scholarly journals The role of magnesium in the hydrolysis of sodium pyrophosphate by inorganic pyrophosphatase

1954 ◽  
Vol 57 (1) ◽  
pp. 87-92 ◽  
Author(s):  
Leah Bloch-Frankenthal
Keyword(s):  
Sodium Pyrophosphate ◽  
Inorganic Pyrophosphatase ◽  
Hydrolysis Of

scholarly journals A STUDY OF THE NUCLEOSIDE TRI- AND DIPHOSPHATE ACTIVITIES OF RAT LIVER MICROSOMES

1962 ◽  
Vol 15 (3) ◽  
pp. 563-578 ◽  
Author(s):  
Lars Ernster ◽  
Lois C. Jones
Keyword(s):  
Rat Liver ◽  
Liver Microsomes ◽  
Physiological Role ◽  
Sodium Deoxycholate ◽  
Inorganic Pyrophosphatase ◽  
Rat Liver Microsomes ◽  
High Concentrations ◽  
Hydrolysis Of ◽  
No Activation

Rat liver microsomes catalyze the hydrolysis of the triphosphates of adenosine, guanosine, uridine, cytidine, and inosine into the corresponding diphosphates and inorganic orthophosphate. The activities are stimulated by Na2S2O4, and inhibited by atebrin, chlorpromazine, sodium azide, and deaminothyroxine. Sodium deoxycholate inhibits the ATPase activity in a progressive manner; the release of orthophosphate from GTP and UTP is stimulated by low, and inhibited by high, concentrations of deoxycholate, and that from CTP and ITP is unaffected by low, and inhibited by high, concentrations of deoxycholate. Subfractionation of microsomes with deoxycholate into ribosomal, membrane, and soluble fractions reveals a concentration of the triphosphatase activity in the membrane fraction. Rat liver microsomes also catalyze the hydrolysis of the diphosphates of the above nucleosides into the corresponding monophosphates and inorganic orthophosphate. Deoxycholate strongly enhances the GDPase, UDPase, and IDPase activities while causing no activation or even inhibition of the ADPase and CDPase activities. The diphosphatase is unaffected by Na2S2O4 and is inhibited by azide and deaminothyroxine but not by atebrin or chlorpromazine. Upon fractionation of the microsomes with deoxycholate, a large part of the GDPase, UDPase, and IDPase activities is recovered in the soluble fraction. Mechanical disruption of the microsomes with an Ultra Turrax Blender both activates and releases the GDPase, UDPase, and IDPase activities, and the former effect occurs more readily than the latter. The GDPase, UDPase, and IDPase activities of the rat liver cell reside almost exclusively in the microsomal fraction, as revealed by comparative assays of the mitochondrial, microsomal, and final supernatant fractions of the homogenate. The microsomes exhibit relatively low nucleoside monophosphatase and inorganic pyrophosphatase activities, and these are unaffected by deoxycholate or mechanical treatment. Different approaches toward the function of the liver microsomal nucleoside tri- and diphosphatases are reported, and the possible physiological role of the two enzymes is discussed.

scholarly journals Steroid Sulphatase and Its Inhibitors: Past, Present and Future

Molecules ◽  
2021 ◽  
Vol 26 (10) ◽  
pp. 2852
Author(s):  
Paul A. Foster
Keyword(s):  
Good Evidence ◽  
The Past ◽  
Steroid Sulphatase ◽  
University Of Oxford ◽  
Therapeutic Value ◽  
Breast And Prostate Cancer ◽  
The University ◽  
Further Development ◽  
Hydrolysis Of

Steroid sulphatase (STS), involved in the hydrolysis of steroid sulphates, plays an important role in the formation of both active oestrogens and androgens. Since these steroids significantly impact the proliferation of both oestrogen- and androgen-dependent cancers, many research groups over the past 30 years have designed and developed STS inhibitors. One of the main contributors to this field has been Prof. Barry Potter, previously at the University of Bath and now at the University of Oxford. Upon Prof. Potter’s imminent retirement, this review takes a look back at the work on STS inhibitors and their contribution to our understanding of sulphate biology and as potential therapeutic agents in hormone-dependent disease. A number of potent STS inhibitors have now been developed, one of which, Irosustat (STX64, 667Coumate, BN83495), remains the only one to have completed phase I/II clinical trials against numerous indications (breast, prostate, endometrial). These studies have provided new insights into the origins of androgens and oestrogens in women and men. In addition to the therapeutic role of STS inhibition in breast and prostate cancer, there is now good evidence to suggest they may also provide benefits in patients with colorectal and ovarian cancer, and in treating endometriosis. To explore the potential of STS inhibitors further, a number of second- and third-generation inhibitors have been developed, together with single molecules that possess aromatase–STS inhibitory properties. The further development of potent STS inhibitors will allow their potential therapeutic value to be explored in a variety of hormone-dependent cancers and possibly other non-oncological conditions.

scholarly journals Regulation of the synthesis and hydrolysis of ATP by mitochondrial ATPase. Role of Mg2+.

1983 ◽  
Vol 258 (22) ◽  
pp. 13673-13679 ◽  
Author(s):  
A Gómez-Puyou ◽  
G Ayala ◽  
U Muller ◽  
M Tuena de Gómez-Puyou
Keyword(s):  
Mitochondrial Atpase ◽  
Hydrolysis Of

The role of pretreatment in improving the enzymatic hydrolysis of lignocellulosic materials

2016 ◽  
Vol 199 ◽  
pp. 49-58 ◽  
Author(s):  
Shaoni Sun ◽  
Shaolong Sun ◽  
Xuefei Cao ◽  
Runcang Sun
Keyword(s):  
Enzymatic Hydrolysis ◽  
Lignocellulosic Materials ◽  
Hydrolysis Of

scholarly journals “Newton’s cradle” proton relay with amide–imidic acid tautomerization in inverting cellulase visualized by neutron crystallography

2015 ◽  
Vol 1 (7) ◽  
pp. e1500263 ◽  
Author(s):  
Akihiko Nakamura ◽  
Takuya Ishida ◽  
Katsuhiro Kusaka ◽  
Taro Yamada ◽  
Shinya Fushinobu ◽  
...  
Keyword(s):  
Glycoside Hydrolases ◽  
Side Chain ◽  
Enzymatic Reactions ◽  
X Ray Diffraction ◽  
Peptide Bonds ◽  
Proton Relay ◽  
Newton’S Cradle ◽  
Dynamics Simulations ◽  
Hydrolysis Of

Hydrolysis of carbohydrates is a major bioreaction in nature, catalyzed by glycoside hydrolases (GHs). We used neutron diffraction and high-resolution x-ray diffraction analyses to investigate the hydrogen bond network in inverting cellulase PcCel45A, which is an endoglucanase belonging to subfamily C of GH family 45, isolated from the basidiomycete Phanerochaete chrysosporium. Examination of the enzyme and enzyme-ligand structures indicates a key role of multiple tautomerizations of asparagine residues and peptide bonds, which are finally connected to the other catalytic residue via typical side-chain hydrogen bonds, in forming the “Newton’s cradle”–like proton relay pathway of the catalytic cycle. Amide–imidic acid tautomerization of asparagine has not been taken into account in recent molecular dynamics simulations of not only cellulases but also general enzyme catalysis, and it may be necessary to reconsider our interpretation of many enzymatic reactions.

scholarly journals The role of cellulase concentration in determining the degree of synergism in the hydrolysis of microcrystalline cellulose

1988 ◽  
Vol 255 (3) ◽  
pp. 895-899 ◽  
Author(s):  
J Woodward ◽  
M Lima ◽  
N E Lee
Keyword(s):  
Microcrystalline Cellulose ◽  
Apparent Relationship ◽  
Beta Glucosidase ◽  
Hydrolysis Of

Microcrystalline cellulose (10 mg of Avicel/ml) was hydrolysed to glucose by different concentrations of the purified cellulase components endoglucanase (EG) II and cellobiohydrolases (CBH) I and II, alone and in combination with each other, in the presence of excess beta-glucosidase. At a concentration of 360 micrograms/ml (160 micrograms of EG II/ml, 100 micrograms of CBH I/ml and 100 micrograms of CBH II/ml) the degree of synergism among them was negligible. As the concentration of cellulase decreased, the degree of synergism increased, reaching an optimum at 20 micrograms/ml (5 micrograms of EG II/ml, 10 micrograms of CBH I/ml and 5 micrograms of CBH II/ml). There was no apparent relationship between the ratio of the components and the degree of synergism. The latter is probably due, though it could not be proved, to the level of saturation of the substrate with each component. Inhibition of Avicel hydrolysis was observed when the substrate was incubated with saturating and nonsaturating concentrations of a mixture of EG II and CBH I respectively. A similar result was also observed with a combination of EG I and EG II.

Chemistry of oxylipin pathways in marine diatoms

2007 ◽  
Vol 79 (4) ◽  
pp. 481-490 ◽  
Author(s):  
Angelo Fontana ◽  
Giuliana d'Ippolito ◽  
Adele Cutignano ◽  
Antonio Miralto ◽  
Adrianna Ianora ◽  
...  
Keyword(s):  
Higher Plants ◽  
Larval Growth ◽  
Marine Macroalgae ◽  
High Concentration ◽  
Marine Diatoms ◽  
Fatty Acid Derivatives ◽  
The Family ◽  
Hydrolysis Of ◽  
Catalyzed Oxidation

Oxylipins are important signal transduction molecules widely distributed in animals and plants where they regulate a variety of events associated with physiological and pathological processes. The family embraces several different metabolites that share a common origin from the oxygenase-catalyzed oxidation of polyunsaturated fatty acids. The biological role of these compounds has been especially studied in mammalians and higher plants, although a varied and very high concentration of these products has also been reported from marine macroalgae. This article gives a summary of our results concerning the oxylipin chemistry of marine diatoms, a major class of planktonic microalgae that discourage predation from their natural grazers, zooplanktonic copepods, using chemical warfare. These apparently harmless microscopic cells produce a plethora of oxylipins, including short-chain unsaturated aldehydes, hydroxyl-, keto-, and epoxyhydroxy fatty acid derivatives, that induce reproductive failure in copepods through abortions, congenital malformations, and reduced larval growth. The biochemical process involved in the production of these compounds shows a simple regulation based on decompartmentation and mixing of preexisting enzymes and requires hydrolysis of chloroplast-derived glycolipids to feed the downstream activities of C16 and C20 lipoxygenases.

Theoretical study on the role of cooperative solvent molecules in the neutral hydrolysis of ketene

2010 ◽  
Vol 127 (5-6) ◽  
pp. 493-506 ◽  
Author(s):  
Xiao-Peng Wu ◽  
Xi-Guang Wei ◽  
Xiao-Ming Sun ◽  
Yi Ren ◽  
Ning-Bew Wong ◽  
...  
Keyword(s):  
Theoretical Study ◽  
Solvent Molecules ◽  
Hydrolysis Of

Kinetic Study of Hydrolysis of Benzoates. Part XXV. Ortho Substituent Effect in Alkaline Hydrolysis of Phenyl Esters of Substituted Benzoic Acids in Water

2006 ◽  
Vol 71 (1) ◽  
pp. 107-128 ◽  
Author(s):  
Vilve Nummert ◽  
Mare Piirsalu ◽  
Vahur Mäemets ◽  
Ilmar Koppel
Keyword(s):  
Acid Hydrolysis ◽  
Alkaline Hydrolysis ◽  
Substituent Effect ◽  
Ethyl Esters ◽  
Benzoic Acids ◽  
Neat Water ◽  
Substituted Benzoic Acids ◽  
Hydrolysis Of Esters ◽  
Hydrolysis Of

The second-order rate constants k2 for alkaline hydrolysis of phenyl esters of meta-, para- and ortho-substituted benzoic acids, X-C6H4CO2C6H5 (X = H, 3-Cl, 3-NO2, 3-CH3, 4-NO2, 4-Cl, 4-F, 4-CH3, 4-OCH3, 4-NH2, 2-NO2, 2-CN, 2-F, 2-Cl, 2-Br, 2-I, 2-CH3, 2-OCH3, 2-CF3, 2-NH2), and of substituted phenyl esters of benzoic acid, C6H5CO2C6H4-X (X = 2-I, 2-CF3, 2-C(CH3)3, 4-Cl, 4-CH3, 4-OCH3, 4-NH2), have been measured spectrophotometrically in water at 25 °C. The substituent effect in alkaline hydrolysis of phenyl esters of para-substituted benzoic acids, similar to that for ethyl esters of para-substituted benzoic acids, was found to be precisely described by the Hammett relationship (ρ = 1.7 in water). The log k value for alkaline hydrolysis of phenyl and ethyl esters of meta-, para- and ortho-substituted benzoic acids, X-C6H4CO2R, was nicely correlated with log km,p,ortho = log ko + (ρ)m,pσ + (ρI)orthoσI + (ρ°R)orthoσ°R + δorthoEsB where σ, σI, σ°R are the Hammett polar, Taft inductive and Taft resonance (σ°R = σ° - σI) substituent constants, respectively. EsB is the steric scale for ortho substituents calculated on the basis of the log k values for the acid hydrolysis of ortho- substituted phenyl benzoates in water owing to the ortho substituent in the phenyl of phenyl benzoates. In water, the main factors responsible for changes in the ortho substituent effect in alkaline hydrolysis of phenyl and ethyl esters of ortho-substituted benzoic acids, X-C6H4CO2R, were found to be the inductive and steric factors while the role of the resonance term was negligible ((ρ°R)ortho ca. 0.3). In alkaline hydrolysis of substituted benzoates in neat water, the ortho inductive effect appeared to be 1.5 times and steric influence 2.7 times higher than the corresponding influences from the ortho position in the phenyl of phenyl benzoates. The contributions of the steric effects in alkaline hydrolysis of esters of ortho-substituted benzoic acids was found to be approximately the same as in acid hydrolysis of esters of ortho-substituted benzoic and acid esterification of ortho-substituted benzoic acids.

Sign in / Sign up

Export Citation Format

Share Document