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SB Flashcards

1
Q

Phosphorylase

A
  • is an enzyme that removes a phosphate group from its substrate.
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2
Q

Kinases

A
  • catalyses the transfer of γ-phosphate from ATP (or GTP) to its protein substrates.
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3
Q

Phosphatase

A
  • is an enzyme that removes a phosphate group from a protein.
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4
Q

Synthase

A
  • is an enzyme that catalyses a synthesis process.
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5
Q

Ligase

A
  • is an enzyme that can catalyze the joining of two large molecules by forming a new chemical bond.
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6
Q

G-actin

A
  • monomeric globular actin.
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7
Q

Monomer

A
  • a molecule that can be bonded to other identical molecules to form a polymer.
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8
Q

Actin Polymeralization

A
  • monomers of globular actin (G-actin) polymerize into filamentous actin (F-actin).
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9
Q

F-actin

A
  • the form involved in muscle contraction.
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10
Q

Integrase

A
  • Integrase cleaves two nucleotides from the 3’ ends of the viral DNA (vDNA). The enzyme catalyzes the nucleophilic attack of the 3’ hydroxyl group at the end of the processed DNA on a pair of phosphodiester bond wich is between the Phosphate group and the oxygen.
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11
Q

Phosphodiester Bond

A
  • is the linkage between the 3’ carbon atom of one sugar molecule and the 5’ carbon atom of another, deoxyribose in DNA and ribose in RNA.
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12
Q

Mendelian Inheritance

A
  • p^2 + 2pq + q^2 = 1
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13
Q

Reverse Transcriptase

A
  • is an enzyme used to generate complementary DNA (cDNA) from an RNA template.
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14
Q

Hill Coefficient

A
  • measures cooperativity.
  • n>1 = cooperativity
  • n=1 no cooperativity
  • n<1 = negative cooperativity
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15
Q

Kd

A
  • Small Kd = high affinity/binding because smaller concentration of substrate required to saturate 50% of the enzyme available
  • Big Kd = less affinity/binding because bigger concentration of substrate required to saturate 50% of the enzyme available

[Enzyme][Substrate]

[Enzyme-Substrate].

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16
Q

Ka

A
  • Opposite of Kd
  • High Ka = high affinity/binding
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17
Q

Competitive Inhibitor

A
  • Increases Km (the amount of substrate you need to get to 1/2 the max velocity)
  • Increases Kd (parallels Km; substrate “affinity” is decreased)
  • Doesn’t affect the enzyme itself; once we get enough substrate in there, the enzyme will get to the same top speed. Vmax is unchanged.
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18
Q

Noncompetitive Inhibitor

A
  • Km and Kd are unchanged
  • The enzyme itself is sketched up. It can’t reach the same Vmax.
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19
Q

Uncompetitive Inhibitor

A
  • The inhibitor binds to the ES complex only, not to the naked enzyme or the free substrate. It stabilizes the ES complex.
  • Km decreases (the affinity for enzyme and substrate increases, because we have this matchmaker inhibitor stabilizing the ES complex)
  • Kd decreases (ES complex doesn’t wanna dissociate)
  • The matchmaker inhibitor wants the ES bound in holy matrimony for good, so the rate of product formation is slower. Vmax is decreased
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20
Q

Mixed Inhibitor

A
  • The inhibitor can bind either the naked enzyme or the ES complex. Maybe it prefers one over the other–that depends on the inhibitor.
  • Think of it as a mix of competitive and uncompetitive. So obviously, Vmax is going down (noncompetitive and uncompetitive have that in common).
  • According to my quick sheet, Km may decrease or increase? I don’t understand how an allosteric inhibitor could increase Km, but Kaplan hasn’t been wrong yet.
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21
Q

Isoelectric Point

A
  • is the pH at which a molecule carries no net electrical charge or is electrically neutral in the statistical mean.
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22
Q

Lineweaver–Burk Plot:

Competitive Inhibitor

A

*

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23
Q

Lineweaver–Burk Plot:

Noncompetitive Inhibitor

A
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24
Q

Lineweaver–Burk Plot:

Mixed Inhibitor

A
  • The curves for the activity with and without the inhibitor intersect at a point that is not on either axis.
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25
Q

Lineweaver–Burk Plot:

Uncompeititve Inhibitor

A
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26
Q

GTPase

A
  • are enzymes that catalyze the hydrolysis of guanosine triphosphate (GTP) to guanosine diphosphate (GDP).
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27
Q

Deaminase

A
  • is the removal of an amino group from a molecule
28
Q

Isoform

A
  • is a member of a set of highly similar proteins that originate from a single gene or gene family and are the result of genetic differences.
29
Q

Acetilation

A
  • introduces an acetyl functional group into a chemical compound.
30
Q

Epithelial Cells

A
  • are cells that come from surfaces of your body, such as your skin, blood vessels, urinary tract, or organs.
31
Q

Connective Tissue

A
  • Tissue that supports, protects, and gives structure to other tissues and organs in the body.
  • Types of connective tissue include bone, cartilage, fat, blood, and lymphatic tissue.
32
Q

Nervous Tissue

A
  • is found in the brain, spinal cord, and nerves.
33
Q

Transmembrane Helix

A
  • The inner part of the membrane where the hydrophobic parts are. Composed of integral proteins.
34
Q

Dimeralization

A
  • is an oligomer consisting of two monomers joined by bonds that can be either strong or weak, covalent or intermolecular.
35
Q

Homodimer

A
  • a protein composed of two polypeptide chains that are identical in the order, number, and kind of their amino acid residues.
36
Q

Phosphoglucomutase

A
  • catalyzes the interconversion between glucose-1-phosphate (G-l-P) and glucose-6-phosphate (G-6-P), which represents a branch point in carbohydrate metabolism.
37
Q

Glucose 6-Phosphatase

A
  • an enzyme found mainly in the liver and the kidneys, plays the important role of providing glucose during starvation.
38
Q

Hexokinase

A
  • is an enzyme that phosphorylates a six-carbon sugar, a hexose, to a hexose phosphate.
39
Q

Glucokinase

A
  • is a gene which plays an important role in recognising how high the blood glucose is in the body.
40
Q

DNA Polymerase

A
  • is an enzyme that synthesizes DNA molecules from deoxyribonucleotides, which are the building blocks of DNA.
41
Q

RNA Polymerase

A
  • is an enzyme that is responsible for copying a DNA sequence into an RNAsequence, duyring the process of transcription.
42
Q

DNA Ligase

A
  • is an enzyme which can connect two strands of DNA together by forming a bond between the phosphate group of one strand and the deoxyribose group on another.
43
Q

Reverse Transcriptase

A
  • is an enzyme used to generate complementary DNA (cDNA) from an RNA template, a process termed reverse transcription.
44
Q

Adenylate Cyclase

A
  • is the enzyme that synthesizes cyclic AMP from adenosine triphosphate (ATP).
45
Q

Protein Kinase A

A
  • is an enzyme that covalently decorates proteins with phosphate groups.
  • Works through cAMP
46
Q

Glycosidic Bonds

A
  • is a type of covalent bond that joins a carbohydrate (sugar) molecule to another group, which may or may not be another carbohydrate.
  • The numbers 1-4 and 1-6 refer to the carbon number of the two residues that have joined to form the bond. As illustrated in Figure 6, amylose is starch formed by unbranched chains of glucose monomers (only α 1-4 linkages), whereas amylopectin is a branched polysaccharide (α 1-6 linkages at the branch points).
47
Q

1,4 Glycosidic Bond

A
  • is formed between the carbon-1 of one monosaccharide and carbon-4 of the other monosaccharide.
48
Q

Pyruvate Dehydrogenase

A
  • Converts pyruvate to Acetyl-CoA.
  • Increases flux of Acetyl CoA from Glycolysis to CAC.
49
Q

Citrate Synthase

A
  • First reaction of CAC
  • Condensation of Acetyl CoA andoxaloacetate to form Citrate.
50
Q

Acomitase

A
  • Converts Citrate to Isocitrate.
  • Essential enzyme is the CAC and Iron regulatory protein
  • Interacts with mRNA to control the levels of iron inside the cell.
51
Q

Isocitrate Dehydrogenase

A
  • It’;s a digestive enzyme in the CAC.
  • It functions by catalyzing the oxidative decarboxylation of Isocitrate into Alpha-Ketoglutarate.
52
Q

Alpha-Ketoglutarate Dehydrogenase

A
  • It’s a highly regulated enzyme.
  • Catalyzes the conversion of Alpha-Ketoglutarate into succinyl-CoA.
  • Produces NADH and CO2
53
Q

Succinyl CoA Synthase

A
  • Is the only mitochondrial enzyme capable of ATP production through Substrate-Level-Phosphorylation.
  • In CAC, converts Succinyl-CoAto Succinate
  • Produces GTP
54
Q

Succinate Dehydrogenase

A
  • The only enzyme in both CAC and ETC.
  • Oxidizes Succinate into Fumerate
  • Produces GTP
55
Q

Fumerase

A
  • Is the enzyme that catalyzes the reversible hydration/dehydration of Fumerate to Malate
56
Q

Malate Dehydrogenase

A
  • Converts Malate into Oxaloacetate
  • Produces NADH
57
Q

NADH Dehydrogenase

A
  • Converts NADH to NAD+ to provide protons.
  • Is part of Complex I in ETC at the Mitochondrial respiration chain which catalyzes transfer of Electrons from NADH to Ubiquione
  • 4H+ pumped.
58
Q

Cytochrome Reductase

A
  • Accepts Electrons from ETC and transfer them to Cytochrome C
  • E -> Cyt C ->Cyt B -> Cyt-C
  • Complex III
  • 4H+ Pumped
59
Q

Cytochrome C Oxidase

A
  • Removes Electrons from Cyt-C and uses Electrons for reduction of O2 to H2O
60
Q

Palindrome Sequence

A
  • A palindromic sequence is a nucleic acid sequence in a double-stranded DNA or RNA molecule wherein reading in a certain direction on one strand matches the sequence reading in the same direction on the complementary strand.
  • GAATTC is a palindrome of CTTAAG.
61
Q

Punett Square

A
62
Q

Endomembrane System

A
63
Q

Enzyme Alterations

A
  • Local pH
  • Substrate Shape
  • Co-localizing substrate
64
Q

Lipid Raft

A
  • are areas of high cholesterol.
65
Q

Na+K+ ATPase

A
  • Na+ is transported out of the cell; K+ is transported into the cell.
66
Q

Kidney

A
  • Secretion = movement of material in to the tubule lumen (ie. bicarbonate ions)
  • Excretion = movement of material along the kidney tubules for ultimate elimination from the body (ie. urine leaves medullary collecting duct –> ureter –> urethra –> in to Walter Palmer’s mouth)
  • Resorption = process of losing a substance (ie. breaking down bone to release Ca2+ ions)
  • Reabsorption = process of reabsorbing again (ie. water that was first filtered in the glomerulus is reabsorbed back in to the blood stream via loop of henle)
67
Q
A

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