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The Citric acid cycle (2)
The Citric acid cycle (2)

... • It also has a central role in gluconeogenesis, lipogenesis, and interconversion of amino acids. – So, components of the cycle have a direct or indirect controlling effects in key enzymes of other pathways. ...
Sixth Southeast Enzyme Conference
Sixth Southeast Enzyme Conference

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... Polyprotic systems-acids or bases can donate or accept more than one proton. Diprotic systems (with two acidic or basic sites). ...
Enzymes - Clayton State University
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... substrate, the lower the [S] range in which the enzyme is effective • Vmax is important, as a measure of the potential maximum rate of the reaction • By knowing Vmax, Km, and the in vivo substrate concentration, we can estimate the likely rate of the reaction under cellular conditions © 2012 Pearson ...
Structural and Biochemical Characterization of a Bifunctional
Structural and Biochemical Characterization of a Bifunctional

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Krebs Cycle - USD Home Pages

... -­‐  increases  local  concentration  of  substrate  for  each  subunit    -­‐  multi-­‐enz  complexes  allows  little  chance  for  diffusion  and  side  reactions  and     direct  transfer  of  substrate  from  E1  to  E2  to  E3   ...
Digestive enzymes of the West African giant land snail, Archachatina
Digestive enzymes of the West African giant land snail, Archachatina

Identification of Surface Residues Involved in Protein
Identification of Surface Residues Involved in Protein

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Chemical Biology - Chem 370 (3 credits)
Chemical Biology - Chem 370 (3 credits)

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CH - IS MU
CH - IS MU

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Amino Acids

... their side chains. The simplest amino acid is glycine, which contains a hydrogen in place of the side chain. The other six amino acids in group A contain alkyl or aryl hydrocarbon side chains. Proline differs slightly from the other amino acids in Table below. It contains a secondary rather than a ...
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... of NO in response to infection or injury can result in arterial expansion and may ultimately lead to cardiovascular collapse. In order to maintain acceptable cardiovascular function under such conditions, it is important for the availability of NO to be controlled efficiently. This can be achieved us ...
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... • However, they are important in vision, bone formation, antioxidants, and blood clotting • Fat soluble vitamins are stored in the body, so should not be consumed in excess, as they can be toxic at high levels ...
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lecture notes

... From Figure C.1B, it should be apparent that amino acids readily react as acids and bases. In aqueous solution, only a miniscule fraction of the total number of dissolved molecules in fact exist as "amino acids". Perhaps a more appropriate name might be "ammonium carboxylates". The αamino group is ...
Structural Features of Angiotensin-I Converting Enzyme Catalytic Sites
Structural Features of Angiotensin-I Converting Enzyme Catalytic Sites

... (RAS) [1-3]. Renin is responsible for the liberation of Angiotensin I (AI) in blood, after renin’s catalytic action on the angiotensinogen. ACE possesses a crucial role in the regulation of blood pressure since it catalyzes the cleavage of the C-terminal His-Leu dipeptide of the rather inactive deca ...
Amino Acid Oxidation, the Production of Urea, and Amino Acid
Amino Acid Oxidation, the Production of Urea, and Amino Acid

Protein mteabolism
Protein mteabolism

... I- Removal of α-amino group: The removal of amino group takes place in two steps which are Transamination (that produce glutamate) followed by oxidative deamination of the produced glutamate to give ammonia. Transamination: is the transfer of α-amino group from α-amino acid to α-keto acid to yield ...
Nitrogen Assimilation 1. Introduction and Overview Importance of
Nitrogen Assimilation 1. Introduction and Overview Importance of

Synthesis of Phosphopeptides Containing O
Synthesis of Phosphopeptides Containing O

... the most widespread and important reactions in the regulation of cellular processes. Specific serine, threonine, or tyrosine residues in substrate proteins become phosphorylated by the action of protein kinases that catalyze the transfer of phosphate from high-energy nucleoside triphosphate. Major p ...
NH 2
NH 2

... hist) , these a.a are +ve charged at physiological pH and can form ionic bonds with acidic amino acids. ...
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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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