Iron Dienylphosphate Tricarbonyl Complexes as Water-Soluble Enzyme-Triggered CO-Releasing Molecules (ET-CORMs)

2012 ◽  
Vol 31 (16) ◽  
pp. 5800-5809 ◽  
Author(s):  
Steffen Romanski ◽  
Hannelore Rücker ◽  
Eleni Stamellou ◽  
Miguel Guttentag ◽  
Jörg-Martin Neudörfl ◽  
...  
Keyword(s):  
Water Soluble ◽  
Soluble Enzyme

scholarly journals The activity of the intrinsically water-soluble enzyme ADAMTS13 correlates with the membrane state when bound to a phospholipid bilayer

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Andrej Kamenac ◽  
Tobias Obser ◽  
Achim Wixforth ◽  
Matthias F. Schneider ◽  
Christoph Westerhausen
Keyword(s):  
Phase Transition ◽  
Acyl Chain ◽  
Water Soluble ◽  
Main Phase ◽  
Phospholipid Bilayer ◽  
Alternative Theory ◽  
Soluble Enzyme ◽  
Arrhenius Behavior ◽  
Activity Measurements ◽  
Gibb’S Free Energy

AbstractMembrane-associated enzymes have been found to behave differently qualitatively and quantitatively in terms of activity. These findings were highly debated in the 1970s and many general correlations and reaction specific models have been proposed, reviewed, and discarded. However, new biological applications brought up the need for clarification and elucidation. To address literature shortcomings, we chose the intrinsically water-soluble enzyme a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13 (ADAMTS13) and large unilamellar vesicles with a relative broad phase transition. We here present activity measurements of ADAMTS13 in the freely dissolved state and the membrane associated state for phosphocholine lipids with different acyl-chain lengths (13:0, 14:0 and 15:0) and thus main phase transition temperatures. While the freely dissolved enzyme shows a simple Arrhenius behavior, the activity of membrane associated ADAMTS13 in addition shows a peak. This peak temperature correlates with the main phase transition temperature of the used lipids. These findings support an alternative theory of catalysis. This theory predicts a correlation of the membrane associated activity and the heat capacity, as both are susceptibilities of the same surface Gibb’s free energy, since the enzyme is attached to the membrane.

scholarly journals Sulphation as a metabolic pathway for oestradiol in the sea urchin Strongylocentrotus franciscanus

1967 ◽  
Vol 102 (3) ◽  
pp. 898-904 ◽  
Author(s):  
John E. Creange ◽  
Clara M. Szego
Keyword(s):  
Sea Urchin ◽  
Metabolic Pathway ◽  
Enzyme System ◽  
Water Soluble ◽  
Soluble Form ◽  
Soluble Enzyme ◽  
Aerobic Incubation ◽  
Strongylocentrotus Franciscanus ◽  
Rapid Formation

1. Aerobic incubation of [(14)C]oestradiol, in the presence of surviving gut tissue of the sea urchin Strongylocentrotus franciscanus, or a soluble enzyme system prepared therefrom, resulted in rapid formation of a water-soluble metabolite, identified as oestradiol 3-sulphate. 2. No evidence was obtained for the formation of other metabolic derivatives by the urchin-gut enzymes, or for the presence of the sulphating capacity in any other tissues of the organism under the conditions used. 3. The data are consistent with the possibility that oestradiol, previously detected in the gonads, is synthesized therein and excreted in a conjugated, highly water-soluble form via the gut.

scholarly journals BIOSYNTHESIS OF FATTY ACIDS BY CELL-FREE OR WATER-SOLUBLE ENZYME SYSTEMS

1952 ◽  
Vol 199 (1) ◽  
pp. 421-431 ◽  
Author(s):  
Roscoe O. Brady ◽  
Samuel Gurin ◽  
With the technical assistance of Jessie Van Baalen
Keyword(s):  
Fatty Acids ◽  
Water Soluble ◽  
Soluble Enzyme ◽  
Enzyme Systems

scholarly journals Phosphatidylinositol phosphodiesterase in higher plants

1980 ◽  
Vol 192 (1) ◽  
pp. 279-283 ◽  
Author(s):  
R F Irvine ◽  
A J Letcher ◽  
R M C Dawson
Keyword(s):  
Phosphatidic Acid ◽  
Phospholipase C ◽  
Higher Plants ◽  
Water Soluble ◽  
Apium Graveolens ◽  
Soluble Enzyme ◽  
Ph Optimum ◽  
Bivalent Cation ◽  
Detectable Activity ◽  
Ph Range

1. The lower regions of the stem of celery (Apium graveolens L.) contain a soluble enzyme that hydrolyses phosphatidylinositol. 2. The lipoidal product of hydrolysis is diacylglycerol, and the water-soluble products are 1:2-cyclic phosphoinositol and phosphoinositol in the approximate proportions of 60% and 40% respectively: this indicates that a phosphodiesterase (phospholipase C-like) activity is cleaving the phosphatidylinositol. 3. The enzyme requires a bivalent cation, Ca2+ being the most effective activator. 4. The enzyme has a pH optimum, depending on conditions of assay, of pH 5.9-6.6 and in this pH range shows no detectable activity against phosphatidylcholine or phosphatidylethanolamine. 5. The activity is stimulated by phosphatidic acid and slightly inhibited (30% at concentrations equimolar with phosphatidylinositol) by phosphatidylcholine. 6. The phosphodiesterase was also detected (but not quantified) in the tips of the flowers in cauliflowers, in outer leaves of onion and in the elongating stem of daffodils. 7. The enzyme's properties are compared with equivalent mammalian enzymes, and its possible role in the catabolism of phosphatidylinositol in higher plants is discussed.

Molecular Engineering of Microsomal P450 2a-4 to a Stable, Water-Soluble Enzyme

1995 ◽  
Vol 322 (1) ◽  
pp. 265-271 ◽  
Author(s):  
T. Sueyoshi ◽  
L.J. Park ◽  
R. Moore ◽  
R.O. Juvonen ◽  
M. Negishi
Keyword(s):  
Molecular Engineering ◽  
Water Soluble ◽  
Soluble Enzyme

scholarly journals Secretion by overexpression and purification of the water-soluble Streptomyces K15 dd-transpeptidase/penicillin-binding protein

1992 ◽  
Vol 288 (1) ◽  
pp. 87-91 ◽  
Author(s):  
P Palomeque-Messia ◽  
V Quittre ◽  
M Leyh-Bouille ◽  
M Nguyen-Distèche ◽  
C J L Gershater ◽  
...  
Keyword(s):  
Culture Supernatant ◽  
Binding Capacity ◽  
Binding Protein ◽  
Water Soluble ◽  
Appreciable Amount ◽  
Soluble Enzyme ◽  
Penicillin Binding Protein ◽  
Wild Type ◽  
Wild Type Enzyme ◽  
Membrane Bound

Though synthesized with a cleavable signal peptide and devoid of membrane anchors, the 262-amino-acid-residue Streptomyces K15 DD-transpeptidase/penicillin-binding protein is membrane-bound. Overexpression in Streptomyces lividans resulted in the export of an appreciable amount of the synthesized protein (4 mg/litre of culture supernatant). The water-soluble enzyme was purified close to protein homogeneity with a yield of 75%. It requires the presence of 0.5 M-NaCl to remain soluble. It is indistinguishable from the detergent-extract wild-type enzyme with respect to molecular mass, thermostability, transpeptidase activity and penicillin-binding capacity.

Disposable electrochemical capillary-fill device for glucose sensing incorporating a water-soluble enzyme/mediator layer

2001 ◽  
Vol 442 (2) ◽  
pp. 257-265 ◽  
Author(s):  
Chengxiao Zhang ◽  
Tetsuya Haruyama ◽  
Eiry Kobatake ◽  
Masuo Aizawa
Keyword(s):  
Glucose Sensing ◽  
Water Soluble ◽  
Soluble Enzyme
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