Optical properties of dimedonyl derivative of aromatic amines and amino acids

Tetrahedron ◽  
1972 ◽  
Vol 28 (11) ◽  
pp. 2991-2997 ◽  
Author(s):  
V. Tortorella ◽  
G. Bettoni ◽  
B. Halpern ◽  
P. Crabbe'
1982 ◽  
Vol 60 (9) ◽  
pp. 861-866
Author(s):  
Chiu-Yin Kwan ◽  
Robert C. Davis

The kinetic and optical properties of Co(II)-substituted pyruvate kinase in the presence of D-phenylalanine (D-Phe) were investigated. The results are discussed in comparison with the effects of its optical isomer L-phenylalanine (L-Phe) on the same enzyme. The catalytic effect of D-Phe on rabbit muscle pyruvate kinase depended upon the nature of the activating divalent metal ion used. It has stimulatory effect on Mg(II)-activated enzyme, but inhibitory effect on Co(II)-activated enzyme. Unlike the inhibitory effect of L-Phe, the inhibition of Co(II)–enzyme by D-Phe was not sensitive to the changes of pH and temperature, could not be reversed by L-alanine (L-Ala), displayed hyperbolic kinetics, and was noncompetitive with respect to phosphoenolpyruvate saturation. D-Phe induced substantial visible circular dichroism (CD) spectral changes of Co(II)–enzyme similar to those induced by L-Phe. Although ultraviolet CD spectrum was not affected, D-Phe induced an ultraviolet difference absorption spectral change very similar to, but much smaller than, that induced by L-Phe. Our results support that D-Phe and other amino acids interact with the enzyme at two different sites: a common site, causing similar conformational changes which bear little direct kinetic relevance, and a kinetically relevant site, which is sterically dependent upon the side chain of the amino acids.


2017 ◽  
Vol 17 (1) ◽  
pp. 127-137
Author(s):  
Emildo Marcano ◽  
José Gregorio Cisneros ◽  
Johana Alayón ◽  
Juan Murgich

2000 ◽  
Vol 352 (2) ◽  
pp. 533-538 ◽  
Author(s):  
Mariarita BERTOLDI ◽  
Carla BORRI VOLTATTORNI

Analysis of the reaction of dopa decarboxylase (DDC) with L-dopa reveals that loss of decarboxylase activity with time is observed at enzyme concentrations approximately equal to the binding constant, Kd, of the enzyme for pyridoxal 5ƀ-phosphate (PLP). Instead, at enzyme concentrations higher than Kd the course of product formation proceeds linearly until complete consumption of the substrate. Evidence is provided that under both experimental conditions no pyridoxamine 5ƀ-phosphate (PMP) is formed during the reaction and that dissociation of coenzyme occurs at low enzyme concentration, leading to the formation of a PLP-L-dopa Pictet–Spengler cyclic adduct. Taken together, these results indicate that decarboxylation-dependent transamination does not accompany the decarboxylation of L-dopa proposed previously [O'Leary and Baughn (1977) J. Biol. Chem. 252, 7168–7173]. Nevertheless, when the reaction of DDC with L-dopa is studied under anaerobic conditions at an enzyme concentration higher than Kd, we observe that (1) the enzyme is gradually inactivated and inactivation is associated with PMP formation and (2) the initial velocity of decarboxylation is approximately half of that in the presence of O2. Similar behaviour is observed by comparing the reaction with L-5-hydroxytryptophan occurring in aerobiosis or in anaerobiosis. Therefore the reaction of DDC with L-aromatic amino acids seems to be under O2 control. In contrast, the reactivity of the enzyme with D-aromatic amino acids does not change in the presence or absence of O2. These and other results, together with previous results on the effect exerted by O2 on reaction specificity of DDC towards aromatic amines [Bertoldi, Frigeri, Paci and Borri Voltattorni (1999) J. Biol. Chem. 274, 5514–5521], suggest a productive effect of O2 on an intermediate complex of the reaction of the enzyme with L-aromatic amino acids or aromatic amines.


Author(s):  
S Yoshida ◽  
K Kobayashi

AbstractThe aim of the present study was to gain further understanding of the precursors in tobacco of four polycyclic aromatic amines (PAAs) - 1- and 2-aminonaphthalene, 3- and 4-aminobiphenyl. We carried out non-isothermal pyrolysis of the residues, which were obtained after extraction of tobacco cut filler with methylene chloride followed by extraction with water, under three different pyrolysis conditions (target temperature 800 °C / 800 °C / 400 °C and O2 concentration in carrier gas 0% / 20% / 3%, resp.). The yields of the four PAAs obtained by the pyrolysis of each sample were evaluated. Several nitrogenous components in the sample were also analyzed. The results under all these pyrolysis conditions showed that 1) the methylene chloride-soluble fraction, in which 50-60% of nicotine was extracted, did NOT contribute significantly contribution to the yields of the four PAAs; 2) the watersoluble fraction, in which most of the nitrogenous inorganic ions and amino acids were extracted, contributed at an average of about 30% to total PAA yield; and 3) the insoluble residue, in which only protein was detected during the investigation of the nitrogenous components in the present study, showed the highest contribution, 50-60% of the four PAAs formed. Consequently, it is concluded that protein-like components in tobacco contribute highly to the formation of the four PAAs by tobacco pyrolysis.


Nanomaterials ◽  
2021 ◽  
Vol 11 (10) ◽  
pp. 2607
Author(s):  
Chunyu Ji ◽  
Yiqun Zhou ◽  
Wenquan Shi ◽  
Jiajia Wu ◽  
Qiurui Han ◽  
...  

In this article, we have designed both colorimetric (including solution and test paper type) and spectral sensors (including UV-vis and PL type) for the quick and sensitive detection of general nitrogen-containing organic bases (NCOBs); the limit of detection could reach as low as 0.50 nM. NCOBs included 11 examples, covering aliphatic and aromatic amines, five- and six-membered heterocyclics, fused-ring heterocyclics, amino acids, and antibiotics. Furthermore, the assays demonstrated high reliability in sensing NCOBs and excellent ability to distinguish NCOBs from oxygen and sulfur containing organics. The assays developed could find important applications for the detection of NCOBs in the fields of biomedicine, chemistry, and agriculture.


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