73684-69-2

Usage

Uses

Used in Veterinary Medicine:
Miporamicin is used as an antibiotic for treating respiratory infections in cattle and pigs. It is effective against a variety of Gram-positive and Gram-negative bacteria, including antibiotic-resistant strains, making it a valuable treatment option in veterinary medicine.
Used in Livestock Farming:
In the livestock farming industry, miporamicin is used as a therapeutic agent to combat bacterial infections in animals. Its low toxicity and effectiveness against a broad spectrum of bacteria make it a preferred choice for maintaining the health of farm animals and ensuring the quality of livestock products.
It is important to use miporamicin judiciously to prevent the development of antibiotic resistance in agricultural settings.

InChI:InChI=1/C37H61NO13/c1-11-27-37(43,18-46-36-33(45-10)32(44-9)29(41)23(6)48-36)34-26(49-34)14-13-25(39)20(3)16-21(4)31(19(2)12-15-28(40)50-27)51-35-30(42)24(38(7)8)17-22(5)47-35/h12-15,19-24,26-27,29-36,41-43H,11,16-18H2,1-10H3/b14-13+,15-12+/t19-,20+,21-,22+,23+,24-,26-,27+,29+,30+,31+,32+,33+,34+,35-,36+,37-/m0/s1

Synthetic route

mycinamicin II 3'-N-oxide (122825-79-0) → mycinamicin II (73684-69-2)

Conditions	Yield
With triphenylphosphine In dichloromethane at 55℃; for 67h;	56%

mycinamicin-IV → C36H59NO11 + mycinamicin-I + mycinamicin-III (73684-71-6) + mycinamicin V (73684-72-7) + mycinamicin II (73684-69-2)

Conditions	Yield
With multifunctional biosynthetic P450 monooxygenase; rhodococcus reductase domain; NADPH In aq. buffer at 28℃; for 2h; pH=7.3; Kinetics; Reagent/catalyst; Enzymatic reaction;	A 18.5% B n/a C n/a D n/a E n/a

mycinamicin V (73684-72-7) → mycinamicin II (73684-69-2)

Conditions	Yield
Multi-step reaction with 2 steps 1: 39 percent / MCPBA, disodium hydrogen phosphate / CH2Cl2 / 23 h / 60 °C 2: 56 percent / triphenylphosphine / CH2Cl2 / 67 h / 55 °C View Scheme

Upstream product

• 122825-79-0 mycinamicin II 3'-N-oxide 
• 73684-72-7 mycinamicin V 

Relevant academic research and scientific papers

New reactions and products resulting from alternative interactions between the P450 enzyme and redox partners

Cytochrome P450 enzymes are capable of catalyzing a great variety of synthetically useful reactions such as selective C-H functionalization. Surrogate redox partners are widely used for reconstitution of P450 activity based on the assumption that the choice of these auxiliary proteins or their mode of action does not affect the type and selectivity of reactions catalyzed by P450s. Herein, we present an exceptional example to challenge this postulate. MycG, a multifunctional biosynthetic P450 monooxygenase responsible for hydroxylation and epoxidation of 16-membered ring macrolide mycinamicins, is shown to catalyze the unnatural N-demethylation(s) of a range of mycinamicin substrates when partnered with the free Rhodococcus reductase domain RhFRED or the engineered Rhodococcus-spinach hybrid reductase RhFRED-Fdx. By contrast, MycG fused with the RhFRED or RhFRED-Fdx reductase domain mediates only physiological oxidations. This finding highlights the larger potential role of variant redox partner protein-protein interactions in modulating the catalytic activity of P450 enzymes.

Semisynthetic Macrolide Antibacterials Derived from Tylosin. Synthesis of 3-O-Acetyl-23-O-demycinosyl-4''-O-isovaleryltylosin and Related Compounds, as well as the 12,13-Epoxy Derivatives

Selective acylation techniques have been developed that enable the synthesis of 3-O-acetyl-4''-O-isovaleryltylosin and 3-O-acetyl-23-O-demycinosyl-4''-O-isovaleryltylosin to be carried out in an efficient manner starting from tylosin.The syntheses of the 2'-O-acetyl, 23-O-acetyl, and 2',23-di-O-acetyl derivatives of the latter are also described.The synthesis of key hydrazones is also described.The regio- and stereo-selective epoxidation of tylosin and its acyl derivatives afforded the 12,13-epoxyanalogues, which were used to synthesize novel acylated 12,13-epoxy derivatives of 23-O-demycinosyltylosin.