Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UMLS:C0267964 (
PAA
)
2,561
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The mechanism of the enzyme benzoylformate decarboxylase (BFDC), which carries out a typical thiamin diphosphate (ThDP)-dependent nonoxidative decarboxylation reaction, was studied with the chromophoric alternate substrate (E)-2-oxo-4(pyridin-3-yl)-3-butenoic acid (3-PKB). Addition of 3-PKB resulted in the appearance of two transient intermediates formed consecutively, the first one to be formed a predecarboxylation ThDP-bound intermediate with lambda(max) at 477 nm, and the second one corresponding to the first postdecarboxylation intermediate the enamine with lambda(max) at 437 nm. The time course of formation/depletion of the PKB-ThDP covalent complex and of the enamine showed that decarboxylation was slower than formation of the PKB-ThDP covalent adduct. When the product of decarboxylation 3-(pyridin-3-yl)acrylaldehyde (
PAA
) was added to BFDC, again an absorbance with lambda(max) at 473 nm was formed, corresponding to the tetrahedral adduct of
PAA
with ThDP. Addition of well-formed crystals of BFDC to a solution of
PAA
resulted in a high resolution (1.34 A) structure of the BFDC-bound adduct of ThDP with
PAA
confirming the tetrahedral nature at the C2alpha atom, rather than of the enamine, and supporting the assignment of the lambda(max) at 473 nm to the
PAA
-ThDP adduct. The structure of the
PAA
-ThDP covalent complex is the first example of a product-ThDP adduct on BFDC. Similar studies with 3-PKB indicated that decarboxylation had taken place. Evidence was also obtained for the slow formation of the enamine intermediate when BFDC was incubated with
benzaldehyde
, the product of the decarboxylation reaction thus confirming its presence on the reaction pathway.
...
PMID:Detection and time course of formation of major thiamin diphosphate-bound covalent intermediates derived from a chromophoric substrate analogue on benzoylformate decarboxylase. 1914 Jun 82
We report a solution-phase synthetic route to copper nanoparticles with controllable size and shape. The synthesis of the nanoparticles is achieved by the reduction of copper(II) salt in aqueous solution with hydrazine under air atmosphere in the presence of poly(acrylic acid) (
PAA
) as capping agent. The results suggest that the pH plays a key role for the formation of pure copper nanoparticles, whereas the concentration of
PAA
is important for controlling the size and geometric shape of the nanoparticles. The average size of the copper nanoparticles can be varied from 30 to 80 nm, depending on the concentration of
PAA
. With a moderate amount of
PAA
, faceted crystalline copper nanoparticles are obtained. The as-synthesized copper nanoparticles appear red in color and are stable for weeks, as confirmed by UV/Vis and X-ray photoemission (XPS) spectroscopy. The faceted crystalline copper nanoparticles serve as an effective catalyst for N-arylation of heterocycles, such as the C--N coupling reaction between p-nitrobenzyl chloride and morpholine producing 4-(4-nitrophenyl)morpholine in an excellent yield under mild reaction conditions. Furthermore, the nanoparticles are proven to be versatile as they also effectively catalyze the three-component, one-pot Mannich reaction between p-substituted
benzaldehyde
, aniline, and acetophenone affording a 100% conversion of the limiting reactant (aniline).
...
PMID:Controlled synthesis of water-dispersible faceted crystalline copper nanoparticles and their catalytic properties. 2064 84