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Kinetics and mechanisms of reactions catalyzed by
Kinetics and mechanisms of reactions catalyzed by

... functional criterion for distinction between lipases and esterases, namely their ability to be or not to be activated by oil/water interfaces, respectively. Interfacial activation of lipases is characterized by a sharp increase in lipolytic activity once the substrate solubility is exceeded [18,75], ...
Substrate recognition by nonribosomal peptide
Substrate recognition by nonribosomal peptide

... L-Phe-, L-Glu- and L-Asp-activating domains have been mutated, using this method, to domains activating preferentially L-Leu, L-Gln and L-Asn, respectively, as evaluated by the ATP-pyrophosphate exchange assay. Because no kinetic parameters could be determined for the activation of the noncognate am ...
Lesson 8. Enzymes
Lesson 8. Enzymes

... Enzymes are protein catalyst produced by a cell and responsible ‘for the high rate’ and specificity of one or more intracellular or extracellular biochemical reactions. Enzymes are biological catalysts responsible for supporting almost all of the chemical reactions that maintain animal homeostasis. ...
Structural and mechanistic studies of enolase George H Reed
Structural and mechanistic studies of enolase George H Reed

... by soaking substrate into crystals of Mg2+-enolase at p H 6 in 3M(NH4)zSO4 [16]. This structure revealed electron density for the substrate/product in the active site. Modeling of 2-PGA into the density suggested that the carboxylates from Glu168 and Glu211 and an intervening water might serve as th ...
A Protein Extract from Chicken Reduces Plasma Homocysteine in Rats
A Protein Extract from Chicken Reduces Plasma Homocysteine in Rats

Quantitative analysis of complex amino acids and RGD peptides by
Quantitative analysis of complex amino acids and RGD peptides by

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abstract
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... Inflammation is a complex physiological phenomenon involving chemical and enzymatic mechanisms. During this event, Polymorphonuclear Neutrophil Leukocytes (PMNs) play an important role by producing reactive oxygen species (ROS) and releasing myeloperoxidase (MPO), an oxidant enzyme. The latter one h ...
Lecture 17 Expanded Genetic Code
Lecture 17 Expanded Genetic Code

... 2) Engineer a tRNA that is orthogonal to all other tRNAs 3) Evolve an aminoacyl-tRNA synthetase to uniquely recognize this tRNA 4) Evolve a synthetase to uniquely charge this tRNA with the 21st amino acid 5) Biosynthesize or transport amino acid (most amino acids are transported into bacteria as the ...
Determination of Amino Acid Composition of Cell Culture Media and
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Effect of peptide chain length on amino acid and

... amino acid and peptide transport [4] and many diand tri-peptide bound residues have been shown to be absorbed faster than when presented in the free form [l-31. Similar observations were also made from human intestinal perfusion studies with partial enzymic hydrolysates of whole protein (consisting ...
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... • The name and abbreviation of amino acids – All the AAs were given a trivial (common) name. • Glutamate from wheat gluten. • Tyrosine from cheese (“tyros” in Greek). – Each AA is given a 3 letter abbreviation and 1 ...
Basic amino acid in the pathogenesis of caries
Basic amino acid in the pathogenesis of caries

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The Enzyme as a Catalyst
The Enzyme as a Catalyst

... accept protons in order to stabilize developing charges in the transition state. This has the effect of activating nucleophile and electrophile groups, or stabilizing leaving groups. Histidine is often the residue involved in these acid-base reactions, since it has a pKa close to neutral pH and can ...
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... itself, producing the compact 3D shape seen in ...
Computational Studies of Multi-Active Site Enzymes
Computational Studies of Multi-Active Site Enzymes

... binding of its cognate and non-cognate Thr- and Ser-AMP substrates respectively, and (ii) mechanism of hydrolytic pre-transfer editing. In contrast to bound Thr-AMP, bound SerAMP is less constrained; i.e., greater positional variability, and as a result more waters are able to permeate the active si ...
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Carbamoyl phosphate synthetase: a tunnel runs through it Hazel M
Carbamoyl phosphate synthetase: a tunnel runs through it Hazel M

... such that the reaction mechanism must be exquisitely timed. Visual inspection of the CPS model, in addition to a computational search using the software package 'GRASP' [27], indicates a possible tunnel connecting the three active sites in the (x,[3 heterodimer. This tunnel, as depicted in Figure 4, ...
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... 2. Isoleucine: This amino acid is both ketogenic and glucogenic, because its metabolism yields acetyl CoA and propionyl CoA.  The first three steps in the metabolism of isoleucine are virtually identical to the initial steps in the degradation of the other branched-chain amino acids, valine and leu ...
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... • About 80% of the excreted nitrogen is in the form of urea is produced exclusively in the liver, in a series of reactions that are distributed between the mitochondrial matrix and the cytosol. • The series of reactions that form urea is known as the Urea Cycle or the Krebs-Henseleit Cycle. • In the ...
Notes: Amino Acids and Proteins:
Notes: Amino Acids and Proteins:

... A chiral compound must contain a carbon that is bonded to four different atoms/groups. If you look at the above amino acids you will see that, with the exception of glycine, each structure is chiral around the carbon with the R group. Each amino acid will come in two structural formats, called enant ...
Function and biotechnology of extremophilic enzymes in low water
Function and biotechnology of extremophilic enzymes in low water

... archaeaon Haloarcula marismortui received considerable attention from Mevarech and co-workers [40] and the group of Zaccai [19]. The presence of clusters of acidic residues has been observed in the crystal structure of dihydrofolate reductase (DHFR) and proliferating cell nuclear antigen (PCNA) from ...
A: _____/18
A: _____/18

... Choice A: Briefly explain the concept of transition state stabilization in enzyme catalysis. Your answer should include a discussion of enthalphic versus entropic effects. Provide an example for one of these effects. The transition state is a high energy intermediate in the reaction. By reducing the ...
New insight into plant intramembrane proteases
New insight into plant intramembrane proteases

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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.
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