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Biocatalysis - School of Chemical Sciences
Biocatalysis - School of Chemical Sciences

... and fewer environmental problems. Other advantages, like high catalytic efficiency and mild operational conditions, are also very attractive in commercial applications. The characteristics of limited operating regions, substrate or product inhibition, and reactions in aqueous solutions have often bee ...
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... Basic*Chemical*Reac)ons* •  Backbone:'common'to'all'amino'acids' –  Amines'and'carboxylic'acids'undergo'dehydration'to'form'amides' –  Peptides'are'polyamides'formed'by'α7amino'acids' ...
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A1121 SD1 - Food Standards Australia New Zealand
A1121 SD1 - Food Standards Australia New Zealand

... processing (Pariza and Johnson, 2001). Protease derived from A. melleus was marketed as a digestive aid in North America prior to 1994 (ETA, 2015). Further, protease derived from A. melleus is included on the Association of Manufacturers and Formulators of Enzyme Products (AMFEP, 2015) list of comme ...
Title: Author - Department of Biochemistry and Molecular Biology
Title: Author - Department of Biochemistry and Molecular Biology

Motif recognition - www.bioinf.org.uk
Motif recognition - www.bioinf.org.uk

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4 Titration Curve of an Amino Acid
4 Titration Curve of an Amino Acid

... A few amino acids are classified as triprotic. This is because, in addition to the ionizable protons of the α-COOH and α-NH3 groups, they also have a dissociable proton in their R group. Although triprotic amino acids can exist as zwitterions, under physiological conditions these amino acids will be ...
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... al , 1987). This supports an unusually short Fe=O bond which is measured to be 1.67 Å by EXAFS (Chance et al., 1986). The heme group is located between two protein helices, and completely covered except for the edges of pyrrole rings A and D; it can be reached by the oxidant through a well-designed ...
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... activity in A. ambisexualis. Among individual amino acids only L-methionine induced a tropic response (Table 1a). The reorientation of hyphal tips (Fig. 1d) in response to changed positions of methionine-containing donor blocks is consistent with the conclusion that this compound is chemotropically ...
1 enzyme catalysis lab protocol
1 enzyme catalysis lab protocol

... the temperature increases, more of the reacting molecules have enough kinetic energy to undergo the reaction. Since enzymes are catalysts for chemical reactions, enzyme reactions also tend to go faster with increasing temperature. However, if the temperature of an enzyme-catalyzed reaction is raised ...
Cyclooxygenase mechanisms Lawrence J Marnett
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... expected, it is positioned close to C-13 in both structures. In addition, Trp387 is close to the endoperoxide group in the COX-2–PGH2 crystal structure, suggesting that it may restrict the conformation of the 11-peroxyl radical to facilitate cyclization at C-9 [11••]. Indeed, mutation of Trp387 to P ...
INDIGO-BINDING DOMAINS IN CELLULASE MOLECULES
INDIGO-BINDING DOMAINS IN CELLULASE MOLECULES

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Amino Acids: An Introduction to Their Structure, Functions and

... carbon atoms covalently bonded to each other (Image at right). To one carbon atom, two oxygen atoms are bonded; to the other carbon atom, an amino group (NH3+) and 2 hydrogen atoms are bonded. The carbon that is directly attached to the CO2- is called the -carbon. It is this carbon that makes all a ...
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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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