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E. coli
E. coli

... deprotonation of NH4+ by an Asp causes a flap (324-328) to close over active site ammonia attacks glutamyl-g-P forming tetrahedral intermediate Pi and a proton are lost The flap opens and glutamine leaves ...
Organic Chemistry/Fourth Edition: e-Text
Organic Chemistry/Fourth Edition: e-Text

nucleicacidmetabolism
nucleicacidmetabolism

... Cys439 reacts with substrate 3’-OH to form free radical at C3’ Substrate dehydrates to carbonyl at C3’ and free radical at C2’; S- formed at Cys462 Disulfide formed between Cys462,Cys225; radical regenerated at Cys439 ...
AMINO ACID METABOLISM
AMINO ACID METABOLISM

... acids are used for the synthesis of proteins in the liver and in other tissues. Carbon skeletons of excess amino acids may be oxidized for energy, converted to fatty acids, or, in some physiological situations, converted to glucose. During fasting, muscle protein is cleaved to amino acids, some of w ...
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View Full Text-PDF

The acetaminophen metabolite
The acetaminophen metabolite

Studies Into the Allosteric Regulation of ADP
Studies Into the Allosteric Regulation of ADP

abbreviations and symbols for nucleic
abbreviations and symbols for nucleic

Enzymatic activation of sulfur for incorporation into biomolecules in
Enzymatic activation of sulfur for incorporation into biomolecules in

PDH02 - OSU Biochemistry and Molecular Biology
PDH02 - OSU Biochemistry and Molecular Biology

... metabolism: the oxidative decarboxylation of pyruvate, branched chain amino acid metabolism, glycine decarboxylation, and in the citric acid cycle. Lipoic acid is formed from octanoic acid via an enzymatic S-insertion. Additional details have been learned about lipoic acid synthesis. The question of ...
9. proteins i
9. proteins i

... GENERAL STRUCTURE OF PROTEINS ...
Transamination and Reductive Amination
Transamination and Reductive Amination

... branched, and unbranched carbon side chains with up to six carbon atoms, as well as some alicyclic keto acids, as substrates; however, a substrate with the adamantyl group as a side chain, where the geometric limit seems to be reached, is not accepted. 2-Oxo-3methylpentanoic acid is the preferred su ...
The Sulphur Metabolism of Pityrosporum male and its
The Sulphur Metabolism of Pityrosporum male and its

... organisms was slightly less than the amount of methionine; the incorporation of either was inhibited by the presence of the other and both were incorporated when present together. Methionine and seleno-methionine are known to behave as a competitive pair in a similar manner to sulphate/selenate and ...
IOSR Journal of Applied Chemistry (IOSR-JAC) e-ISSN: 2278-5736.
IOSR Journal of Applied Chemistry (IOSR-JAC) e-ISSN: 2278-5736.

... lott,1985). GGT is present in serum as part of several molecular complexes,with distinct physiochemical properties(Huseby,1982;Wenham,Horn et al,1984). GGT measurement was introduced into clinical laboratories some 45 years ago, and over that times a large amount of information on factors influencin ...
Fatty Acid Biosynthesis
Fatty Acid Biosynthesis

WRL3116.tmp
WRL3116.tmp

... E. All of the above 47. The concentrations of enzymes is determined by using pseudo first-order conditions in which A. S concentration is kept the same and the rate is measured B. E concentration is kept the same and the rate is measured C. * S concentration is constant, E concentration varied and t ...
Effects of Molecular Crowding on Binding Affinity of Dihydrofolate to
Effects of Molecular Crowding on Binding Affinity of Dihydrofolate to

Deciphering the molecular basis of the specificity of protein
Deciphering the molecular basis of the specificity of protein

... determine their amino acid preferences. Two datasets have been examined. Firstly, one composed of non-covalently bound carbohydrates ligands. The results of this analysis is compared to the second dataset, obtained from the study of the spatial vicinity of the monosaccharides that form the common st ...
BIOCHEMISTRY AND MOLECULAR BIOLOGY Problem Unit Two
BIOCHEMISTRY AND MOLECULAR BIOLOGY Problem Unit Two

TETHERING: Fragment-Based Drug Discovery
TETHERING: Fragment-Based Drug Discovery

Anaerobic Glucose and Serine Metabolism in Staphy
Anaerobic Glucose and Serine Metabolism in Staphy

... Organism. Staphylococcus epidermidis was isolated in our laboratory from a contaminated culture of Peptococcrrs pre'votii. We are grateful to Dr I. Leighton (Hull Royal Infirmary) for its identification by the biochemical tests of Schleifer & Kocur (1973) and Schleifer & Kloos (1975). Growth of orga ...
Conformational Preferences of Amino Acids in Globular Proteins?
Conformational Preferences of Amino Acids in Globular Proteins?

... structure, and 0.9 < Pi;_I< 1.1 for one that is indifferent. Results and Discussion The Protein Data and Weighting Scheme. The 66 protein structures used here are listed in Table I. These proteins fall into 3 1 families of structures having up to nine members in a family (the hemoglobin family). Whe ...
The Ostrich (Struthio camelus) egg
The Ostrich (Struthio camelus) egg

Glycogen Earth organisms use three major forms of - Rose
Glycogen Earth organisms use three major forms of - Rose

... residues from preexisting glycogen molecules. Formation of new glycogen molecules requires a starting place. The starting place is provided by a protein called glycogenin discovered in the late 1980s by Bill Whelan. Glycogenin is glycosylated on the hydroxyl of a tyrosine residue; glycogenin then ac ...
A Systematic Approach to Enzyme Assay Optimization, Illustrated by
A Systematic Approach to Enzyme Assay Optimization, Illustrated by

... As stated above, our choice for the additional constraint is arbitrary. However, depending on what criterion is chosen, different substrate concentrations result. These different concentration pairs are equally valid in that they are all optimal in some way, and they all yield the same enzyme activi ...
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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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