scholarly journals Drosophila melanogaster alcohol dehydrogenase: product-inhibition studies

1994 ◽  
Vol 301 (3) ◽  
pp. 901-909 ◽  
Author(s):  
J O Winberg ◽  
J S McKinley-McKee
Keyword(s):  
Acetic Acid ◽  
Drosophila Melanogaster ◽  
Alcohol Dehydrogenase ◽  
Ternary Complex ◽  
Product Inhibition ◽  
Ternary Complexes ◽  
Binary Complexes ◽  
Inhibition Studies ◽  
Inhibition Pattern ◽  
Drosophila Adh

The Drosophila melanogaster alleloenzymes AdhS and AdhF have been studied with respect to product inhibition by using the two substrate couples propan-2-ol/acetone and ethanol/acetaldehyde together with the coenzyme couple NAD+/NADH. With both substrate couples the reaction was consistent with an ordered Bi Bi mechanism. The substrates added to the enzyme in a compulsory order, with coenzyme as the leading substrate, to give two interconverting ternary complexes. The second ternary complex broke down with release of products in an obligatory order, with the aldehyde/ketone leaving first. Both the acetaldehyde and acetone products formed binary complexes with the enzyme that affected NAD+ binding. However, only an enzyme-acetone complex seemed to affect NADH binding and hence the reverse reaction. The inhibitory pattern with acetaldehyde as product was also affected by the formation of a ternary enzyme-NAD(+)-acetaldehyde complex, which broke down to acetic acid and NADH. The product-inhibition pattern shown in the present work is different from that published for Drosophila Adh previously and this discrepancy can not be explained by the use of different variants of Drosophila Adh.

Equilibrium Studies of Binary and Ternary Complexes of Palladium(II) Involving Amino Acids

1993 ◽  
Vol 58 (5) ◽  
pp. 1103-1108 ◽  
Author(s):  
Mohamed M. Shoukry ◽  
Eman M. Shoukry
Keyword(s):  
Amino Acids ◽  
Relative Stability ◽  
Ternary Complex ◽  
Formation Constants ◽  
Ternary Complexes ◽  
Conductivity Measurements ◽  
Equilibrium Studies ◽  
Binary And Ternary Complexes ◽  
Binary Complexes

The formation constants of the binary and ternary complexes of palladium(II) with diethylenetriamine and amino acids as ligands have been determined potentiometrically at 25 °C in 0.1 M NaNO3 solution. The relative stability of each ternary complex was compared with that of the corresponding binary complexes in terms of ∆logK values. The mode of chelation was ascertained by conductivity measurements.

scholarly journals Purification and kinetic properties of ox brain histamine N-methyltransferase

1986 ◽  
Vol 233 (3) ◽  
pp. 669-676 ◽  
Author(s):  
W L Gitomer ◽  
K F Tipton
Keyword(s):  
Acetic Acid ◽  
Steady State ◽  
Mouse Brain ◽  
Initial Rate ◽  
Substrate Inhibition ◽  
Gel Filtration ◽  
Product Inhibition ◽  
Kinetic Properties ◽  
Brain Histamine ◽  
Inhibition Studies

Histamine N-methyltransferase (EC 2.1.1.8) was purified 1100-fold from ox brain. The native enzyme has an Mr of 34800 +/- 2400 as measured by gel filtration on Sephadex G-100. The enzyme is highly specific for histamine. It does not methylate noradrenaline, adrenaline, DL-3,4-dihydroxymandelic acid, 3,4-dihydroxyphenylacetic acid, 3-hydroxytyramine or imidazole-4-acetic acid. Unlike the enzyme from rat and mouse brain, ox brain histamine N-methyltransferase did not exhibit substrate inhibition by histamine. Initial rate and product inhibition studies were consistent with an ordered steady-state mechanism with S-adenosylmethionine being the first substrate to bind to the enzyme and N-methylhistamine being the first product to dissociate.

scholarly journals Kinetic mechanism of pulmonary carbonyl reductase

1988 ◽  
Vol 252 (1) ◽  
pp. 17-22 ◽  
Author(s):  
K Matsuura ◽  
T Nakayama ◽  
M Nakagawa ◽  
A Hara ◽  
H Sawada
Keyword(s):  
Kinetic Mechanism ◽  
Product Inhibition ◽  
Carbonyl Reductase ◽  
Ternary Complexes ◽  
Enzyme Mechanism ◽  
The Other ◽  
Binding Studies ◽  
Forward Reaction ◽  
Cibacron Blue ◽  
Inhibition Studies

The kinetic mechanism of guinea-pig lung carbonyl reductase was studied at pH 7 in the forward reaction with five carbonyl substrates and NAD(P)H and in the reverse reaction with propan-2-ol and NAD(P)+. In each case the enzyme mechanism was sequential, and product-inhibition studies were consistent with a di-iso ordered bi bi mechanism, in which NAD(P)H binds to the enzyme first and NAD(P)+ leaves last and the binding of cofactor induces isomerization. The kinetic and binding studies of the cofactors and several inhibitors such as pyrazole, benzoic acid, Cibacron Blue and benzamide indicate that the cofactor and Cibacron Blue bind to the free enzyme whereas the other inhibitors bind to the binary and/or ternary complexes.

scholarly journals Stability Constants of Mixed Ligand Complexes of Nickel(II) with Adenine and Some Amino Acids

2015 ◽  
Vol 2015 ◽  
pp. 1-9 ◽  
Author(s):  
Naciye Türkel
Keyword(s):  
Aqueous Solution ◽  
Amino Acids ◽  
Ternary Complex ◽  
Coordination Complexes ◽  
Ternary Complexes ◽  
Mixed Ligand ◽  
Relative Stabilities ◽  
Binary And Ternary Complexes ◽  
Binary Complexes ◽  
Essential Trace Elements

Nickel is one of the essential trace elements found in biological systems. It is mostly found in nickel-based enzymes as an essential cofactor. It forms coordination complexes with amino acids within enzymes. Nickel is also present in nucleic acids, though its function in DNA or RNA is still not clearly understood. In this study, complex formation tendencies of Ni(II) with adenine and certain L-amino acids such as aspartic acid, glutamic acid, asparagine, leucine, phenylalanine, and tryptophan were investigated in an aqueous medium. Potentiometric equilibrium measurements showed that both binary and ternary complexes of Ni(II) form with adenine and the above-mentioned L-amino acids. Ternary complexes of Ni(II)-adenine-L-amino acids are formed by stepwise mechanisms. Relative stabilities of the ternary complexes are compared with those of the corresponding binary complexes in terms ofΔlog10⁡K,log10⁡X, and % RS values. It was shown that the most stable ternary complex is Ni(II):Ade:L-Asn while the weakest one is Ni(II):Ade:L-Phe in aqueous solution used in this research. In addition, results of this research clearly show that various binary and ternary type Ni(II) complexes are formed in different concentrations as a function of pH in aqueous solution.

scholarly journals Binding characteristics of pro-insulin-like growth factor-II from cancer patients: binary and ternary complex formation with IGF binding proteins-1 to -6

2000 ◽  
Vol 165 (2) ◽  
pp. 253-260 ◽  
Author(s):  
JJ Bond ◽  
S Meka ◽  
RC Baxter
Keyword(s):  
Complex Formation ◽  
Ternary Complex ◽  
Binding Proteins ◽  
Ternary Complexes ◽  
Binary Complex ◽  
Igf Binding Proteins ◽  
Ternary Complex Formation ◽  
Binary Complexes ◽  
Igf Binding ◽  
Igfbp 3

Many tumours secrete IGF-II in incompletely processed precursor forms. The ability of these pro-IGF-II forms to complex with the six IGF binding proteins (IGFBPs) is poorly understood. In this study, pro-IGF-II has been extracted from the serum and tumour tissue of two patients with non-islet cell tumour hypoglycaemia. These samples were used to study binary complex formation with IGFBPs-1 to -6 using competitive IGF-II binding assays and ternary complex formation with IGFBP-3 and IGFBP-5. In each case, IGFBPs-1 to -6 showed little difference in their ability to form binary complexes with recombinant IGF-II or tumour-derived pro-IGF-II forms, when the preparations were standardised according to IGF-II immunoreactivity. As previously described, ternary complex formation by acid-labile subunit (ALS) with IGFBP-3 and pro-IGF-II was greatly decreased compared with complex formation with mature IGF-II. In contrast, ALS bound similarly to IGFBP-5 in the presence of pro-IGF-II and mature IGF-II. These studies suggest that pro-IGF-II preferentially forms binary complexes with IGFBPs, and ternary complexes with IGFBP-5, rather than ternary complexes with IGFBP-3 as seen predominantly in normal serum. This may increase the tissue availability of serum pro-IGF-II, allowing its insulin-like potential to be realised.

scholarly journals A study of the kinetics and mechanism of yeast alcohol dehydrogenase with a variety of substrates

1973 ◽  
Vol 131 (2) ◽  
pp. 261-270 ◽  
Author(s):  
F. M. Dickinson ◽  
G. P. Monger
Keyword(s):  
Alcohol Dehydrogenase ◽  
Ethanol Oxidation ◽  
Ternary Complexes ◽  
Kinetics Of Oxidation ◽  
Yeast Alcohol Dehydrogenase ◽  
Rate Limiting Step ◽  
Limiting Step ◽  
Binary Complexes ◽  
Rate Limiting ◽  
Kinetics Of

1. The kinetics of oxidation of ethanol, propan-1-ol, butan-1-ol and propan-2-ol by NAD+ and of reduction of acetaldehyde and butyraldehyde by NADH catalysed by yeast alcohol dehydrogenase were studied. 2. Results for the aldehyde–NADH reactions are consistent with a compulsory-order mechanism with the rate-limiting step being the dissociation of the product enzyme–NAD+ complex. In contrast the results for the alcohol–NAD+ reactions indicate that some dissociation of coenzyme from the active enzyme–NAD+–alcohol ternary complexes must occur and that the mechanism is not strictly compulsory-order. The rate-limiting step in ethanol oxidation is the dissociation of the product enzyme–NADH complex but with the other alcohols it is probably the catalytic interconversion of ternary complexes. 3. The rate constants describing the combination of NAD+ and NADH with the enzyme and the dissociations of these coenzymes from binary complexes with the enzyme were measured.

scholarly journals The mechanism of the reaction between glutathione and 1-menaphthyl sulphate catalysed by a glutathione S-transferase from rat liver

1973 ◽  
Vol 135 (4) ◽  
pp. 797-804 ◽  
Author(s):  
Brian Gillham
Keyword(s):  
Rat Liver ◽  
Gel Filtration ◽  
Product Inhibition ◽  
Glutathione S Transferase ◽  
Michaelis Constant ◽  
Dead End ◽  
Michaelis Constants ◽  
Inhibition Studies ◽  
Inhibition Pattern ◽  
Mechanism Of The Reaction

1. The glutathione S-transferase that catalyses the reaction of 1-menaphthyl (naphth-1-ylmethyl) sulphate with GSH was purified 76-fold from rat liver. 2. The properties of the purified enzyme were studied by gel filtration and isoelectric focusing. 3. The initial-velocity pattern in the absence of products and the product-inhibition pattern have been determined. These are consistent with an Ordered Bi Bi mechanism in which the GSH adds to the enzyme before 1-menaphthyl sulphate and the products are released in the order SO42−followed by S-(1-menaphthyl)glutathione. 4. Dead-end-inhibition studies with p-aminobenzoic acid, which has been shown to be competitive with GSH and non-competitive with 1-menaphthyl sulphate, support the suggestion that an Ordered Bi Bi mechanism is operative. 5. Values were determined for some of the dissociation and Michaelis constants for the reaction of the substrates and products with the enzyme. 6. It appears that S-(1-menaphthyl)glutathione activates the enzyme when the concentration of GSH is saturating and that of 1-menaphthyl sulphate is low (of the order of its Michaelis constant).

scholarly journals Thermodynamics of binary and ternary complexes of 3-amino-1, 2, 4-triazole and aminoacids with Ni(II) and Co(II) metal ions

2005 ◽  
Vol 70 (8-9) ◽  
pp. 1057-1066 ◽  
Author(s):  
Ayse Erçag ◽  
Tuba Sismanoglu ◽  
Suheyla Pura
Keyword(s):  
Ionic Strength ◽  
Aqueous Solutions ◽  
Glutamic Acid ◽  
Driving Force ◽  
Ternary Complex ◽  
Ternary Complexes ◽  
Binary And Ternary Complexes ◽  
Enthalpy Changes ◽  
Binary Complexes ◽  
The Stability

The stability constants of the 1:1 binary complexes of Ni(II) and Co(II) with 3-amino-1,2,4-triazole (AT), leucine (Leu) and glutamic acid (Glu), and the 1:1:1 ternary complex of them and the protonation constants of the ligands were determined potentiometrically at a constant ionic strength of I = 0.10 mol L-1 (NaClO4) in aqueous solutions at 15.0 and 25.0 ?C. The thermodynamic parameters ?Gf0, ?Hf0 and ?Sf0 are reported for the formation reactions of the complexes. The enthalpy changes of all the complexations were found to be negative but the entropy changes positive. While the driving force for the formation of the Ni(II), Co(II) ? AT complexes is the enthalpy decrease, the driving force for the ternary complexes of AT is the entropy increase.

scholarly journals Complex Equilibria and Distribution of Metal (II) Ions with Biologically Active Chelating Agents in Aqueous and Aqueous-organic Media

2021 ◽  
pp. 25-38
Author(s):  
K. T. Ishola ◽  
O. T. Olanipekun ◽  
O. T. Bolarinwa ◽  
R. D. Oladeji ◽  
A. Abubakar
Keyword(s):  
Metal Ions ◽  
Species Distribution ◽  
Ternary Complex ◽  
Aqueous System ◽  
Ternary Complexes ◽  
Teller Distortion ◽  
Complex Equilibria ◽  
Binary Complexes ◽  
The Stability ◽  
Ph Range

An understanding of the principles of complex equilibria and species distribution in different solutions is important in expounding and correlating the interaction of different ligands with different metal ions in complex formation. Therefore, acid-base equilibria involved in the formation of binary and ternary complexes of Co (II), Cu (II) and Pb (II) with methionine (Met) and uracil (Urc) have been determined by potentiometric titration technique. The stability constants of the complexes were evaluated at 35 ± 0.1°C and 0.02 M ionic strength (kept constant with NaNO3) in aqueous and organic-aqueous media. The species distribution in solutions as a function of pH was determined using the Hyss program. The stability of the ternary complexes relative to the corresponding binary complexes of the secondary ligand is measured in terms ΔlogK and % RS values. The ternary complexes are observed to be more stable than binary complexes in the media except for [CuMetUrc] ternary complex in organic-aqueous medium where the ternary complex is less stable than the binary complex of the uracil. The overall stability of the ternary complexes was higher in organic-aqueous system than aqueous system. The stability of the complexes was found to be correlated with the covalent index of the metal ions and Jahn Teller distortion. pH-studies of these systems revealed an increase in the concentrations of the ternary complexes with increase in pH. The formation of binary complexes was shown to be favoured in physiological pH range (3-7) while that of the ternary complexes is observed to be favoured in the pH range 5-10.

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