DA Exam 4 Lecture 2: Enzymes- Shaw Dawg

biological catalysts

enzymes

what are various types of proteins that drive the chemical reaction required for a specific action or nutrient

enzymes

how can enzymes affect a reaction

by launching or speeding up

what are the chemicals called that are acted upon by the enzymes

substrates

in the absence of enzymes what are substrates called

reactants

in the absence of enzymes reactants take longer/shorter to convert into a useable product

longer, if at all

T/F: enzymes are very specific

t- only work with certain substrates

T/F: enzymes can work with any substrate

f- very specific

in what 3 ways do enzymes work on substrates

1. substrate orientation

2. physical stress

3. changes in substrate reactivity

what is described as occurring when an enzyme causes substrate molecules to align with each other and from a bond

substrate orientation

T/F: in order to have substrate orientation occur the substrate has to be in a particular arrangement

t

substrate orientation causes substrate molecules to do what

align with each other and from a bond

what happens when an enzyme uses physical stress on a substrate

it in effect grips the substrate and forces the molecule to break apart

how does physical stress affect the enzyme and substrate

forces them to break apart

an enzyme that causes changes in substrate reactivity alters what

placement of the molecules electrons

because the placement of the molecules electrons are altered how does this affect a molecule

influences the molecules ability to bond with other molecules

an increase in the instability of an enzyme leads to an increase/decrease in the reactivity

increase

active sites of enzymes

where enzymes come into contact with their substrates

after a substrate comes into contact with the active site of an enzyme what happens

it is modified by the enzyme to form the end product

T/F: once the enzyme and substrate bind and the process is complete, the enzyme releases the product and is ready to begin the process with new substrates

t

T/F: enzymes are never wasted and always recycled

t

T/F: enzymes last only for a few minutes

F- they last for a long time

T/F: the absence of enzymes is responsible for many diseases

t

phenylketonuria (PKU)

an inherited disorder of protein metabolism in which the absence of an enzyme leads to a toxic buildup of certain compounds, causing mental retardation and even death in infants

PKU is caused by what

absence of one type of enzyme

Tay-Sachs disease

an enzyme deficiency that causes retardation, paralysis, and often death in early childhood when left untreated

what is a chronological disorder of lipid metabolism caused by a deficiency of the enzyme B-glucocerebrosidase

Gaucher's disease

where is B-glucocerebrosidase purified from to treat Gaucher's disease

human placenta

what are characteristics of Gaucher's disease

enlarged liver and spleen, increased skin pigmentation, and painful bone lesions

what does Gaucher's disease require

purification of protein from 50,000 placentas per patient per year, puts a limit on the amount of purified protein available

the use of recombinant form of B-glucocerebrosidaes eliminates what risk

of transmissible (viral or prion) diseases associated with purifying the protein from human placentas

a change of amino acid arginine______ to histidine allows the addition of mannose residues to the protein

495

a change of amino acid arginine 495 to ____ allows the addition of mannose residues to the protein

histidine

a change of amino acid arginine 495 to histidine allows the addition of _____ residues to the protein

mannose

mannose is recognized by what type of receptors on macrophages

endocytic carbohydrate

mannose being recognized by endocytic carbohydrate receptors allows the enzyme to enter the cell more/less efficiently and to cleave the intracellular lipid that has accumulated in pathological amounts

more

examples of metabolic enzyme deficiencies

- B- Glucocerebrosidase

- taligucerase alfa (biosimilar to glucocerebrosidase)

- velaglucerase alfa (biosimilar to glucerebrosidase)

- alglucosidase alfa

- idursulfase

- elosulfase alfa

- galsulfase

- human a-galactosidase A, Aglsidase B

what 2 metabolic deficiencies are biosimilar to glucocerebrosidase

taliglucerase alfa

velaglucerase alfa

what are 3 examples of pulmonary and gastrointestinal tract disorders

1. a-I-proteinase inhibitor

2. lactase

3. pancreatic enzymes (lipase, amylase, protease)

what leads to milk product sensitivity

lactase

T/F: you can digest pancreatic enzymes

f

what are 3 important pancreatic enzymes

lipase, amylase, protease

role of lipase

breakdown fat

role of amylase

break down starch into simple sugars

role of protease

breaks down proteins into amino acids

adenosone deaminase is what

immunodeficiencies

blood should clot immediately when externally exposed, but what happens internally

does not clot immediately

why is it important that blood does not clot immediately internally

can cause stroke and heart attack

what is given to people who have tendency to produce more blood clots in the body

Tenecteplase

what is thrombin pooled from

human plasma

what is fibrin sealant a mixture of

fibrinogen and thrombin