The enzymic degradation of L-serine O-sulphate. Mechanism of the reaction.
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ABSTRACT:
SUBMITTER: Tudball N
PROVIDER: S-EPMC1173567 | biostudies-other | 1972 Jun
REPOSITORIES: biostudies-other
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Project description:1. By using [(18)O]water it was demonstrated that l-serine O-sulphate undergoes C-O cleavage during enzyme-catalysed degradations. 2. C-O cleavage of substrate also occurs under the agency of alkali and pyridoxal phosphate, but, as expected, acid-catalysed degradation involves S-O scission. 3. Aminoacrylate was identified as an intermediate in the enzyme-catalysed degradation of l-serine O-sulphate.
| S-EPMC1178363 | biostudies-other
Project description:1. The enzyme system of rat liver responsible for the degradation of l-serine O-sulphate was purified 300-fold and the optimum conditions for the activity were determined. 2. Inorganic sulphate, pyruvate and ammonia were found to be the products of enzyme action on lserine O-sulphate, being formed in equivalent amounts under all conditions examined. No free l-serine was detected as a product of enzyme action. 3. The enzyme preparation was free from other serine-metabolizing systems such as O-phospho-l-serine phosphatase and l-serine dehydratase. 4. The enzyme has a very narrow substrate specificity and is inactive towards a wide variety of related sulphate esters and amino acids. 5. Pyridoxal 5'-phosphate is capable of catalysing the non-enzymic breakdown of l-serine O-sulphate in the presence of metal salts to yield inorganic sulphate, pyruvate and ammonia as products. 6. The possible role of pyridoxal 5'-phosphate as a coenzyme in the enzymic degradation of l-serine O-sulphate is discussed.
| S-EPMC1198333 | biostudies-other
Project description:Non-enzymic transamination reactions at 85 degrees between various amino acids and alpha-oxoglutaric acid are catalysed by metal ions, e.g. Al(3+), Fe(2+), Cu(2+) and Fe(3+). The reaction is optimum at pH4.0. Of the 14 amino acids studied histidine is the most active. In the presence of Al(3+) histidine transaminates with alpha-oxoglutaric acid, forming glutamic acid and Al(3+)-imidazolylpyruvic acid complex as the end products. However, in the presence of Fe(2+) or Cu(2+) the products are glutamic acid and a 1:2 metal ion-imidazolylpyruvic acid chelate. The greater effectiveness of histidine in these reactions is attributed to the presence of the tertiary imidazole nitrogen atom, which is involved in the formation of stable sparingly soluble metal ion-imidazolylpyruvic acid complexes or chelates as end products of these reactions. Of the metal ions studied only Al(3+), Fe(2+), Fe(3+) and Cu(2+) are effective catalysts for the transamination reactions, and EDTA addition completely inhibits the catalytic effect of the Al(3+). Spectrophotometric evidence is presented to demonstrate the presence of metal ion complexes of Schiff bases of histidine as intermediates in the transamination reactions. These results may contribute to understanding the role of histidine in enzyme catalysis.
| S-EPMC1187772 | biostudies-other
Project description:Serine hydroxymethyltransferase catalyzes the reversible interconversion of L-serine and glycine with transfer of one-carbon groups to and from tetrahydrofolate. Active site residue Thr254 is known to be involved in the transaldimination reaction, a crucial step in the catalytic mechanism of all pyridoxal 5'-phosphate- (PLP-) dependent enzymes, which determines binding of substrates and release of products. In order to better understand the role of Thr254, we have expressed, characterized, and determined the crystal structures of rabbit cytosolic serine hydroxymethyltransferase T254A and T254C mutant forms, in the absence and presence of substrates. These mutants accumulate a kinetically stable gem-diamine intermediate, and their crystal structures show differences in the active site with respect to wild type. The kinetic and crystallographic data acquired with mutant enzymes permit us to infer that conversion of gem-diamine to external aldimine is significantly slowed because intermediates are trapped into an anomalous position by a misorientation of the PLP ring, and a new energy barrier hampers the transaldimination reaction. This barrier likely arises from the loss of the stabilizing hydrogen bond between the hydroxymethyl group of Thr254 and the ? -amino group of active site Lys257, which stabilizes the external aldimine intermediate in wild type SHMTs.
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Project description:Atomic resolution structures of trypsin acyl-enzymes and a tetrahedral intermediate analog, along with previously solved structures representing the Michaelis complex, are used to reconstruct events in the catalytic cycle of this classic serine protease. Structural comparisons provide insight into active site adjustments involved in catalysis. Subtle motions of the catalytic serine and histidine residues coordinated with translation of the substrate reaction center are seen to favor the forward progress of the acylation reaction. The structures also clarify the attack trajectory of the hydrolytic water in the deacylation reaction.
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Project description:Microcystin-LR (MCLR) is the most common cyanotoxin in contaminated aquatic systems. MCLR inhibits protein phosphatases 1 and 2A, leading to liver damage and tumor formation. MCLR is relatively stable owing to its cyclic structures. The combined UV/H2O2 technology can degrade MCLR efficiently. The second-order rate constant of the reaction between MCLR and hydroxyl radical (·OH) is 2.79(±0.23)×1010 M-1 s-1 based on the competition kinetics model using nitrobenzene as reference compound. The probable degradation pathway was analyzed through liquid chromatography mass spectrometry. Results suggested that the major destruction pathways of MCLR were initiated by ·OH attack on the benzene ring and diene of the Adda side chain. The corresponding aldehyde or ketone peptide residues were formed through further oxidation. Another minor destruction pathway involved ·OH attack on the methoxy group of the Adda side chain, followed by complete removal of the methoxy group. The combined UV/H2O2 system is a promising technology for MCLR removal in contaminated aquatic systems.
| S-EPMC4900665 | biostudies-literature
Project description:Aminoglycoside 2''-phosphotransferases are clinically important enzymes that cause high levels of resistance to aminoglycoside antibiotics by the organisms that harbor them. These enzymes phosphorylate aminoglycosides, and the modified antibiotics show significant reduction in the binding ability to target the bacterial ribosome. This report presents a detailed characterization of the antibiotic resistance profile and the aminoglycoside and nucleotide triphosphate substrate profiles of four common aminoglycoside 2''-phosphotransferases widely distributed in clinically important Gram-positive microorganisms. Although the antibiotic resistance phenotypes exhibited by these enzymes are similar, their aminoglycoside and nucleotide triphosphate substrate profiles are distinctive. Contrary to the dogma that these enzymes use ATP as the source of phosphate in their reactions, two of the four aminoglycoside 2'-phosphotransferases utilize GTP as the phosphate donor. Of the other two enzymes, one exhibits preference for ATP, and the other can utilize either ATP or GTP as nucleotide triphosphate substrate. A new nomenclature for these enzymes is put forth that takes into account the differences among these enzymes based on their respective substrate preferences. These nucleotide triphosphate preferences should have ramifications for understanding of the evolution, selection, and dissemination of the genes for these important resistance enzymes.
| S-EPMC2652286 | biostudies-literature
Project description:1. l-Serine O-sulphate and l-threonine O-sulphate are degraded in the presence of pyridoxal 5'-phosphate to yield equimolar amounts of the corresponding keto acid, ammonia and sulphate. 2. Pyridoxal catalyses the same reactions at a faster rate. 3. One of a number of bi- or ter-valent metal ions must be present for these degradations to proceed. The reaction rates are dependent on a number of factors including pH and the nature of the metal ion used. 4. Studies with related sulphate esters indicate that the alpha-hydrogen atom and the amino group are essential for activity. 5. Spectral changes during the pyridoxal and pyridoxal 5'-phosphate catalysis of l-serine O-sulphate breakdown suggest the formation of a Schiff base. 6. The mechanism for these reactions appears to be in accordance with the general mechanism proposed for pyridoxal-catalysed alphabeta-elimination reactions.
| S-EPMC1187441 | biostudies-other
Project description:Graphene represents an attractive two-dimensional carbon-based nanomaterial that holds great promise for applications such as electronics, batteries, sensors, and composite materials. Recent work has demonstrated that carbon-based nanomaterials are degradable/biodegradable, but little work has been expended to identify products formed during the degradation process. As these products may have toxicological implications that could leach into the environment or the human body, insight into the mechanism and structural elucidation remain important as carbon-based nanomaterials become commercialized. We provide insight into a potential mechanism of graphene oxide degradation via the photo-Fenton reaction. We have determined that after 1 day of treatment intermediate oxidation products (with MW 150-1000 Da) were generated. Upon longer reaction times (i.e., days 2 and 3), these products were no longer present in high abundance, and the system was dominated by graphene quantum dots (GQDs). On the basis of FTIR, MS, and NMR data, potential structures for these oxidation products, which consist of oxidized polycyclic aromatic hydrocarbons, are proposed.
| S-EPMC4025574 | biostudies-literature
Project description:1. A multienzyme system capable of degrading keratosulphates to yield galactose, N-acetylglucosamine and sulphate was found in the liver extract of a marine gastropod, Charonia lampas. 2. During the degradation, neither oligosaccharides nor sulphated sugars were produced. 3. It is suggested that the degradation could be attributed to the concerted action of beta-galactosidase, beta-N-acetylglucosaminidase and a sulphatase (sulphohydrolase), tentatively designated keratosulphatase. 4. Two forms of keratosulphatase (I and II) were separated by DEAE-Sephadex column chromatography. Both forms could release all the sulphate from keratosulphates and neither appeared to be identical with glycosulphatase or chondrosulphatase, both of which are also present in Charonia lampas. 5. beta-Galactosidase and beta-N-acetylglucosaminidase could degrade keratopolysulphate to a greater extent in the presence of keratosulphatase than in its absence. 6. It is suggested that keratosulphate was first desulphated by the action of keratosulphatase, and the desulphated polymer was then degraded to galactose and N-acetylglucosamine by the action of beta-galactosidase and beta-N-acetylglucosaminidase. 7. beta-Galactosidase alone released a small amount of galactose from shark cartilage keratopolysulphate, but beta-N-acetylglucosaminidase alone did not release N-acetylglucosamine. This indicates that unsulphated galactose residues occupy all the non-reducing terminal positions in keratopolysulphate chains.
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