485-13-2 Usage
Description
Fluoroacetyl-coenzyme A, also known as fluoroacetyl-CoA, is a compound formed by the formal condensation of the thiol group of coenzyme A (Co-A) with the carboxylic acid group of fluoroacetic acid. It plays a significant role in various biological processes and has potential applications in different industries.
Uses
Used in Pharmaceutical Industry:
Fluoroacetyl-coenzyme A is used as an intermediate in the synthesis of certain pharmaceutical compounds for [application reason]. Its unique structure allows it to be a key component in the development of drugs targeting specific metabolic pathways.
Used in Biochemical Research:
In the field of biochemical research, fluoroacetyl-coenzyme A is used as a research tool for [application reason]. It helps scientists understand the mechanisms of various metabolic processes and the role of acyl-CoA compounds in cellular functions.
Used in Chemical Synthesis:
Fluoroacetyl-coenzyme A is used as a building block in the chemical synthesis of various organic compounds for [application reason]. Its unique properties make it a valuable starting material for the development of new molecules with potential applications in various industries.
Used in Environmental Applications:
In environmental applications, fluoroacetyl-coenzyme A is used as a component in bioremediation processes for [application reason]. Its ability to interact with specific enzymes and metabolic pathways can help in the degradation of pollutants and the cleanup of contaminated sites.
Used in Agricultural Industry:
Fluoroacetyl-coenzyme A is used as a component in the development of new agrochemicals for [application reason]. Its potential to target specific metabolic pathways in pests and pathogens can lead to the creation of more effective and environmentally friendly pest control solutions.
Check Digit Verification of cas no
The CAS Registry Mumber 485-13-2 includes 6 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 3 digits, 4,8 and 5 respectively; the second part has 2 digits, 1 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 485-13:
(5*4)+(4*8)+(3*5)+(2*1)+(1*3)=72
72 % 10 = 2
So 485-13-2 is a valid CAS Registry Number.
485-13-2Relevant articles and documents
Structural and biochemical studies of a fluoroacetyl-CoA-specific thioesterase reveal a molecular basis for fluorine selectivity
Weeks, Amy M.,Coyle, Scott M.,Jinek, Martin,Doudna, Jennifer A.,Chang, Michelle C. Y.
, p. 9269 - 9279 (2010)
We have initiated a broad-based program aimed at understanding the molecular basis of fluorine specificity in enzymatic systems, and in this context, we report crystallographic and biochemical studies on a fluoroacetyl-coenzyme A (CoA) specific thioesterase (FlK) from Streptomyces cattleya. Our data establish that FlK is competent to protect its host from fluoroacetate toxicity in vivo and demonstrate a 106-fold discrimination between fluoroacetyl-CoA (kcat/KM = 5 × 107 M-1 s-1) and acetyl-CoA (k cat/KM = 30 M-1 s-1) based on a single fluorine substitution that originates from differences in both substrate reactivity and binding. We show that Thr 42, Glu 50, and His 76 are key catalytic residues and identify several factors that influence substrate selectivity. We propose that FlK minimizes interaction with the thioester carbonyl, leading to selection against acetyl-CoA binding that can be recovered in part by new C=O interactions in the T42S and T42C mutants. We hypothesize that the loss of these interactions is compensated by the entropic driving force for fluorinated substrate binding in a hydrophobic binding pocket created by a lid structure, containing Val 23, Leu 26, Phe 33, and Phe 36, that is not found in other structurally characterized members of this superfamily. We further suggest that water plays a critical role in fluorine specificity based on biochemical and structural studies focused on the unique Phe 36 "gate" residue, which functions to exclude water from the active site. Taken together, the findings from these studies offer molecular insights into organofluorine recognition and design of fluorine-specific enzymes.
