Metabolic Processes
... Properties of water are due to hydrogen bonds I. They are responsible for the surface tension properties of water. II. They are responsible for the relatively high boiling point of water. III. They are responsible for adhesion- cohesion IV. The make water a good heat sink. V. The maximum density o ...
... Properties of water are due to hydrogen bonds I. They are responsible for the surface tension properties of water. II. They are responsible for the relatively high boiling point of water. III. They are responsible for adhesion- cohesion IV. The make water a good heat sink. V. The maximum density o ...
Effect of Temperature Increasing the temperature increases the
... • Proteins take on the 3-D structure with lowest potential energy - increases their stability • Increased energy causes increased motion within the molecule as well as between molecules • Weak bonds in the tertiary structure (hydrogen bonds) are broken and new bonds form in different positions • New ...
... • Proteins take on the 3-D structure with lowest potential energy - increases their stability • Increased energy causes increased motion within the molecule as well as between molecules • Weak bonds in the tertiary structure (hydrogen bonds) are broken and new bonds form in different positions • New ...
The Need for Constant Renewal of the Antibacterial
... • Alteration in target site • Alteration in access to the target site • Production of inactivating enzymes ...
... • Alteration in target site • Alteration in access to the target site • Production of inactivating enzymes ...
Step 1 - Template Recognition and Initial Alignment
... the web, selects the PDB as database to search, wait 5 seconds, and obtains a list of hits the modeling templates and corresponding alignments. Usually, the hit with most sequence identity will be the first option, see figure 2, but one should keep in mind other points of interest, for example activ ...
... the web, selects the PDB as database to search, wait 5 seconds, and obtains a list of hits the modeling templates and corresponding alignments. Usually, the hit with most sequence identity will be the first option, see figure 2, but one should keep in mind other points of interest, for example activ ...
File
... 7. Effect of pH on Enzymes Enzymes work best within a range of pH depending on the type of enzyme. The pH that the enzymes works best at is called it’s Optimum pH If the pH is too high, the enzymes active site changes shape (denatured) What is the optimum pH of this enzyme ? ...
... 7. Effect of pH on Enzymes Enzymes work best within a range of pH depending on the type of enzyme. The pH that the enzymes works best at is called it’s Optimum pH If the pH is too high, the enzymes active site changes shape (denatured) What is the optimum pH of this enzyme ? ...
Lecture 21
... Isozymes: Enzymes that catalyze the same reaction but are different in their kinetic behavior Tissue specific Glucokinase- Liver controls blood glucose levels. Hexokinase in muscle - allosteric inhibition by ATP Hexokinase in brain - NO allosteric inhibition by ATP ...
... Isozymes: Enzymes that catalyze the same reaction but are different in their kinetic behavior Tissue specific Glucokinase- Liver controls blood glucose levels. Hexokinase in muscle - allosteric inhibition by ATP Hexokinase in brain - NO allosteric inhibition by ATP ...
Protein Turnover and Amino Acid Catabolism
... The aldehyde forms a Schiff–base with an ε– amino group on the enzyme. This Schiff-bases can be exchanged for one with the α– amino group of an amino acid See here for summary of Schiff Base addition/elimination rxn http://www.cem.msu.edu/~reusch/VirtTxtJml/aldket1.htm ...
... The aldehyde forms a Schiff–base with an ε– amino group on the enzyme. This Schiff-bases can be exchanged for one with the α– amino group of an amino acid See here for summary of Schiff Base addition/elimination rxn http://www.cem.msu.edu/~reusch/VirtTxtJml/aldket1.htm ...
Enzymes
... utilized by time it reaches the large intestines -- leaving only waste (cellulose, pectins, etc..). ...
... utilized by time it reaches the large intestines -- leaving only waste (cellulose, pectins, etc..). ...
Slide 12
... *Sequence of amino acids matters : Example : If you have 2 amino acids you can make 2 peptides ( Ala – Cys ) and ( Cys – Ala ) are 2 different peptides -By convention , we read the sequence of amino acids in a peptide from free amino group toward free carboxylic group ...
... *Sequence of amino acids matters : Example : If you have 2 amino acids you can make 2 peptides ( Ala – Cys ) and ( Cys – Ala ) are 2 different peptides -By convention , we read the sequence of amino acids in a peptide from free amino group toward free carboxylic group ...
88. Merging photoredox with nickel catalysis: Coupling of -carboxyl sp 3 -carbons with aryl halides
... in recent years as a powerful technique in organic synthesis. This class of catalysis makes use of transition metal polypyridyl complexes that, upon excitation by visible light, engage in single-electron transfer (SET) with common functional groups, activating organic molecules toward a diverse arra ...
... in recent years as a powerful technique in organic synthesis. This class of catalysis makes use of transition metal polypyridyl complexes that, upon excitation by visible light, engage in single-electron transfer (SET) with common functional groups, activating organic molecules toward a diverse arra ...
File
... • State which enzymes and isoenzymes are found in which tissues • Use of enzymes as diagnostic & therapeutic tool ...
... • State which enzymes and isoenzymes are found in which tissues • Use of enzymes as diagnostic & therapeutic tool ...
Glucogenic and ketogenic amino acids
... Catabolism of the carbon skeletons of amino acids The catabolism of the amino acids found in proteins involves : the removal of α-amino groups. followed by the breakdown of the resulting carbon skeletons. These pathways converge to form seven intermediate products : oxaloacetate, α-ketoglutarate ...
... Catabolism of the carbon skeletons of amino acids The catabolism of the amino acids found in proteins involves : the removal of α-amino groups. followed by the breakdown of the resulting carbon skeletons. These pathways converge to form seven intermediate products : oxaloacetate, α-ketoglutarate ...
Crystal Structure of the Carboxyltransferase Domain of Acetyl
... superfamily. The active site is at the interface of a dimer. Mutagenesis and kinetic studies reveal the functional roles of conserved residues here. The herbicides target the active site of CT, providing a lead for inhibitor development against human ACCs. Acetyl–coenzyme A carboxylases (ACCs) catal ...
... superfamily. The active site is at the interface of a dimer. Mutagenesis and kinetic studies reveal the functional roles of conserved residues here. The herbicides target the active site of CT, providing a lead for inhibitor development against human ACCs. Acetyl–coenzyme A carboxylases (ACCs) catal ...
Problem Set 2 (multiple choice) Biochemistry 3300 1. What classes
... a) All living organisms try to be in equilibrium. b) A living cell tries to maintain a steady state. c) Maintaining a steady state is coupled to a flux of metabolites d) Organisms use metabolic processes to obtain the free energy they need to carry out various functions. e) Chemotrophs rely on chemi ...
... a) All living organisms try to be in equilibrium. b) A living cell tries to maintain a steady state. c) Maintaining a steady state is coupled to a flux of metabolites d) Organisms use metabolic processes to obtain the free energy they need to carry out various functions. e) Chemotrophs rely on chemi ...
6.3 Protein Synthesis Translation
... The ribosome has 2 sites for the tRNA’s to “lock” into for translation. They are the A (acceptor) site and the P (peptide) site. The process begins with the tRNA carrying methionine locking into the P site. The next tRNA carrying the corresponding amino acid enters A site and the methonine forms a p ...
... The ribosome has 2 sites for the tRNA’s to “lock” into for translation. They are the A (acceptor) site and the P (peptide) site. The process begins with the tRNA carrying methionine locking into the P site. The next tRNA carrying the corresponding amino acid enters A site and the methonine forms a p ...
Cellular Energy and Enzymatic Function
... • Substrates bind to active site on enzyme • Binding induces conformational change in enzyme--better ”fit” for substrate • Active sites are highly specific and ...
... • Substrates bind to active site on enzyme • Binding induces conformational change in enzyme--better ”fit” for substrate • Active sites are highly specific and ...
Cyclic AMP and Hormone Action
... that work through the action of 3’-5’-cyclic AMP (cAMP) control enzymes by using ATP to phosphorylate serine and threonine groups on target enzymes. These so-called protein kinases represent a sequel of catalytic steps designed to amplify the action of the hormone. The key word here is “catalytic”, ...
... that work through the action of 3’-5’-cyclic AMP (cAMP) control enzymes by using ATP to phosphorylate serine and threonine groups on target enzymes. These so-called protein kinases represent a sequel of catalytic steps designed to amplify the action of the hormone. The key word here is “catalytic”, ...
Catalytic triad
A catalytic triad refers to the three amino acid residues that function together at the centre of the active site of some hydrolase and transferase enzymes (e.g. proteases, amidases, esterases, acylases, lipases and β-lactamases). An Acid-Base-Nucleophile triad is a common motif for generating a nucleophilic residue for covalent catalysis. The residues form a charge-relay network to polarise and activate the nucleophile, which attacks the substrate, forming a covalent intermediate which is then hydrolysed to regenerate free enzyme. The nucleophile is most commonly a serine or cysteine amino acid, but occasionally threonine. Because enzymes fold into complex three-dimensional structures, the residues of a catalytic triad can be far from each other along the amino-acid sequence (primary structure), however, they are brought close together in the final fold.As well as divergent evolution of function (and even the triad's nucleophile), catalytic triads show some of the best examples of convergent evolution. Chemical constraints on catalysis have led to the same catalytic solution independently evolving in at least 23 separate superfamilies. Their mechanism of action is consequently one of the best studied in biochemistry.