of cell
myosin
primary motor protein interacting with actin
- is a thick filament in myofibrils, also involved in cell transport
- part of POWER STROKE in sarcomere
kinesins vs dyneins
motor proteins associated w/ MTs
- Kinesins play role in aligning chromosomes; bring vesicles to + end of MT
- Dyneins are involved in sliding movement of cilia and flagella; bring vesicles to - end of MT
cell adhesion molecules (CAMs), what are the 3 types?
proteins found on surface of most cells and aid in binding cell to ECM or other cells
- ALL are integral membrane proteins
- Cadherins, integrins, selectins
cadherins
group of glycoproteins that mediate Ca2+ dependent cell adhesion
- hold similar cell types together
integrins
group of proteins that all have 2 membrane-spanning chains called alpha and beta, which bind to and communicate w/ extracellular matrix
- play role in cell signaling
selectins
bind to carbohydrate molecules that project from other cell surfaces (weakest bonds)
- expressed on WBCs and endothelial cells that line blood vessels
- play important role in host defense, including inflammation and WBC migration