L -Glutamic acid (G1251) - Product Information Sheet - Sigma
... pI: 3.081 pKa: 2.10 (α-COOH), 9.47 (α-NH2), 4.07 (ϕ-COOH)1 Specific Rotation: D +31.4 ° (6 N HCl, 22.4 °C)2 Synonyms: (S)-2-aminoglutaric acid, (S)-2aminopentanedioic acid, 1-aminopropane-1,3dicarboxylic acid, Glu2 L-Glutamic acid is one of the two amino acids that contains a carboxylic acid group i ...
... pI: 3.081 pKa: 2.10 (α-COOH), 9.47 (α-NH2), 4.07 (ϕ-COOH)1 Specific Rotation: D +31.4 ° (6 N HCl, 22.4 °C)2 Synonyms: (S)-2-aminoglutaric acid, (S)-2aminopentanedioic acid, 1-aminopropane-1,3dicarboxylic acid, Glu2 L-Glutamic acid is one of the two amino acids that contains a carboxylic acid group i ...
Chapter 16 - The Citric Acid Cycle
... •NAD+ and HS-CoA are cosubstrates •TPP, lipoate and FAD are prosthetic groups •ATP is a regulator of the PDH complex •Lipoamide (on E2) acts as a “swinging arm” to transfer the two carbon unit from the active site of E1 to the active site of E3 (substrate channeling) ...
... •NAD+ and HS-CoA are cosubstrates •TPP, lipoate and FAD are prosthetic groups •ATP is a regulator of the PDH complex •Lipoamide (on E2) acts as a “swinging arm” to transfer the two carbon unit from the active site of E1 to the active site of E3 (substrate channeling) ...
HL Construct your own polypeptide
... Can you construct a polypeptide and fold it into a quaternary structure? You will be given a fictional ‘protein’ to construct that is 10 amino acids in length You will need to show all 4 stages of folding (primary, secondary both beta sheet and alpha helix) on your poster including any bonds that ca ...
... Can you construct a polypeptide and fold it into a quaternary structure? You will be given a fictional ‘protein’ to construct that is 10 amino acids in length You will need to show all 4 stages of folding (primary, secondary both beta sheet and alpha helix) on your poster including any bonds that ca ...
OCHeM.com ©1999 Thomas Poon Amino Acids, Peptides, and
... Be able to predict the structure of any amino acid based on its pKa values and the pH of the surrounding solution. The Henderson-Hasselbalch equation can be used to determine the major form of an amino acid at any pH. In general, if the pKa < pH a protic functional group will be “more acidic than th ...
... Be able to predict the structure of any amino acid based on its pKa values and the pH of the surrounding solution. The Henderson-Hasselbalch equation can be used to determine the major form of an amino acid at any pH. In general, if the pKa < pH a protic functional group will be “more acidic than th ...
Slide 1
... •Need to model side-chains where these differ from aligned template sequence •Search database for all occurrences of given side-chain in backbone conformation and minimal clash with neighbouring residues •Computationally prohibitive •Library of rotamers •Collection of conformations for each residue ...
... •Need to model side-chains where these differ from aligned template sequence •Search database for all occurrences of given side-chain in backbone conformation and minimal clash with neighbouring residues •Computationally prohibitive •Library of rotamers •Collection of conformations for each residue ...
Chem*3560 Lecture 27: Membrane transport
... If the channel binds a solute too tightly, it will enter the channel easily, but now there's an activation energy barrier for the solute to reenter the aqueous solution on the other side. ...
... If the channel binds a solute too tightly, it will enter the channel easily, but now there's an activation energy barrier for the solute to reenter the aqueous solution on the other side. ...
How ribosomes make peptide bonds
... catalysis and indicates that general acid–base catalysis is not used to a great extent. Peptide-bond formation between full-length peptidyl-tRNA and aa-tRNAs with a native amino group is also independent of pH [22]. Although the accommodation step, which is rate-limiting, might mask part of a potent ...
... catalysis and indicates that general acid–base catalysis is not used to a great extent. Peptide-bond formation between full-length peptidyl-tRNA and aa-tRNAs with a native amino group is also independent of pH [22]. Although the accommodation step, which is rate-limiting, might mask part of a potent ...
PMC-AT Enzyme Engineering Research Overview.
... φ,ψ = the backbone torsion angles Backbone = the sequence of (COOH)-[N-(CH-Ri)-(C=O)]N-NH2 , where Ri is the i'th side chain. 2N torsion angles specify the backbone configuration. ...
... φ,ψ = the backbone torsion angles Backbone = the sequence of (COOH)-[N-(CH-Ri)-(C=O)]N-NH2 , where Ri is the i'th side chain. 2N torsion angles specify the backbone configuration. ...
Active site mapping, biochemical properties and
... Received 8 June 2001; received in revised form 31 July 2001; accepted 21 August 2001 ...
... Received 8 June 2001; received in revised form 31 July 2001; accepted 21 August 2001 ...
Journal of Molecular Biology
... TIM-barrel fold, whereas the microbial enzymes are classified as members of family 16 with a b-sandwich architecture. b-Glucanases are retaining glycosidases2 acting by general acid/base catalysis in a double-displacement reaction mechanism.3,4 Depolymerization of b-D-glucans involves two Sn2-type n ...
... TIM-barrel fold, whereas the microbial enzymes are classified as members of family 16 with a b-sandwich architecture. b-Glucanases are retaining glycosidases2 acting by general acid/base catalysis in a double-displacement reaction mechanism.3,4 Depolymerization of b-D-glucans involves two Sn2-type n ...
Chapter 15
... - When it is bonded to enzyme, change the shape of enzyme (active site) and substrate cannot fit in the active site (change tertiary structure). - Like heavy metal ions (Pb2+, Ag+, or Hg2+) that bond with –COO-, or –OH groups of amino acid in an enzyme. - Penicillin inhibits an enzyme needed for for ...
... - When it is bonded to enzyme, change the shape of enzyme (active site) and substrate cannot fit in the active site (change tertiary structure). - Like heavy metal ions (Pb2+, Ag+, or Hg2+) that bond with –COO-, or –OH groups of amino acid in an enzyme. - Penicillin inhibits an enzyme needed for for ...
General pathways of amino acids transformation
... alanine aminotransferase alanine + -ketoglutarate pyruvate + glutamate aspartate aminotransferase aspartate + -ketoglutarate oxaloacetate + glutamate Aminotransferases funnel -amino groups from a variety of amino acids to -ketoglutarate with glutamate formation Glutamate can be deaminated wi ...
... alanine aminotransferase alanine + -ketoglutarate pyruvate + glutamate aspartate aminotransferase aspartate + -ketoglutarate oxaloacetate + glutamate Aminotransferases funnel -amino groups from a variety of amino acids to -ketoglutarate with glutamate formation Glutamate can be deaminated wi ...
Arg305 of Streptomyces l-glutamate oxidase plays a crucial role for
... tested by the MBTH method with 0.5 mM L-tyrosine, 1 mM L-tryptophan and L-aspartate, 5 mM L-leucine, and 10 mM other substrates with the purified enzymes. Effects of pH on activity were examined using Britton-Robinson buffer at a pH range of 4.0–12.0. The activities were measured by the MBTH method a ...
... tested by the MBTH method with 0.5 mM L-tyrosine, 1 mM L-tryptophan and L-aspartate, 5 mM L-leucine, and 10 mM other substrates with the purified enzymes. Effects of pH on activity were examined using Britton-Robinson buffer at a pH range of 4.0–12.0. The activities were measured by the MBTH method a ...
Amino Acid Catabolism
... • Amino acids from degraded proteins or from diet can be used for the biosynthesis of new proteins • During starvation proteins are degraded to amino acids to support glucose formation • First step is often removal of the α-amino group • Carbon chains are altered for entry into central pathways of c ...
... • Amino acids from degraded proteins or from diet can be used for the biosynthesis of new proteins • During starvation proteins are degraded to amino acids to support glucose formation • First step is often removal of the α-amino group • Carbon chains are altered for entry into central pathways of c ...
BIOC*4540 ENZYMOLOGY Winter 2015
... and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding, 2nd edition (1999), Alan Fersht, W.H. Freeman and Co. New York, NY 1999. A copy of each of these texts has been placed on reserve for reference purposes. Also, a number of related texts have been placed on reserve ...
... and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding, 2nd edition (1999), Alan Fersht, W.H. Freeman and Co. New York, NY 1999. A copy of each of these texts has been placed on reserve for reference purposes. Also, a number of related texts have been placed on reserve ...
Enzymes
... 1. Covalent catalysis. In covalent catalysis, the active site contains a reactive group, usually a powerful nucleophile that becomes temporarily covalently modified in the course of catalysis. The proteolytic enzyme chymotrypsin provides an excellent example of this mechanism. ...
... 1. Covalent catalysis. In covalent catalysis, the active site contains a reactive group, usually a powerful nucleophile that becomes temporarily covalently modified in the course of catalysis. The proteolytic enzyme chymotrypsin provides an excellent example of this mechanism. ...
By P. R. CARNEGIE Russell Grimwade School of Biochemitry
... of this zone for 5hr. at 1050 yielded serine and a small amount of alanine. Acetohydrazine was identified by paper electrophoresis at pH 2-1. Samples of N-acetylalanine and N-acetylglycine were used as reference compounds. Acetohydrazine had a mobility relative to lysine of 0-9. Therefore the sequen ...
... of this zone for 5hr. at 1050 yielded serine and a small amount of alanine. Acetohydrazine was identified by paper electrophoresis at pH 2-1. Samples of N-acetylalanine and N-acetylglycine were used as reference compounds. Acetohydrazine had a mobility relative to lysine of 0-9. Therefore the sequen ...
Chapter 3 Problem Set
... Lys) then the pI of the protein will be high. Conversely, if it has a relatively large number of acidic residues (Asp, Glu), then the protein will have a low pI. Histones have high pI values because they have large numbers of His, Arg, and Lys residues. Because the side-chains of these residues are ...
... Lys) then the pI of the protein will be high. Conversely, if it has a relatively large number of acidic residues (Asp, Glu), then the protein will have a low pI. Histones have high pI values because they have large numbers of His, Arg, and Lys residues. Because the side-chains of these residues are ...
ENZYMES
... Once formed, they are released from the active site Enzyme is free to act on another substrate ...
... Once formed, they are released from the active site Enzyme is free to act on another substrate ...
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.