64493-16-9

Basic information

• Product Name: 3-fluoro-DL-phenylalanine methyl ester hydrochloride
• Synonyms: 3-fluoro-DL-phenylalanine methyl ester hydrochloride
• CAS NO: 64493-16-9
• Molecular Weight: 233.67
• Mol File: 64493-16-9.mol
• Article Data: 6

Chemical Properties

• CAS DataBase Reference: 3-fluoro-DL-phenylalanine methyl ester hydrochloride(CAS DataBase Reference)
• NIST Chemistry Reference: 3-fluoro-DL-phenylalanine methyl ester hydrochloride(64493-16-9)
• EPA Substance Registry System: 3-fluoro-DL-phenylalanine methyl ester hydrochloride(64493-16-9)

Safety Data

• Hazardous Substances Data: 64493-16-9(Hazardous Substances Data)

Upstream product

• 75-77-4 chloro-trimethyl-silane 
• 19883-77-3 L-3-fluorophenylalanine 
• 456-42-8 m-fluorobenzyl chloride 
• 67-56-1 methanol 
• 456-88-2 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 
• 131235-56-8 3-(3-Fluoro-phenyl)-2-[(imidazole-1-carbonyl)-amino]-propionic acid methyl ester 
• 102422-47-9 C₁₁H₁₁FNO₆S^(1-)*K⁽¹⁺⁾ 

Relevant articles and documents

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

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.

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.