Chapter 8: Microbial Metabolism Flashcards
how do enzymes increase the rate of a chemical reaction?
by lowering the energy of activation
what is meant by a simple enzyme
consists of only a protein
what is a conjugated enzyme and what is another word for it?
contains protein and nonprotein molecules; can also go by holoenzymes
what is the protein portion of a conjugated enzyme called?
apoenzyme
what is the nonprotein portion of a conjugated enzyme called?
cofactor
what are the two types of cofactors?
- inorganic elements such as metal ions
- organic molecules (coenzymes)
what does catalase do and what cofactor does it need?
breaks down hydrogen peroxide; Fe
what does oxidase do and what cofactor does it need?
adds an electron to oxygen; Fe and Cu
what does hexokinase do and what cofactor does it need?
transfers a phosphate to glucose, which is the first step of glycolysis; Mg
what does DNA polymerase do and what cofactor does it need?
responsible for DNA synthesis; Zn and Mg
what does pyruvate dehydrogenase do and what cofactor does it need?
converts pyruvic acid to acetyl-CoA and CO2 in the transitional step of cell metabolism; thiamine and Mg
what does succinate dehydrogenase do and what cofactor does it need?
oxidizes succinate to fumarate in Kreb’s cycle; FAD (contains riboflavin)
what is the active site
site specific for substrate binding
what are the purpose of cofactors?
they support the work the of the enzyme
functions of metallic cofactors
- activate enzymes
- bring active site and substrate together
- actively participates in chemical reaction of enzyme-substrate complex
functions of coenzymes
- serve as temporary carrier for functional groups
- most commonly vitamins
what are exoenzymes
enzymes that leave the cell to break down large food molecules or harmful chemicals
ex. cellulase, amylase, penicillinase
what are endoenzymes?
enzymes that remain inside the cell
constitutive enzymes
always present, does not rely on substrate for its product
regulated enzymes
induced or repressed based on substrate concentration
condensation reaction
removes a water molecule to form a bond
ex. two glucose molecules form a glycosidic bond with removal of water creating maltose
hydrolysis reaction
breaks bond with the use of water
competitive inhibiton
competition for the active site
allosteric inhibiton
competitive inhibition, but on allosteric site rather than active
noncompetitive inhibiton
inhibitor binds to entire complex preventing reaction
enzyme supression
suppressing enzyme synthesis when there is too much end product
enzyme induction
enzymes made when there are substrates present
molecular structure of ATP
- 5C ribose sugar
- 3 phosphate
- adenine nitrogenous base
explain glucose phosphorylation
- glucose and ATP bind to hexokinase sites
- hexokinase transfers a phosphate to glucose
examples of coenzymes
NAD and FAD
arginase function and its cofactor
acts on amino acid arginine; Manganese
nitrate reductase function and cofactor
reduces nitrate to nitrite; Mo
botulinum toxin function and cofactor
hydrolyzes protein needed for vesicle transport; Zn
what are oxireductases
enzymes that can remove electrons from one substrate and add them to another
aminotransferases
- involves NH3+
- redistributes nitrogen between amino acids
- happens in protein metabolism and glucogenesis
phosphotransferases
- involves (PO4)3-
- enzyme transfers phosphate groups
methyltransferases
- involves CH3
- methyl groups are transferred to other molecules
decarboxylases
- involves CO2
- removes a carboxyl group and releases carbon dioxide
dehydrogenases
involves H+
- hydrogen removed from organic compounds
transferases
- involves C, N, P, and S
- move functional groups from one molecule to another
Hydrolases
involves H2O
- breaks bonds using water
isomerases
molecule is turned from one isomer to another
lyases
- chemical bonds broken and double bonds/rings are created
ligase
two molecules joined together with covalent bond
lipase
breaks down fats in the body
DNAase
break down DNA w hydrolysis of phosphate DNA backbone
synthetases
joins two molecules by splitting phosphate group from a triphosphate
polymerases
formation of a specific polymer
cellulase
degrades cellulose
lactase
breaks down lactose into glucose and galactose
aldosaes
breaks down sugar to produce energy
- found in liver and muscles
oxidase
O2 used as an electron acceptor to catalyze oxidation reactions
what happens in glycolysis
Glucose is oxidized and split into two molecules of pyruvic acid. NADH is a byproduct.
what is the final electron acceptor of aerobic respiration?
oxygen
what is the final electron acceptor in anaerobic respiration?
inorganic molecules
what is the final electron acceptor in fermentation?
organic compounds
steps of Kreb’s cycle
- Acetyl-CoA and oxaloacetate form citrate
- Citrate is transformed to isocitrate
- Isocitrate then converted to beta-ketoglutarate. NADH and CO2 released.
- Beta-ketoglutarate then converted to Succinyl CoA. CO2 and NADH released.
- Succinyl CoA converted to succinate. ATP created.
- Succinyl CoA becomes fumarate. FADH2 released.
- With the addition of water, fumarate is then turned into malate.
- Malate is then converted back to oxaloacetate. NADH created.
what are the products of Kreb’s cycle
2 CO2
3 NADH
3 H+
1 FADH2
1 ATP
Where does the Kreb’s cycle occur
cytoplasm in prokaryotes and mitochondria in eukaryotes
glycolysis features
- oxidation of glucose
- occurs in cytoplasm of all cells
- DOES NOT REQUIRE OXYGEN
glycolysis products
2 ATP
2 NADH
2 H2O
Electron transport system products
34 ATP
6 H2O
chemiosmosis
- pertains to the electron potential gradients across a membrane that leads to ATP synthesis with ATP synthase
in cellular metabolism how much ATP is generated in total?
38 total; 36 net
what happens in fermentation
pyruvic acid is converted to organic acid or alcohol
how many ATPs are produced in fermentation
2
amphibolism
refers to the way metabolic pathways have multiple functions
ex. numerous intermediates can synthesize amino acids, fats, nucleic acids, carbs
amination
the addition of NH4 to pyruvic acid to create amino acids
transamination
when an amino acid makes another amino acid
deamination
amino acids being used as a source of glucose by releasing NH4
what are the two stages of photosynthesis
light-dependent and light-independent reactions
light dependent reaction
Either chlorophyll, carotenoid, or phycobilin pigments absorb photons. Photons excite an electron, which goes through photosystem II. As this happens, H2O is split by photolysis, releasing O2. Electrons pass through several structures that pump H ions. Once PS I is reached, NADPH is created. Because of the H ions being pumped, the gradient activates ATP synthase, creating ATP.
light-independent reaction
uses ATP to fix CO2 to ribulose-1-5-bisphosphate and convert it to glucose
phases of calvin cycle
- Carbon fixation
- Reduction
- Regeneration of RuBP
where do light dependent reactions occur
thylakoid