Enzyme Regulation I. Dr. Kevin Ahern
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1 Enzyme Regulation I Dr. Kevin Ahern
2 Enzyme Regulation Mechanisms
3 Enzyme Regulation Mechanisms 1. Allosterism
4 Enzyme Regulation Mechanisms 1. Allosterism 2. Covalent Modification
5 Enzyme Regulation Mechanisms 1. Allosterism 2. Covalent Modification 3. Control of Synthesis
6 Enzyme Regulation Mechanisms Allosterism Covalent Modification Control of Synthesis Availability of Substrate
7 Control of Enzyme Activity
8 Control of Enzyme Activity
9 Control of Enzyme Activity
10 Control of Enzyme Activity Substrate Does Not Change Enzyme Binding of Substrate
11 Control of Enzyme Activity Substrate Does Not Change Enzyme Binding of Substrate Substrate Does Change Enzyme Binding of Substrate
12 Control of Enzyme Activity Homotropic and Heterotropic Effectors
13 Control of Enzyme Activity Homotropic and Heterotropic Effectors
14 Control of Enzyme Activity Homotropic and Heterotropic Effectors
15 Control of Enzyme Activity Aspartate Transcarbamoylase (ATCase)
16 Control of Enzyme Activity Aspartate Transcarbamoylase (ATCase) Six Regulatory Subunits
17 Control of Enzyme Activity Aspartate Transcarbamoylase (ATCase) Six Regulatory Subunits Six Catalytic Subunits
18 Control of Enzyme Activity
19 Control of Enzyme Activity Aspartate Transcarbamoylase (ATCase)
20 Control of Enzyme Activity Aspartate Transcarbamoylase (ATCase)
21 Control of Enzyme Activity Aspartate Transcarbamoylase (ATCase) Aspartate - Amino Acid
22 Control of Enzyme Activity Aspartate Transcarbamoylase (ATCase) Aspartate - Amino Acid ATP - High Energy, Purine
23 Control of Enzyme Activity Aspartate Transcarbamoylase (ATCase) Aspartate - Amino Acid ATP - High Energy, Purine CTP - End Product of Pathway
24 Control of Enzyme Activity Aspartate Transcarbamoylase (ATCase) Substrates Aspartate - Amino Acid ATP - High Energy, Purine CTP - End Product of Pathway
25 Control of Enzyme Activity
26 Control of Enzyme Activity ATCase is Affected by One of its Substrates - Aspartate Aspartate is a Heterotropic Effector of ATCase
27 Control of Enzyme Activity ATCase is Affected by One of its Substrates - Aspartate Aspartate is a Heterotropic Effector of ATCase Binding of Aspartate by ATCase Favors the R-State so Additional Substrate Binding is Favored
28 Control of Enzyme Activity Allosteric Control of ATCase
29 Control of Enzyme Activity Allosteric Control of ATCase 2 mm ATP
30 Control of Enzyme Activity Allosteric Control of ATCase 2 mm ATP No ATP
31 Control of Enzyme Activity Allosteric Control of ATCase In the Presence of ATP, the V0 is Increased Compared to No ATP
32 Control of Enzyme Activity Allosteric Control of ATCase ATP Activates ATCase (Converts to R State) In the Presence of ATP, the V0 is Increased Compared to No ATP
33 Control of Enzyme Activity Allosteric Control of ATCase
34 Control of Enzyme Activity Allosteric Control of ATCase CTP Reduces the Activity of ATCase - Converts to T State
35 Control of Enzyme Activity Allosteric Control of ATCase CTP Reduces the Activity of ATCase - Converts to T State V0 Decreases as [CTP] Increases
36 Control of Enzyme Activity Allosteric Control
37 Control of Enzyme Activity Allosteric Control Aspartate is a Substrate, but Neither ATP nor CTP is. All Affect the Enzyme
38 Control of Enzyme Activity Allosteric Control Aspartate is a Substrate, but Neither ATP nor CTP is. All Affect the Enzyme Six Regulatory Subunits - R1 to R6
39 Control of Enzyme Activity Allosteric Control Aspartate is a Substrate, but Neither ATP nor CTP is. All Affect the Enzyme ATP and CTP Bind Regulatory Sites Six Regulatory Subunits - R1 to R6
40 Control of Enzyme Activity Allosteric Control Aspartate is a Substrate, but Neither ATP nor CTP is. All Affect the Enzyme ATP and CTP Bind Regulatory Sites ATP Favors R State Six Regulatory Subunits - R1 to R6
41 Control of Enzyme Activity Allosteric Control Aspartate is a Substrate, but Neither ATP nor CTP is. All Affect the Enzyme ATP and CTP Bind Regulatory Sites ATP Favors R State CTP Favors T State Six Regulatory Subunits - R1 to R6
42 Control of Enzyme Activity Allosteric Control Aspartate is a Substrate, but Neither ATP nor CTP is. All Affect the Enzyme ATP and CTP Bind Regulatory Sites ATP Favors R State CTP Favors T State
43 Control of Enzyme Activity Allosteric Control Aspartate is a Substrate, but Neither ATP nor CTP is. All Affect the Enzyme ATP and CTP Bind Regulatory Sites ATP Favors R State CTP Favors T State Six Catalytic Subunits - C1 to C6
44 Control of Enzyme Activity Allosteric Control Aspartate is a Substrate, but Neither ATP nor CTP is. All Affect the Enzyme ATP and CTP Bind Regulatory Sites ATP Favors R State CTP Favors T State Six Catalytic Subunits - C1 to C6 Aspartate Binds to Catalytic Subunits Favors R State
45 Control of Enzyme Activity Allosteric Control
46 Control of Enzyme Activity Allosteric Control At Low [S], ATCase in T State
47 Control of Enzyme Activity Allosteric Control At Low [S], ATCase in T State As [S] Increases, ATCase Increasingly in R State
48 Control of Enzyme Activity Allosteric Control At High [S], ATCase Mostly in R State At Low [S], ATCase in T State As [S] Increases, ATCase Increasingly in R State
49 Control of Enzyme Activity Allosteric Control
50 Control of Enzyme Activity Allosteric Control Thus, ATCase is Most Active When Energy (ATP) is High and When Pyrimidines are Low in Concentration Relative to Purines
51 Control of Enzyme Activity Allosteric Control Thus, ATCase is Most Active When Energy (ATP) is High and When Pyrimidines are Low in Concentration Relative to Purines ATCase is Least Active When Pyrimidine Concentration (CTP) is High
52 Feedback Inhibition Aspartate Transcarbamoylase (ATCase) Carbamoyl Phosphate Aspartate Pi ATCase Carbamoyl Aspartate Multiple Reactions CTP
53 Feedback Inhibition Aspartate Transcarbamoylase (ATCase) Carbamoyl Phosphate Aspartate Pi ATCase Carbamoyl Aspartate Accumulating CTP Inhibits Enzyme Multiple Reactions CTP
54 Feedback Inhibition Aspartate Transcarbamoylase (ATCase) Aspartate Pi Carbamoyl Phosphate ATCase Cells in a High Energy State Have Lots of ATP ATP Activates ATCase Carbamoyl Aspartate Accumulating CTP Inhibits Enzyme Multiple Reactions CTP
55 Feedback Inhibition Aspartate Transcarbamoylase (ATCase) Aspartate Pi Carbamoyl Phosphate ATCase Carbamoyl Aspartate Cells With Abundant Amino Acids Have Lots of Aspartate - Activates ATCase Cells in a High Energy State Have Lots of ATP ATP Activates ATCase Accumulating CTP Inhibits Enzyme Multiple Reactions CTP
56 Covalent Modification
57 Covalent Modification
58 Zymogen Activation
59 Zymogen Activation Trypsinogen Enteropeptidase Trypsin
60 Zymogen Activation Chymotrypsinogen Trypsinogen Chymotrypsin Enteropeptidase Trypsin
61 Zymogen Activation Chymotrypsinogen Trypsinogen Chymotrypsin Enteropeptidase Proelastase Trypsin Elastase
62 Zymogen Activation Chymotrypsinogen Trypsinogen Chymotrypsin Enteropeptidase Proelastase Trypsin Elastase Procarboxypeptidase Carboxypeptidase
63 Zymogen Activation Chymotrypsinogen Trypsinogen Chymotrypsin Enteropeptidase Proelastase Trypsin Elastase Procarboxypeptidase Prolipase Carboxypeptidase Lipase
64 Zymogen Activation Chymotrypsinogen Trypsinogen Chymotrypsin Enteropeptidase Cascading Effects Trypsin Proelastase Elastase Procarboxypeptidase Prolipase Carboxypeptidase Lipase
65 Control of Enzyme of Activity Covalent Modification Control S-S Chymotrypsinogen (Inactive) S-S 1 245
66 Control of Enzyme of Activity Covalent Modification Control S-S Chymotrypsinogen (Inactive) S-S 1 Trypsin 245 S-S π - Chymotrypsin (Partly Active) S-S
67 Control of Enzyme of Activity Covalent Modification Control S-S Chymotrypsinogen (Inactive) S-S 1 Trypsin Peptide Bond Broken 245 S-S π - Chymotrypsin (Partly Active) S-S
68 Control of Enzyme of Activity Covalent Modification Control S-S Chymotrypsinogen (Inactive) S-S 1 Trypsin Peptide Bond Broken 245 S-S π - Chymotrypsin (Partly Active) S-S π - Chymotrypsin π - Chymotrypsin S-S α - Chymotrypsin (Fully Active) S-S
69 Control of Enzyme of Activity Covalent Modification Control S-S Chymotrypsinogen (Inactive) S-S 1 Trypsin Peptide Bond Broken 245 S-S π - Chymotrypsin (Partly Active) S-S π - Chymotrypsin π - Chymotrypsin S-S α - Chymotrypsin (Fully Active) S-S Peptide Bond Broken, Dipeptide Released
70 Control of Enzyme of Activity Covalent Modification Control S-S Chymotrypsinogen (Inactive) S-S 1 Trypsin Peptide Bond Broken 245 S-S π - Chymotrypsin (Partly Active) S-S π - Chymotrypsin π - Chymotrypsin S-S α - Chymotrypsin (Fully Active) S-S Peptide Bond Broken, Dipeptide Released Peptide Bonds Broken, Tripeptide Released
71 Control of Enzyme of Activity Zymogens
72 Control of Enzyme of Activity Zymogens Protease Precursors Pepsinogen Proenteropeptidase Trypsinogen Chymotrypsinogen Procarboxypeptidases Blood Clotting Proteins Procaspases Proelastase
73 Control of Enzyme of Activity Zymogens Protease Precursors Pepsinogen Proenteropeptidase Trypsinogen Chymotrypsinogen Procarboxypeptidases Blood Clotting Proteins Procaspases Proelastase Other Pacifastin Plasminogen Angiotensinogen Prolipase Pre-proinsulin
74 Control of Enzyme of Activity Other Covalent Modifications to Proteins
75 Control of Enzyme of Activity Other Covalent Modifications to Proteins Phosphorylation - Kinase Cascades
76 Control of Enzyme of Activity Other Covalent Modifications to Proteins Phosphorylation - Kinase Cascades Acetylation - Histones
77 Control of Enzyme of Activity Other Covalent Modifications to Proteins Phosphorylation - Kinase Cascades Acetylation - Histones Formylation - All Prokaryotic Proteins
78 Control of Enzyme of Activity Other Covalent Modifications to Proteins Phosphorylation - Kinase Cascades Acetylation - Histones Formylation - All Prokaryotic Proteins Acylation - Anchored Membrane Proteins (SRC)
79 Control of Enzyme of Activity Other Covalent Modifications to Proteins Phosphorylation - Kinase Cascades Acetylation - Histones Formylation - All Prokaryotic Proteins Acylation - Anchored Membrane Proteins (SRC) ADP Ribosylation - Transcription Factors
80 Control of Enzyme of Activity Other Covalent Modifications to Proteins Phosphorylation - Kinase Cascades Acetylation - Histones Formylation - All Prokaryotic Proteins Acylation - Anchored Membrane Proteins (SRC) ADP Ribosylation - Transcription Factors Prenylation - Ras
81 Control of Enzyme of Activity Other Covalent Modifications to Proteins Phosphorylation - Kinase Cascades Acetylation - Histones Formylation - All Prokaryotic Proteins Acylation - Anchored Membrane Proteins (SRC) ADP Ribosylation - Transcription Factors Prenylation - Ras Sulfation - Serine Protease Inhibitors
82 Control of Enzyme of Activity Other Covalent Modifications to Proteins Phosphorylation - Kinase Cascades Acetylation - Histones Formylation - All Prokaryotic Proteins Acylation - Anchored Membrane Proteins (SRC) ADP Ribosylation - Transcription Factors Prenylation - Ras Sulfation - Serine Protease Inhibitors Ubiquitination - Many Proteins
83 Control of Enzyme of Activity Other Covalent Modifications to Proteins Phosphorylation - Kinase Cascades Acetylation - Histones Formylation - All Prokaryotic Proteins Acylation - Anchored Membrane Proteins (SRC) ADP Ribosylation - Transcription Factors Prenylation - Ras Sulfation - Serine Protease Inhibitors Ubiquitination - Many Proteins γ-carboxylation - Clotting Proteins
84 Control of Enzyme of Activity γ-carboxylation Glutamate Side Chain γ - carboxyglutamate
85 Control of Enzyme of Activity γ-carboxylation Carboxyl Group Added Glutamate Side Chain γ - carboxyglutamate
86 Control of Enzyme of Activity γ-carboxylation Carboxyl Group Added Glutamate Side Chain γ - carboxyglutamate
87 Metabolic Melody
88 Protein Wonderland (to the tune of Winter Wonderland ) Copyright Kevin Ahern
89 Protein Wonderland (to the tune of Winter Wonderland ) Copyright Kevin Ahern Mechan-i-sm.. determines How an en.. zyme is workin Here are the ways That each elastase Breaks a peptide bond so easily Starting with the binding of the substrate Catalytic triad is the star Histidine s electron sink reacts to Pull a proton from a serine s a-r-r-r-r Then the al... koxide ion Gets elec... trons a-flyin It makes a big fuss For one nuc-le-us And breaks and makes a bond with carbonyl
90 Protein Wonderland (to the tune of Winter Wonderland ) Copyright Kevin Ahern Mechan-i-sm.. determines How an en.. zyme is workin Here are the ways That each elastase Breaks a peptide bond so easily Starting with the binding of the substrate Catalytic triad is the star Histidine s electron sink reacts to Pull a proton from a serine s a-r-r-r-r Then the al... koxide ion Gets elec... trons a-flyin It makes a big fuss For one nuc-le-us And breaks and makes a bond with carbonyl Then the process switches in its action Water comes to free the carbonyl Loss of proton yields hydroxide ion Attacking on the peptide bound there still -ll -ll Which the en.... zyme releases Otherwise... action ceases The process is done Until the S1 Binds a substrate starting up again
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