Chapter 25 LIPID METABOLISM
... Alpha/beta hydrolase fold 25 AS lid structure catalytic triad, asp ser his hydrolysis similar to peptidase ...
... Alpha/beta hydrolase fold 25 AS lid structure catalytic triad, asp ser his hydrolysis similar to peptidase ...
Multiple Antigen Labeling Simplified using ImmPRESS™ Reagents
... sequence, heat resistance and counterstain compatibility as well as images of each substrate are available on the Vector Labs website (www.vectorlabs.com). Repeat Steps 3-6 for detecting the second antigen. ...
... sequence, heat resistance and counterstain compatibility as well as images of each substrate are available on the Vector Labs website (www.vectorlabs.com). Repeat Steps 3-6 for detecting the second antigen. ...
The Citric acid cycle
... 1 Enzymatic reactions rates are limited by diffusion, with shorter distance between subunits a enzyme can almost direct the substrate from one subunit (catalytic site) to another. 2. Channeling metabolic intermediates between successive enzymes minimizes side reactions ...
... 1 Enzymatic reactions rates are limited by diffusion, with shorter distance between subunits a enzyme can almost direct the substrate from one subunit (catalytic site) to another. 2. Channeling metabolic intermediates between successive enzymes minimizes side reactions ...
Full Text
... emphasizes sequence variation within proteins of common structure or function. Along with the amino acids conserved at any one site, we have looked specifically for conserved correlations between amino acids at two distinct sites in a motif. We felt that if the structure of a motif was highly conser ...
... emphasizes sequence variation within proteins of common structure or function. Along with the amino acids conserved at any one site, we have looked specifically for conserved correlations between amino acids at two distinct sites in a motif. We felt that if the structure of a motif was highly conser ...
Biochemical Thermodynamics
... acids isn’t pure review for you, I strongly encourage you to read sections 2.7 to 2.10 in Horton. We won’t go over this material in detail in class because it should be review, but you do need to know it! ...
... acids isn’t pure review for you, I strongly encourage you to read sections 2.7 to 2.10 in Horton. We won’t go over this material in detail in class because it should be review, but you do need to know it! ...
Slide 1
... acid has different properties, and this in turn means that proteins can have a wide range of properties ...
... acid has different properties, and this in turn means that proteins can have a wide range of properties ...
2. Proteins have Hierarchies of Structure
... path of the main chain in an α-helix, with 3.6 residues per turn, which corresponds to 5.4 Å distance between successive turns (or 1.5 Å per residue). (B) includes the approximate positions of the main chain atoms. The atoms are labeled by the residue they belong to, starting from the N-terminus. Bl ...
... path of the main chain in an α-helix, with 3.6 residues per turn, which corresponds to 5.4 Å distance between successive turns (or 1.5 Å per residue). (B) includes the approximate positions of the main chain atoms. The atoms are labeled by the residue they belong to, starting from the N-terminus. Bl ...
Detection of the reaction intermediates catalyzed by a copper amine
... microspectroscopy and X-ray crystal structure analysis. From the measurements of UV/vis absorption spectra of the crystals it was found that the two peaks for TPQsq arose during the time course of the experiment, but the spectra for the reaction intermediates could not be observed. However, using X- ...
... microspectroscopy and X-ray crystal structure analysis. From the measurements of UV/vis absorption spectra of the crystals it was found that the two peaks for TPQsq arose during the time course of the experiment, but the spectra for the reaction intermediates could not be observed. However, using X- ...
24_Lecture
... In specific-acid catalysis, the proton is fully transferred before the slow step of the reaction ...
... In specific-acid catalysis, the proton is fully transferred before the slow step of the reaction ...
Amino Acids, Proteins, and Enzymes
... 3) isomerase 4) synthetase A. Converts a cis-fatty acid to a trans-fatty acid. B. Removes 2 H atoms to form a double bond. C. Combines two molecules to make a new compound. D. Adds NH3. ...
... 3) isomerase 4) synthetase A. Converts a cis-fatty acid to a trans-fatty acid. B. Removes 2 H atoms to form a double bond. C. Combines two molecules to make a new compound. D. Adds NH3. ...
Chapter 22 Biosynthesis of amino acids, nucleotides and related
... • The activity of PII, in turn, is regulated by the uridylylation of a specific Tyr residue: PII-UMP stimulates the adenylylation activity of AT, however, the unmodified PII stimulates the deadenylylation activity of AT. • The addition and removal of UMP to PII, in turn, are again catalyzed by two ...
... • The activity of PII, in turn, is regulated by the uridylylation of a specific Tyr residue: PII-UMP stimulates the adenylylation activity of AT, however, the unmodified PII stimulates the deadenylylation activity of AT. • The addition and removal of UMP to PII, in turn, are again catalyzed by two ...
HYDROLYSIS OF THE PEPTIDE BOND AND AMINO ACID
... Moreover, the hydrolysis conditions are not as exacting-the reducing nature of the acid is apparently safeguard enough against oxidations which may occur during hydrolyses with hydrochloric acid if traces of oxidants or metals are left in the reagent tube. Iodine (admittedly not a strong oxidizing a ...
... Moreover, the hydrolysis conditions are not as exacting-the reducing nature of the acid is apparently safeguard enough against oxidations which may occur during hydrolyses with hydrochloric acid if traces of oxidants or metals are left in the reagent tube. Iodine (admittedly not a strong oxidizing a ...
Enzymes, ATP and Bioenergetics
... Catalysts increase the rate of chemical reactions (speed them up) hundreds or thousands of times, but they cannot cause chemical reactions to occur that would not otherwise be possible. Enzymes and ribozymes are not changed by the reactions they catalyze, so can be used over and over again. Though m ...
... Catalysts increase the rate of chemical reactions (speed them up) hundreds or thousands of times, but they cannot cause chemical reactions to occur that would not otherwise be possible. Enzymes and ribozymes are not changed by the reactions they catalyze, so can be used over and over again. Though m ...
... “designability” has been demonstrated[25] and whose biotechnological relevance has been established.[26] Directed evolution allows us to engineer into this enzyme functions not required or permitted in its natural biological context. For example, a P450 BM-3 variant which efficiently hydroxylates al ...
Enzyme
... Stored at high concentration, as lyophilized powders, or in a concentrated (NH4)2SO4 solution Some proteases may go through autolysis during storage. Some enzymes are easier to subject to denaturation at low concentrations. Stored at low temperatures Be careful: freeze-thaw cycles would inac ...
... Stored at high concentration, as lyophilized powders, or in a concentrated (NH4)2SO4 solution Some proteases may go through autolysis during storage. Some enzymes are easier to subject to denaturation at low concentrations. Stored at low temperatures Be careful: freeze-thaw cycles would inac ...
pdf file - 366KB
... catalytic Michael addition of a cysteine residue (Cys 146) to C6 of dUMP, generating the dUMP enolate, able to attack either the cyclic or open form of methylenetetrahydrofolate. Apparently, the preferred way is the much more reactive Mannich basic form of the N5iminium ion of methylenetetrahydrofol ...
... catalytic Michael addition of a cysteine residue (Cys 146) to C6 of dUMP, generating the dUMP enolate, able to attack either the cyclic or open form of methylenetetrahydrofolate. Apparently, the preferred way is the much more reactive Mannich basic form of the N5iminium ion of methylenetetrahydrofol ...
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.