CAS No.18125-46-7,4-Fluoro-D-Phenylalanine Suppliers

Detail of "18125-46-7"

CAS Number:

18125-46-7

Name:

4-Fluoro-D-Phenylalanine

Superlist Name:

4-Fluoro-D-phenylalanine

Molecular Structure:

Formula:

C₉H₁₀FNO₂

Molecular Weight:

183.18

Synonyms:

D-4-Fluorophenylalanine;p-Fluoro-D-phenylalanine;Alanine,3-(p-fluorophenyl)-, D- (8CI);D,L-Fluorophenylalanine;D,L-p-Fluorophenylalanine;DL-p-Fluorophenylalanine;

Density:

1.293g/cm³

Melting Point:

~245ºC

Boiling Point:

313.3ºCat760mmHg

Flash Point:

143.3ºC

Safety:

22-24/25 Details

Reference

L-Phenylalanine ammonia-lyase (maize, potato, and Rhodotorula glutinis): L-Phenylalanine ammonia-lyase (maize, potato, and Rhodotorula glutinis). Explaining the kinetic effects of substrate modification by linear free-energy relations. Hanson, Kenneth R.; Havir, Evelyn A. (Dep. Biochem., Connecticut Agric. Exp. Stn., New Haven, Conn., USA). Arch. Biochem. Biophys., 180(1), 102-13 (English) 1977. CODEN: ABBIA4. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) The action of phenylalanine ammonia-lyase (I) on a series of p-substituted L-phenylalanines was investigated. Multiple linear regression anal. was used to relate the logs of kcat, Km, and kcat/Km to substituent parameters for electron withdrawal, hydrophobic bonding, and size. The inhibitory action of the enantiomeric D-phenylalanines was also investigated. 24250-85-9 and 18125-46-7 which are cas registry numbers are also used here. The results indicate that the rate-limiting step is not subsequent to the release of cinnamate from I. Explanations for the obsd. regression consts. are discussed in terms of the influence of the substituent parameters on the dissocn. const. for the bound substrate, the rate-limiting step, and intermediate steps such as the elimination process. The discussion utilizes a new theoretical treatment of the application of linear free-energy relationships to steady-state enzyme kinetics. In order to interpret structure-activity correlations in terms of rate and equil. consts. for an unbranched catalytic sequence, a restricted model must apply. The reaction must have a single rate-limiting step so that quasi-equil. conditions prevail. In the QE-DS (quasi-equil. dominant-state) model, a single state of the enzyme-substrate complex is assumed to predominate. In the QE-FR (quasi-equil. fixed-ratio) model, changes in the enzyme substituents are assumed not to alter the ratio between the different forms of the enzyme-substrate complex prior to the rate-limiting step. .

Detail of "18125-46-7"

4-Fluoro-D-Phenylalanine

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CAS No.18125-46-7 4-Fluoro-D-Phenylalanine

CAS No.18125-46-7 4-Fluoro-D-phenylalanine

CAS No.18125-46-7 4-Fluoro-D-Phenylalanine

CAS No.18125-46-7 4-Fluoro-D-phenylalanine

CAS No.18125-46-7 4-Fluoro-D-Phenylalanine

CAS No.18125-46-7 4-Fluoro-D-Phenylalanine

CAS No.18125-46-7 4-Fluoro-D-Phenylalanine

CAS No.18125-46-7 4-Fluoro-D-Phenylalanine

CAS No.18125-46-7 4-Fluoro-D-Phenylalanine

CAS No.18125-46-7 4-Fluoro-D-Phenylalanine

CAS No.18125-46-7 4-Fluoro-D-Phenylalanine

CAS No.18125-46-7 4-Fluoro-D-Phenylalanine

CAS No.18125-46-7 4-Fluoro-D-Phenylalanine

Reference