1 A Uhcl Biochem Ii Exam2.1 - All Questions

Front 1

--- Simple Uncatalyzed Reaction ---
From the law of *** *** the reaction velocity is given by: v = k[S].

Back 1

mass action

Front 2

Storage polysaccharides like ***(animals) and ***(plants) are broken down into *** which is metabolized via glycolysis.

Back 2

glycogen
starch
glucose 6-phosphate

Front 3

Cooperativity can be defined in terms of the ***.

Back 3

Cooperativity Index (Rx)

Front 4

--- Allosteric Constant ---
Is the equilibrium constant between L and R when no ligand is present.
1) Has the unit of ***.
2) Has a formula of...
3) dissociation constant for...
4) formation constant for...

Back 4

1) L
2) [T2]\[R2]
3) R2
4) T2

Front 5

--- Enzyme Kinetic Study ---
1) *** concentration is varied.
2) *** concentration is constant.
3) The effect on reaction *** is studied.

Back 5

1) Substrate
2) Enzyme
3) velocity

Front 6

--- Lactose ---
1) Disaccharide composed of...
2) Reducing sugar?
3) α/β linked?
4) Broken down by...

Back 6

1) galactose --- glucose
2) Yes
3) β/α
4) lactase

Front 7

---M: monomeric subunit (termed protomer)
---M2 is the dimeric protein.
1) If 1st ligand causes a LARGE affinity increase for the 2nd it has *** Cooperativity.
2) There will be either NO ligand OR saturated w/ligand.

Back 7

1) Complete

Front 8

--- General MWC Equation ---
1) The greater the value for L, the more *** the plot.
2) If L = 0 or n = 1, a *** curve is obtained.

Back 8

1) sigmoidal
2) hyperbolic

Front 9

1) [E0] (free enzyme at *** ***) which is equal to [ET].
2) [ET] = [E]+[ES] --- is called the *** equation.
3) The *** assumption [ES] at any given time will be...
k1[E][S] = k-1[ES]

Back 9

1) zero time
2) conservation
3) equilibrium
4)

Front 10

--- Sucrose ---
1) Disaccharide composed of...
2) Reducing sugar?
3) α/β linked?
4) Broken down by...

Back 10

1) fructose --- glucose
2) No
3) α/β
4) sucrase (invertase)

Front 11

A *** is the structural unit of an oligomeric protein.

Back 11

protomer

Front 12

The *** model is consistent w/sigmoidal binding even though it's assumed there's no protomer cooperativity.

Back 12

MWC

Front 13

What equation is this?

Back 13

Michaelis-Menten equation

Front 14

--- Trehalose ---
1) Disaccharide composed of...
2) Reducing sugar?
3) α/β linked?
4) Broken down by...

Back 14

1) glucose --- glucose
2) No
3) α/α
4) trehalase

Front 15

--- MWC Model ---
•In absence of ligand, equilibrium favors *** state.
•Ligand binding shifts equilibrium toward *** state.

Back 15

T
R

Front 16

The *** relationship is the equilibrium constant for a particular enzyme reaction in terms of VMax and KM.

Back 16

Haldane

Front 17

What equation is this?

Back 17

Steady-State equation

Front 18

--- Maltose ---
1) Produced by enzyme *** during breakdown of
2) grain starches *** and ***. In mammals,
3) it's then hydrolyzed into *** by enzyme ***.

Back 18

1) diastase
2) amylose and amylopectin
3) (2) glucose --- maltase

Front 19

The Adair equation describe binding under the *** model.

Back 19

KNF

Front 20

--- Cooperativity Index ---
1) If h = 1 then Rx = *** (*** type)
2) If h = 2 then Rx = ***
3) If h = 4 then Rx = ***

Back 20

1) 81 (Michaelis-Menten type)
2) 9
3) 3
81^(1/4)

Front 21

1) An alternative to the Michaelis-Menten
model is the....
2) This model assumes that...

Back 21

1) steady-state assumption
2) over time ES levels reach a steady state

Front 22

--- Maltose ---
1) Amylose and amylopectin are similar to glycogen but....
2) Other proteins uses to break down grains also include *** and ***...

Back 22

1) have no/little branching
2) proteases and lipases.

Front 23

1) The classical ligand/protein binding models used the proteins *** and ***.
2) One of these proteins has a ligand that w/*** effects rather than ***.

Back 23

1) myoglobin --- hemoglobin
2) homotropic --- heterotropic

Front 24

A comparison of *** values may provide information about the amount of enzyme in different tissues.

Back 24

Vmax

Front 25

--- Malting Process ---
1) # of steps
2) Which are...?
3) How long is each step?

Back 25

1) 4
2) soak - germinate - heat drying/curing
3) 2-3 --- 7-14 --- 4(2 & 2)

Front 26

Myoglobin --- Hemoglobin
1) Binding Sites?
2) Location?
3) Curve?

Back 26

1) 1 --- 4
2) muscle --- blood
3) hyperbolic --- sigmoidal

Front 27

Vmax depends on the amount of *** used whereas KM does not.

Back 27

enzyme

Front 28

1) ***: process in which cereal grains
2) soak, germinate, and dry in a ***.
3) Heat Drying temp?
4) Heat Curing temp?

Back 28

1) kiln
2) Malting
3) 32-37 C
4) 78-100 C

Front 29

1) General binding curve of Langumir equation is...
2) *** is equivalent to the ligand concentration giving ½ fractional saturation.

Back 29

1) rectangular hyperbola
2) Kd

Front 30

What equation is this?

Back 30

Lineweaver-Burk Equation

Front 31

--- Fructose ---
1) In skeletal muscle, it's metabolized by ***.
2a) In liver, acted on by *** and
2b) metabolized by *** and *** kinase.

Back 31

1) hexokinase
2a) fructokinase
2b) fructose 1-P --- triose

Front 32

Hemoglobin transitions between low and high affinity states due to *** w/in it. This results in a *** binding curve

Back 32

1) cooperativity
2) sigmoidal

Front 33

Briggs and Haldane came up with what?

Back 33

Steady-State Assumption

Front 34

Disaccharide Enzymes
1) Lactose
2) Sucrose
3) Trehalose
4) Maltose

Back 34

1) Lacase
2) sucrase (invertase)
3) trehalase
4) maltase

Front 35

--- pO2 ---
1) Lungs?
2) Peripheral tissues?

Back 35

1) 13.3 kPa
2) 2 kPa

Front 36

--- Mannose ---
1) ***saccharide metabolized to *** which is
2) an intermediate in the *** pathway.
3) 1st --- *** Kinase
4) 2nd --- Phosphomannose ***

Back 36

1) mono --- fructose 6-P
2) glycolysis
3) Hexose Kinase
4) Phosphomannose isomerase

Front 37

--- Adair Equation ---
For the binding of a ligand to a protein w/2 binding sites for the ligand.
1) M2: two protomers are...
2) M2S
3) M2S2

Back 37

1) both unbound
2) 1 bound protomer/1 unbound
3) both bound

Front 38

--- Mannose ---
1) Hexose Kinase
Mannose + ATP ⇌ *** + ADP
2) Phosphomannose isomerase
xxx ⇌ ***

Back 38

1) Mannose 6-P
2) Fructose 6-P

Front 39

--- Adair Equation ---
--Dimeric and NO Cooperativity--
1) M + S ⇌ MS is the *** binding constant labeled K***.
2) M2 + S ⇌ M2S is the *** binding constant labeled K***.
3) M2S + S ⇌ M2S2 is the *** binding constant labeled K***.
4) Kb1 = ***Kb
5) Kb2 = ***Kb

Back 39

1) intrinsic --- Kb
2) apparent --- Kb1
3) apparent --- Kb2
4) Kb1 = 2Kb
5) Kb2 = ½Kb

Front 40

--- Ethanol Synthesis ---
1) Created when *** (generated during glycolysis) is re***
2) with *** serving as final electron acceptor.

Back 40

1) NADH --- reoxidized
2) acetaldehyde

Front 41

--- LIVER Enzyme Locations ---
1) Alcohol DH
2) Cytochrome P-450
3) Catalase
4) ALdehyde DH

Back 41

1) cytosol (ADH)
2) microsomal (smooth ER)
3) peroxisomes
4) MITOCHONDRIA (ALDH)

Front 42

--- Ethanol Metabolism LIVER ---
1) 1st pathways ⇌ ***
2) mito ALDH ⇌ ***
3) then enzyme *** prepares it for
4) TCA cycle by ⇌ ***

Back 42

1) Acetaldehyde
2) Acetate
3) Acetyl-CoA synthetase
4) Acetyl-S-CoA

Front 43

--- Ethanol Metabolism ---
Maximum Theoretical ATP?
1) Alcohol DH
2) ALdehyde DH
3) Catalase

Back 43

1) 13 (5)
2) 8 (-2.5, 2.5)
3) 10.5 (2.5)
(-2, ???, ???, 10)

Front 44

--- Ethanol Metabolism ---
Enzyme most important at this concentration...
1) High
2) Low
3) How many pathways are there?

Back 44

1) Cytochrome P-450 OR MEOS
2) Alcohol DH
3) 3

Front 45

--- Cytochrome P-450 ---
1) Falls w/in class called...
2) Consisting of *#* families and *#* subfamilies

Back 45

1) mixed-function oxidases OR monooxygenases
2) 18--- 43
4)

Front 46

--- Alcohol Enzymes ---
Ethanol + (???) ⇌ Acetaldehyde + (???)
1) Alcohol DH
2) Cytochrome P-450
3) Catalase

Back 46

1) NAD+ ⇌ NADH/H+
2) NADPH/H+/O2 ⇌ NADP+/H2O
3) H2O2 ⇌ (2) H2O

Front 47

--- Aldehyde dehydrogenase (ALDH) ---
Substrates ⇌ Products

Back 47

H2O, NAD+, Acetaldehyde
⇌
NADH, H+, Acetic Acid

Front 48

MEOS?
1) Is a mixed function *** associated
2) with the *** *** of liver cells.
3) requires *** and *** to function

Back 48

Microsomal Ethanol Oxidizing System
1) oxidase
2) endoplasmic reticulum
3) NADPH and O2

Front 49

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Back 49

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