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Translation
Translation

... E. coli contains 15000 ribosomes forming 25% of the dried cell - In eukaryotic cell the ribosomes either free in the cytosol or in close association with endoplasmic reticulum (ER) - Mitochondria contains their own set of ribosomes. ...
Biosynthesis of Nucleotides Biosynthesis of Nucleotides
Biosynthesis of Nucleotides Biosynthesis of Nucleotides

... interacts with dCMP deaminase. ...
Chapter 25
Chapter 25

File
File

... group attached to the same α-carbon ...


... hydrate (figure 4). In the first step of the mechanism, the active site lysine (Lys161 in E.coli DHDPS) forms a Schiff base with pyruvate, subsequent binding of the second substrate ASA is followed by dehydration and cyclisation to form the product.42,43 Based on the X-ray crystal structure of the E ...
Amino Acids - Portal UniMAP
Amino Acids - Portal UniMAP

... Have functional group capable of forming hydrogen bonding, so easily interact with water Serine, threonine, tyrosine, asparagine, glutamine Serine, threonine, tyrosine - contain polar hydroxyl group (-OH) - Thus enable them to from hydrogen bonding (important factor in protein structure) ...
Genes & Inheritance Series: Set 3 Copyright © 2005 Version: 2.0
Genes & Inheritance Series: Set 3 Copyright © 2005 Version: 2.0

... Enzymes are specific for the reactions they catalyze. Enzyme activity depends on the enzyme’s shape and its active site (the binding site for the substrate). Enzymes are often named for the substrate on which they work, and sometimes include the suffix -ase: ...
PROTEIN METABOLISM
PROTEIN METABOLISM

...  It escapes in large amounts from dead or dying tissues and GPT (glutamate pyruvate Transaminase) may be measured in blood samples for medical diagnostic ...
Backbone sequential assigment tutorial
Backbone sequential assigment tutorial

... C', 1Ha and 15N chemical shifts for 20 proteins for which a high resolution X-ray structure is available. The computer program TALOS was developed to search this database for strings of residues with chemical shift and residue type homology. The relative importance of the weighting factors attached ...
Increasing the thermostability of sucrose
Increasing the thermostability of sucrose

Photosynthesis in the Higher Plant, Vicia.faba
Photosynthesis in the Higher Plant, Vicia.faba

CHAPTER 20 - AMINO ACID METABOLISM Introduction Amino acid
CHAPTER 20 - AMINO ACID METABOLISM Introduction Amino acid

... Also, controlling the levels (as well as the activities) of enzymes constitutes an important regulatory mechanism. Accordingly, these enzymes and proteins must be broken down as well as synthesized. Lysosomes are cellular organelles that degrade extracelllar substances that the cell takes up via end ...
1. Metabolic pathways 2. Basic enzyme kinetics 3. Metabolic
1. Metabolic pathways 2. Basic enzyme kinetics 3. Metabolic

... Non-competitive inhibition ...
AArest
AArest

... Start with PRPP and ATP: form phosphoribosyl ATP 3 reactions involving glutamine as nitrogen donor for ring lead to imidazole glycerol phosphate That gets modified and transaminated t make histidine ...
Chapter 10 Enzymes - Angelo State University
Chapter 10 Enzymes - Angelo State University

... – With the exception of some RNA molecules, all enzymes are globular proteins. – Enzymes are extremely efficient catalysts, and some can increase reaction rates by 1020 times that of the uncatalyzed reactions. • Enzymes are well suited to their roles in three major ways: they have enormous catalytic ...
Lecture 27
Lecture 27

... general base catalyst. ...
Amino Acids - UniMAP Portal
Amino Acids - UniMAP Portal

... when amino acid is dissolved in water, it exist predominantly in the isoelectric form (no net charge and electrically neutral) Upon titration with base, it act as an acid (donate proton) Upon titration with acid, it act as a base (accept proton) ...
Unusual dehydrations in anaerobic bacteria
Unusual dehydrations in anaerobic bacteria

406 PRELIMINARY NOTES Formation of lysophosphatidyl
406 PRELIMINARY NOTES Formation of lysophosphatidyl

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GENETIC CODE

... UCU (Ser/S)Serine UCC (Ser/S)Serine UCA (Ser/S)Serine UCG (Ser/S)Serine ...
Enzymes
Enzymes

Transport of Ammonia to the liver
Transport of Ammonia to the liver

... In the metabolic pathway of Amino Acids, we deal with amino group by itself then we deal with its Carbon skeleton . How can we remove the amino group from an Amino Acid ? Answer: by two ways. A. Transamination : For each Amino Acid there's a specific transaminase which removes the amino group from t ...
32 Introduction to Protein Structure Proteins are large
32 Introduction to Protein Structure Proteins are large

... The torsion angles that the atoms of the peptide bond can assume are limited by steric constraints. Some Φ / Ψ pairs will result in atoms being closer than allowed by the van der Waals radii of the atoms, and are therefore extremely unlikely to be observed because of steric clashes (for example: 0° ...
Organic Chemistry
Organic Chemistry

... • Two conformations are possible for a planar peptide bond. • Virtually all peptide bonds in naturally occurring proteins studied to date have the s-trans conformation. ...
Caffeoylquinic acids as inhibitors for HIV-I protease and HIV
Caffeoylquinic acids as inhibitors for HIV-I protease and HIV

... the fact that they do not contain any macro cycles or resemble the conformation of a β-strand protein. The results from the blind docking also support this as all molecules were docked with a very similar conformation at the active site (data not shown). Conclusion Naturally occurring caffeoylquinic ...
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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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