scholarly journals A highly effective and stable CuZn0.3MgxAlOycatalyst for the manufacture of chirall-phenylalaninol: the role of Mg and its hydrotalcite-like precursor

2016 ◽  
Vol 6 (10) ◽  
pp. 3457-3467 ◽  
Author(s):  
Zhangping Shi ◽  
Shuangshuang Zhang ◽  
Xiuzhen Xiao ◽  
Dongsen Mao ◽  
Guanzhong Lu
Keyword(s):  
Methyl Ester ◽  
Catalytic Hydrogenation ◽  
Highly Effective ◽  
Phenylalanine Methyl Ester

A highly effective and stable CuZn0.3Mg0.1AlOycatalyst derived from a Cu-rich hydrotalcite-like precursor was prepared for the catalytic hydrogenation ofl-phenylalanine methyl ester tol-phenylalaninol with ~100% ee selectivity.

Effects of the preparation method on the performance of the Cu/ZnO/Al2O3 catalyst for the manufacture of l-phenylalaninol with high ee selectivity from l-phenylalanine methyl ester

2014 ◽  
Vol 4 (4) ◽  
pp. 1132-1143 ◽  
Author(s):  
Zhangping Shi ◽  
Xiuzhen Xiao ◽  
Dongsen Mao ◽  
Guanzhong Lu
Keyword(s):  
Methyl Ester ◽  
Catalytic Hydrogenation ◽  
Preparation Method ◽  
Phenylalanine Methyl Ester ◽  
Al2o3 Catalyst

Efficient catalytic hydrogenation of l-phenylalanine methyl ester to l-phenylalaninol over the Cu/ZnO/Al2O3 catalyst with ~100% ee selectivity.

scholarly journals 4-fluorobenzylamine and phenylalanine methyl ester conjugates OF 2-nitroimidazole: Evaluation as hypoxic cell radiosensitizers

1992 ◽  
Vol 22 (3) ◽  
pp. 593-596 ◽  
Author(s):  
Pradeep K. Arg ◽  
Sudha Garg ◽  
William G. Degraff ◽  
Michael R. Zalutsky ◽  
James B. Mitchell
Keyword(s):  
Methyl Ester ◽  
Hypoxic Cell ◽  
Phenylalanine Methyl Ester

Significance of C-terminal cysteine modifications to the biological activity of the Saccharomyces cerevisiae a-factor mating pheromone

1991 ◽  
Vol 11 (7) ◽  
pp. 3603-3612
Author(s):  
S Marcus ◽  
G A Caldwell ◽  
D Miller ◽  
C B Xue ◽  
F Naider ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Biological Activity ◽  
Methyl Ester ◽  
Total Synthesis ◽  
Biologically Active ◽  
Structural Genes ◽  
Wild Type ◽  
Mating Pheromone ◽  
Carboxy Terminal

We have undertaken total synthesis of the Saccharomyces cerevisiae a-factor (NH2-YIIKGVFWDPAC[S-farnesyl]-COOCH3) and several Cys-12 analogs to determine the significance of S-farnesylation and carboxy-terminal methyl esterification to the biological activity of this lipopeptide mating pheromone. Replacement of either the farnesyl group or the carboxy-terminal methyl ester by a hydrogen atom resulted in marked reduction but not total loss of bioactivity as measured by a variety of assays. Moreover, both the farnesyl and methyl ester groups could be replaced by other substituents to produce biologically active analogs. The bioactivity of a-factor decreased as the number of prenyl units on the cysteine sulfur decreased from three to one, and an a-factor analog having the S-farnesyl group replaced by an S-hexadecanyl group was more active than an S-methyl a-factor analog. Thus, with two types of modifications, a-factor activity increased as the S-alkyl group became bulkier and more hydrophobic. MATa cells having deletions of the a-factor structural genes (mfal1 mfa2 mutants) were capable of mating with either sst2 or wild-type MAT alpha cells in the presence of exogenous a-factor, indicating that it is not absolutely essential for MATa cells to actively produce a-factor in order to mate. Various a-factor analogs were found to partially restore mating to these strains as well, and their relative activities in the mating restoration assay were similar to their activities in the other assays used in this study. Mating was not restored by addition of exogenous a-factor to a cross of a wild-type MAT alpha strain and a MATaste6 mutant, indicating a role of the STE6 gene product in mating in addition to its secretion of a-factor.

scholarly journals Significance of C-terminal cysteine modifications to the biological activity of the Saccharomyces cerevisiae a-factor mating pheromone.

1991 ◽  
Vol 11 (7) ◽  
pp. 3603-3612 ◽  
Author(s):  
S Marcus ◽  
G A Caldwell ◽  
D Miller ◽  
C B Xue ◽  
F Naider ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Biological Activity ◽  
Methyl Ester ◽  
Total Synthesis ◽  
Biologically Active ◽  
Structural Genes ◽  
Wild Type ◽  
Mating Pheromone ◽  
Carboxy Terminal

We have undertaken total synthesis of the Saccharomyces cerevisiae a-factor (NH2-YIIKGVFWDPAC[S-farnesyl]-COOCH3) and several Cys-12 analogs to determine the significance of S-farnesylation and carboxy-terminal methyl esterification to the biological activity of this lipopeptide mating pheromone. Replacement of either the farnesyl group or the carboxy-terminal methyl ester by a hydrogen atom resulted in marked reduction but not total loss of bioactivity as measured by a variety of assays. Moreover, both the farnesyl and methyl ester groups could be replaced by other substituents to produce biologically active analogs. The bioactivity of a-factor decreased as the number of prenyl units on the cysteine sulfur decreased from three to one, and an a-factor analog having the S-farnesyl group replaced by an S-hexadecanyl group was more active than an S-methyl a-factor analog. Thus, with two types of modifications, a-factor activity increased as the S-alkyl group became bulkier and more hydrophobic. MATa cells having deletions of the a-factor structural genes (mfal1 mfa2 mutants) were capable of mating with either sst2 or wild-type MAT alpha cells in the presence of exogenous a-factor, indicating that it is not absolutely essential for MATa cells to actively produce a-factor in order to mate. Various a-factor analogs were found to partially restore mating to these strains as well, and their relative activities in the mating restoration assay were similar to their activities in the other assays used in this study. Mating was not restored by addition of exogenous a-factor to a cross of a wild-type MAT alpha strain and a MATaste6 mutant, indicating a role of the STE6 gene product in mating in addition to its secretion of a-factor.

Role of NO in goat basal cerebral circulation and after vasodilatation to hypercapnia or brief ischemias

1993 ◽  
Vol 265 (6) ◽  
pp. R1410-R1415 ◽  
Author(s):  
G. Dieguez ◽  
J. L. Garcia ◽  
N. Fernandez ◽  
A. L. Garcia-Villalon ◽  
L. Monge ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Heart Rate ◽  
Methyl Ester ◽  
Cerebral Circulation ◽  
Systemic Arterial Pressure ◽  
Nitric Oxide Production ◽  
Hemodynamic Effects ◽  
Arterial Pco2 ◽  
Different Levels

The role of nitric oxide (NO) in the cerebral circulation under basal conditions and after vasodilatation to hypercapnia or reactive hyperemias was studied in 17 anesthetized goats. The intravenous administration of NG-nitro-L-arginine methyl ester (L-NAME, 3-4 or 8-10 mg/kg), an inhibitor of nitric oxide production, reduced middle cerebral artery (MCA) flow (electromagnetically measured) by 19 and 30% and increased systemic arterial pressure by 21 and 26%, respectively, whereas heart rate did not significantly change; MCA resistance increased by 48 and 86%, respectively. These hemodynamic effects were reversed by L-arginine (200-300 mg/kg iv; 5 goats). Different levels of hypercapnia (PCO2 of 30-35, 40-45, and 55-65 mmHg) (12 goats) produced arterial PCO2-dependent increases in MCA flow that were similar under control and L-NAME treatment. Graded cerebral hyperemia occurred after 5, 10, and 20 s of MCA occlusion in 5 goats, but its magnitude was decreased during L-NAME treatment. It suggests that, in the cerebral circulation, nitric oxide 1) produces a basal vasodilator tone and 2) is probably not involved in the vasodilatation to hypercapnia but may mediate hyperemic responses after short brain ischemias.

Synthesis of aspartame via asymmetric hydrogenation of N-protected (Z)-N-.alpha.-L-aspartyl-.DELTA.-phenylalanine methyl ester

1986 ◽  
Vol 51 (7) ◽  
pp. 1126-1128 ◽  
Author(s):  
Claudio Fuganti ◽  
Piero Grasselli ◽  
Luciana Malpezzi ◽  
Paolo Casati
Keyword(s):  
Methyl Ester ◽  
Asymmetric Hydrogenation ◽  
Phenylalanine Methyl Ester
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