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Oxidation of fatty acids in eukaryotes
Oxidation of fatty acids in eukaryotes

... The evidence for this mechanism was primarily derived from a study of acetyl-CoA synthetase. Although the postulated intermediate, acetyl-AMP, does not accumulate in solution, and therefore only exists bound to the enzyme, the indirect evidence for this intermediate is very compelling. Other fatty a ...
41 Purine and Pyrimidine Metabolism
41 Purine and Pyrimidine Metabolism

BIOSYNTHESIS OF AMINO ACIDS, NUCLEOTIDES, AND
BIOSYNTHESIS OF AMINO ACIDS, NUCLEOTIDES, AND

... other amino acids, through transamination reactions (the reverse of the reaction shown in Fig. 18–4). The amide nitrogen of glutamine is a source of amino groups in a wide range of biosynthetic processes. In most types of cells, and in extracellular fluids in higher organisms, one or both of these a ...
Extended spectrum beta-lactamases - Micro-Rao
Extended spectrum beta-lactamases - Micro-Rao

microbial metabolism of oxalate and one
microbial metabolism of oxalate and one

... tion by NADPH to glyoxylatc which initiates the synthesis of cell constituents. A major factor controlling thesc two alternative pathways is probably the relative levels of reduced and oxidized pyridine n~lcleotid~~, These levels would enable a sensitive balance to be maintained [lg]. (b) The oxalyl ...
Biochemical and physiological bases for utilization
Biochemical and physiological bases for utilization

Carbohydrate metabolism
Carbohydrate metabolism

... •Epinephrine stimulates α1 adrenergic receptors in liver → activation of phospholipase-C which hydrolyses phosphatidyl inositol–P2 into 1,2 diacylglycerol and inositol triphosphate → release Ca++ from its intracellular stores into the cytoplasm raising the intracytoplasmic concentration of Ca++ whic ...
Amino Acid Catabolism: C
Amino Acid Catabolism: C

... Homolytic cleavage of the deoxyadenosyl C-Co bond during catalysis yields a deoxyadenosyl carbon radical, as Co3+ becomes Co2+. Reaction of this with methylmalonyl-CoA generates a radical substrate intermediate and 5'-deoxyadenosine. Following rearrangement of the substrate, the product radical abs ...
Amino Acid Catabolism: C
Amino Acid Catabolism: C

... Homolytic cleavage of the deoxyadenosyl C-Co bond during catalysis yields a deoxyadenosyl carbon radical, as Co3+ becomes Co2+. Reaction of this with methylmalonyl-CoA generates a radical substrate intermediate and 5'-deoxyadenosine. Following rearrangement of the substrate, the product radical abs ...
risk and technical assessment report
risk and technical assessment report

... were no concerns with the safety of B. circulans, when used as a source of β-galactosidase. Question 2: What is the risk to the public from the use of β-galactosidase derived from B. circulans as a processing aid? No safety concerns with the use of this enzyme as a processing aid were raised. The sa ...
X-ray crystal structure of plasmin with tranexamic
X-ray crystal structure of plasmin with tranexamic

Transamination and asymmetry in glutamate transport across the
Transamination and asymmetry in glutamate transport across the

High pKa variability of cysteine residues in structural databases and
High pKa variability of cysteine residues in structural databases and

... these oxidations are effectively counteracted through natural defensive mechanisms [9]; however, intense and/or persistent levels of ROS stress ultimately lead to protein damage (misfolding, cross-linkages, inactivation of functional residues) [10,11]. A critically important aspect of Cys reactivity ...
Ser Trp Thr His Glu Asn Gly Lys His Val Trp Arg
Ser Trp Thr His Glu Asn Gly Lys His Val Trp Arg

... Biomolecular folding is a type of molecular self-assembly in which self-interaction drives a molecule to its native conformation. We synthesized six 12-amino acid β-hairpin peptides stabilized by π-π interactions between the indole groups of two tryptophan residues. Histidine binding pockets of vary ...
REDESIGN OF CARNITINE ACETYLTRANSFERASE SPECIFICITY BY PROTEIN ENGINEERING UNIVERSIDAD DE BARCELONA
REDESIGN OF CARNITINE ACETYLTRANSFERASE SPECIFICITY BY PROTEIN ENGINEERING UNIVERSIDAD DE BARCELONA

... A novel compound, the fatty acid synthase (FAS) inhibitor C75, has been proposed to pharmacologically regulate CPT I activity (Price, 2001). Structurally, C75 is a cell-permeable α-methylene-γ-butyrolactone designed to be less reactive and potentially safer than cerulenin, a natural product obtained ...
as a PDF
as a PDF

... of the mienteric plexuses and infiltration of lymphocytes. In this phase parasites are rarely found. Clinically, there is a third form called latent or subclinical or indeterminate form. It will start immediately after the acute episode and may last lifelong. Patients do not have symptoms and may no ...
a guide-book to biochemistry
a guide-book to biochemistry

Identification of a Chloroplast-encoded 9-kDa
Identification of a Chloroplast-encoded 9-kDa

Predicting DNA-binding sites of proteins from amino acid sequence
Predicting DNA-binding sites of proteins from amino acid sequence

Purification and properties of NADP +-dependent
Purification and properties of NADP +-dependent

Evolution of the Aldose Reductase-Related Gecko Eye Lens Protein
Evolution of the Aldose Reductase-Related Gecko Eye Lens Protein

... these sequences (not shown) confirmed that this superfamily of proteins, the aldo-keto reductases, is highly divergent, with multiple representatives in diverse proand eukaryotes. However, most vertebrate sequences clustered together, as observed earlier (Jez et al. 1997; Seery et al. 1998). Therefo ...
NAD - SBI
NAD - SBI

... • There is a minimum structure conserved in most proteins: first motif (βαβαβ) and β4. β1 and β4 are located in the center of the NAD-binding domain and are involved in cofactor binding. • The fingerprint region (βαβ) is conserved in all proteins and have several conserved residues important for its ...
Slide 1
Slide 1

... No sequence conservation with other PTPs  Asp383 of Cdc25A was implicated as catalytic acid on the basis of reduction of activity of D383N mutant. ...
Malonate decarboxylase of Pseudomonas putida is composed of
Malonate decarboxylase of Pseudomonas putida is composed of

Angiotensin I Converting Enzyme and the Changes
Angiotensin I Converting Enzyme and the Changes

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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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