64493-16-9

Upstream product

• 67-56-1 methanol 
• 456-88-2 3-fluorophenylalanine 
• 456-42-8 m-fluorobenzyl chloride 
• 75-77-4 chloro-trimethyl-silane 
• 19883-77-3 L-3-fluorophenylalanine 
• 7655-55-2 3-fluoro-DL-phenylalanine ; hydrochloride 

Downstream Products

• 102422-59-3 3-(3-Fluoro-phenyl)-2-isocyanato-propionic acid methyl ester 
• 19883-77-3 L-3-fluorophenylalanine 
• 110117-84-5 (R)-2-amino-3-(3-fluorophenyl)propionic acid 
• 102422-47-9 C₁₁H₁₁FNO₆S^(1-)*K⁽¹⁺⁾ 
• 131235-56-8 3-(3-Fluoro-phenyl)-2-[(imidazole-1-carbonyl)-amino]-propionic acid methyl ester 

Relevant academic research and scientific papers

Enzymatic synthesis of chiral phenylalanine derivatives by a dynamic kinetic resolution of corresponding amide and nitrile substrates with a multi-enzyme system

Mutant α-amino-ε-caprolactam (ACL) racemase (L19V/L78T) from Achromobacter obae with improved substrate specificity toward phenylalaninamide was obtained by directed evolution. The mutant ACL racemase and thermostable mutant D-amino acid amidase (DaaA) from Ochrobactrum anthropi SV3 co-expressed in Escherichia coli (pACLmut/pDBFB40) were utilized for synthesis of (R)-phenylalanine and non-natural (R)-phenylalanine derivatives (4-OH, 4-F, 3-F, and 2-F-Phe) by dynamic kinetic resolution (DKR). Recombinant E. coli with DaaA and mutant ACL racemase genes catalyzed the synthesis of (R)-phenylalanine with 84% yield and 99% ee from (RS)-phenylalaninamide (400 mM) in 22 h. (R)-Tyrosine and 4-fluoro-(R)-phenylalanine were also efficiently synthesized from the corresponding amide compounds. We also co-expresed two genes encoding mutant ACL racemase and L-amino acid amidase from Brevundimonas diminuta in E. coli and performed the efficient production of various (S)-phenylalanine derivatives. Moreover, 2-aminophenylpropionitrile was converted to (R)-phenylalanine by DKR using a combination of the non-stereoselective nitrile hydratase from recombinamt E. coli and mutant ACL racemase and DaaA from E. coli encoding mutant ACL racemase and DaaA genes. Copyright

Electrochemical radiofluorination. 3. Direct labeling of phenylalanine derivatives with [18F]fluoride after anodic oxidation

As an example of applying the electrochemical method in radiofluorination a new procedure was developed for preparing [18F]fluorophenylalanine by direct use of [18F]fluoride. Several protecting groups for amino and carboxylic functio

Resolution of non-protein amino acids via the microbial protease-catalyzed enantioselective hydrolysis of their N-unprotected esters

In the Aspergillus oryzae protease-catalyzed ester hydrolysis, substitution of N-unprotected amino acid esters for the corresponding N-protected amino acid esters resulted in a large enhancement of the hydrolysis rate, while the enantioselectivity was deteriorated strikingly when the substrates employed were the conventional methyl esters. This difficulty was overcome by employing esters bearing a longer alkyl chain such as the isobutyl ester. Utilizing this ester, amino acids carrying an aromatic side chain were resolved with excellent enantioselectivities (E=50 to >200). With amino acids bearing an aliphatic side chain also, good results in terms of the hydrolysis rate and enantioselectivity were obtained by employing such an ester as the isobutyl ester. Moreover, the enantioselectivity proved to be enhanced further by conducting the reaction at low temperature. This procedure was applicable to the case where the enantioselectivity was not high enough even by the use of the isobutyl ester.

Process for the preparation of substituted N-(indole-2-carbonyl)- glycinamides

Processes and intermediates for preparing compounds of Formula (I).

Substituted n-(indole-2-carbonyl)-glycinamides and derivatives as glycogen phosphorylase inhibitors

PCT No. PCT/IB95/00442 Sec. 371 Date Dec. 2, 1997 Sec. 102(e) Date Dec. 2, 1997 PCT Filed Jun. 6, 1995 PCT Pub. No. WO96/39384 PCT Pub. Date Dec. 12, 1996Compounds of Formula (1) wherein R6 is carboxy, (C1-C8)alkoxycarbonyl, benzyloxycarbonyl, C(O)NR8R9 or C(O)R12 as glucogen phosphorylase inhibitors, pharmaceutical compositions containing such inhibitors and the use of such inhibitors to treat diabetes, hyperglycemia, hypercholesterolemia, hypertension, hyperinsulinemia, hyperlipidemia, atherosclerosis and myocardial ischemia in mammals.

Inactivation of Leukocyte Elastase by Aryl Azolides and Sulfonate Salts. Structure-Activity Relationship Studies

The inhibitory activity of a series of aryl azolides and sulfonate salts toward human leukocyte elastase is reported.Several of the compounds were found to be potent inhibitors of the enzyme.Active compounds were obtained only when the specificity group and the reactive moiety were separated by a two-carbon chain.The introduction of hydrophobic groups enhanced the inhibitory activity of these compounds, with the exception of the sulfonate salts.The nature of the leaving group had had a profound effect on inhibitory activity, with compounds 23 and 26 being the most active (kobsd/ = 11722 and 13500 M-1 s-1, respectively).