Amino Acids, Peptides, and Proteins
... projection. Because their stereochemistry is similar to that of L-1 - 2 -glyceraldehyde, the naturally occurring (S)-amino acids are classified as L-amino acids. Although D-amino acids are occasionally found in nature, we usually assume the amino acids under discussion are the common L-amino acids. ...
... projection. Because their stereochemistry is similar to that of L-1 - 2 -glyceraldehyde, the naturally occurring (S)-amino acids are classified as L-amino acids. Although D-amino acids are occasionally found in nature, we usually assume the amino acids under discussion are the common L-amino acids. ...
Investigating the Role of ADP-forming Acetyl-CoA
... TCA cycle. Anaerobic fermentation pathways are then used for the primary flow of carbon (1). Acetate assimilation as an alternative carbon source may occur under certain conditions such as when glucose is diminished (1). Acetate is typically activated to form acetyl-CoA, a central metabolic intermed ...
... TCA cycle. Anaerobic fermentation pathways are then used for the primary flow of carbon (1). Acetate assimilation as an alternative carbon source may occur under certain conditions such as when glucose is diminished (1). Acetate is typically activated to form acetyl-CoA, a central metabolic intermed ...
Glycogen Metabolism
... Pyridoxal phosphate (PLP) is held at the active site by a Schiff base linkage, formed by reaction of the aldehyde of PLP with the e-amino group of a lysine residue. ...
... Pyridoxal phosphate (PLP) is held at the active site by a Schiff base linkage, formed by reaction of the aldehyde of PLP with the e-amino group of a lysine residue. ...
Glycogen Metabolism
... Pyridoxal phosphate (PLP) is held at the active site by a Schiff base linkage, formed by reaction of the aldehyde of PLP with the e-amino group of a lysine residue. ...
... Pyridoxal phosphate (PLP) is held at the active site by a Schiff base linkage, formed by reaction of the aldehyde of PLP with the e-amino group of a lysine residue. ...
... produced early on the 10th day, as well as a gradual disappearance of these compounds up to the 25th day. In this period, a new production of oligosaccharides and sugar monomers was detected, with a drop in these productions on the 40th day, due to its consumption by the fungal metabolism. Sugar mon ...
The shikimate pathway in apicomplexan parasites: Implications for
... finally attack of the carbanion at the C-1 keto function to close the ring to yield 3-dehydroquinate (5). The transient oxidation-reduction reaction is performed by NAD+. In addition DHQS requires either Co2+ or Zn2+ to assist catalysis (24, 25). The N-terminal domain of DHQS contains a Rossmann fol ...
... finally attack of the carbanion at the C-1 keto function to close the ring to yield 3-dehydroquinate (5). The transient oxidation-reduction reaction is performed by NAD+. In addition DHQS requires either Co2+ or Zn2+ to assist catalysis (24, 25). The N-terminal domain of DHQS contains a Rossmann fol ...
Comparison of Ligand-Binding Sites of Modeled Apo[a] Kringle
... Lp[a] contains two major and distinctly different highmolecular-weight apoproteins.5-7 Within Lp[a], apoprotein[a], apo[a], a highly glycosylated, hydrophilic protein with little apparent affinity for lipid, is disulfide-linked to one molecule of apo B-100,68-13 a highly hydrophobic apolipoprotein. ...
... Lp[a] contains two major and distinctly different highmolecular-weight apoproteins.5-7 Within Lp[a], apoprotein[a], apo[a], a highly glycosylated, hydrophilic protein with little apparent affinity for lipid, is disulfide-linked to one molecule of apo B-100,68-13 a highly hydrophobic apolipoprotein. ...
PFK - ePrints USM
... PFK production significantly. The ATP-PFK enzyme was purified by desalting (ultrafiltration) chromatography, affinity chromatography and anion exchange chromatography. The purification of ATP-PFK from L.antarcticum yielded 2.85 mg of purified PFK enzyme at a purification fold of about 1.3 with speci ...
... PFK production significantly. The ATP-PFK enzyme was purified by desalting (ultrafiltration) chromatography, affinity chromatography and anion exchange chromatography. The purification of ATP-PFK from L.antarcticum yielded 2.85 mg of purified PFK enzyme at a purification fold of about 1.3 with speci ...
Chapter 8
... At this point all of the reactions that result in reduction in carbon chain length are complete, 2 CO2 have been eliminated 2 NADH and 1 ATP have been made and we are back with a 4-carbon acid. However the acid is succinate, whereas to start a new cycle we need oxalacetate. This requires the oxidati ...
... At this point all of the reactions that result in reduction in carbon chain length are complete, 2 CO2 have been eliminated 2 NADH and 1 ATP have been made and we are back with a 4-carbon acid. However the acid is succinate, whereas to start a new cycle we need oxalacetate. This requires the oxidati ...
Cloning and functional characterization of a new subtype of the
... Received 15 January 2001; accepted in final form 16 July 2001 ...
... Received 15 January 2001; accepted in final form 16 July 2001 ...
12659942_three sites - University of Canterbury
... Tyr binding mode in site 3 In contrast to Tyr binding in site 2, specific interactions with the phenolic hydroxyl of Tyr are established when Tyr binds in site 3: the main-chain carbonyl of Pro16 and a water molecule, which in turn interacts with the backbone amide N–H of Leu261, are located 2.7 and ...
... Tyr binding mode in site 3 In contrast to Tyr binding in site 2, specific interactions with the phenolic hydroxyl of Tyr are established when Tyr binds in site 3: the main-chain carbonyl of Pro16 and a water molecule, which in turn interacts with the backbone amide N–H of Leu261, are located 2.7 and ...
NH2
... It can not be explained by transamination alone as no free ammonia is liberated nor by oxidative deamination alone as oxid. Deamination works efficiently only on glutamic acid as L- glutamate dehydrogenase is of high activity in the mammalian tissue,while the L- amino acid oxidase which works on mos ...
... It can not be explained by transamination alone as no free ammonia is liberated nor by oxidative deamination alone as oxid. Deamination works efficiently only on glutamic acid as L- glutamate dehydrogenase is of high activity in the mammalian tissue,while the L- amino acid oxidase which works on mos ...
2.2. Garrido-Franco, M. Structure E. coli
... surrounding residues (45.6 Å2) and the PNP (33.5 Å2). Attempts to refine a Pi at an equivalent position in monomer B, C and D failed as judged from B factors > 150 Å2 and negative difference electron densities. In the superposition performed with the program O [16], 242 Cα atoms of the free enzyme w ...
... surrounding residues (45.6 Å2) and the PNP (33.5 Å2). Attempts to refine a Pi at an equivalent position in monomer B, C and D failed as judged from B factors > 150 Å2 and negative difference electron densities. In the superposition performed with the program O [16], 242 Cα atoms of the free enzyme w ...
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... cardiovascular system. It is clear that thrombin aids in the formation of blood clots by catalyzing the conversion of ?brinogen to ?brin. which is an integral part of most clots. In addition. thrombin is known to act directly on cells in the blood and in the interior blood vessel wall. and speci?cal ...
... cardiovascular system. It is clear that thrombin aids in the formation of blood clots by catalyzing the conversion of ?brinogen to ?brin. which is an integral part of most clots. In addition. thrombin is known to act directly on cells in the blood and in the interior blood vessel wall. and speci?cal ...
Bacterial methionine biosynthesis
... Methionine is essential in all organisms, as it is both a proteinogenic amino acid and a component of the cofactor, S-adenosyl methionine. The metabolic pathway for its biosynthesis has been extensively characterized in Escherichia coli; however, it is becoming apparent that most bacterial species d ...
... Methionine is essential in all organisms, as it is both a proteinogenic amino acid and a component of the cofactor, S-adenosyl methionine. The metabolic pathway for its biosynthesis has been extensively characterized in Escherichia coli; however, it is becoming apparent that most bacterial species d ...
REDESIGN OF CARNITINE ACETYLTRANSFERASE SPECIFICITY BY PROTEIN ENGINEERING UNIVERSIDAD DE BARCELONA
... antibody, mitochondrial protein from yeast expressing wild-type rat CrAT (Section 3.1.) was separated by SDS-PAGE and subjected to immunoblotting using different dilutions of the anti-rat CrAT antibody, ranging from 1:3,000 to 1:10,000. Goat anti-rabbit secondary antibody was applied at a 1:6,000 di ...
... antibody, mitochondrial protein from yeast expressing wild-type rat CrAT (Section 3.1.) was separated by SDS-PAGE and subjected to immunoblotting using different dilutions of the anti-rat CrAT antibody, ranging from 1:3,000 to 1:10,000. Goat anti-rabbit secondary antibody was applied at a 1:6,000 di ...
Metabolic significance of inorganic triphosphate, thiamine
... Our laboratory has been interested for many years in thiamine triphosphate (ThTP), an unusual triphosphate derivative of thiamine (vitamin B1) found in nearly all organisms. In mammalian tissues, ThTP is hydrolyzed by a very specific cytosolic thiamine triphosphatase (ThTPase) belonging to an ancien ...
... Our laboratory has been interested for many years in thiamine triphosphate (ThTP), an unusual triphosphate derivative of thiamine (vitamin B1) found in nearly all organisms. In mammalian tissues, ThTP is hydrolyzed by a very specific cytosolic thiamine triphosphatase (ThTPase) belonging to an ancien ...
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.