37333-48-5

Basic information

• Product Name: factor 420
• Synonyms: factor 420;7,8-didemethyl-8-hydroxy-5-deazariboflavin
• CAS NO: 37333-48-5
• Molecular Formula: C₁₆H₁₇N₃O₇
• Molecular Weight: 363.32208
• Mol File: 37333-48-5.mol
• Article Data: 7

Chemical Properties

• Boiling Point: °Cat760mmHg
• Flash Point: °C
• Appearance: /
• Density: 1.7g/cm³
• Refractive Index: 1.747
• CAS DataBase Reference: factor 420(CAS DataBase Reference)
• NIST Chemistry Reference: factor 420(37333-48-5)
• EPA Substance Registry System: factor 420(37333-48-5)

Safety Data

• Hazardous Substances Data: 37333-48-5(Hazardous Substances Data)

Usage

Definition

ChEBI: Riboflavin in which the nitrogen at position 5 is replaced by CH and the methyl groups at positions 7 and 8 are substituted by hydrogen and hydroxy, respectively.

InChI:InChI=1/C16H17N3O7/c20-6-12(23)13(24)11(22)5-19-10-4-8(21)2-1-7(10)3-9-14(19)17-16(26)18-15(9)25/h1-4,11-13,20,22-24H,5-6H2,(H2,17,18,25,26)

Upstream product

• 71415-47-9 1-Deoxy-1-<(3-hydroxyphenyl)amino>-D-ribitol 
• 71415-48-0 2,3:4,5-Bis-O-methoxymethylene-1-deoxy-1-(3,4-dihydro-8-hydroxy-2,4-dioxopyrimido<4,5-b>quinolin-10-(2H)-yl)-D-ribitol 
• 63570-47-8 L-tyrosine-(2-d) 
• 14036-89-6 5-amino-6-(D-ribitylamino)uracil 
• 71491-01-5 5-Amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedinone 5'-phosphate 
• 60-18-4 L-tyrosine 
• 591-27-5 m-Hydroxyaniline 
• 71454-03-0 1-Deoxy-1-<(3-hydroxyphenyl)(1,2,3,6-tetrahydro-2,6-dioxo-4-pyrimidinyl)amino>-D-ribitol 
• 71415-46-8 N-(3-Hydroxyphenyl)-D-ribosylamine 
• 56962-11-9 2-chloro-4-hydroxybenzaldehyde 
• 33106-48-8 1-deoxy-1-[(2,6-dioxo-1,2,3,6-tetrahydro-4-pyrimidinyl)amino]-D-ribitol 
• 65644-24-8 6-chloro-2,4-dioxohexahydropyrimidine-5-carbaldehyde 
• 121942-75-4 3-[(tert-butyldimethylsilyl)oxy]aniline 

Relevant articles and documents

A robust synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin

The biosynthetic precursor of redox cofactor F420, 7,8-didemethyl-8-hydroxy-5-deazariboflavin, was prepared in four steps from 6-chlorouracil, 2-chloro-4-hydroxybenzaldehyde and bis-isopropylidene protected D-ribose. The latter aldehyde was transformed to the corresponding protected ribitylamine via the oxime, which was submitted to reduction with LiAlH4. Key advantage compared to previous syntheses is the utilization of a polyol-protective group which allowed the chromatographic purification of a key-intermediate product providing the target compound with high purity.

Biosynthetic versatility and coordinated action of 5′-deoxyadenosyl radicals in deazaflavin biosynthesis

Coenzyme F420 is a redox cofactor found in methanogens and in various actinobacteria. Despite the major biological importance of this cofactor, the biosynthesis of its deazaflavin core (8-hydroxy-5-deazaflavin, Fo) is still poorly understood. Fo synthase, the enzyme involved, is an unusual multidomain radical SAM enzyme that uses two separate 5′-deoxyadenosyl radicals to catalyze Fo formation. In this paper, we report a detailed mechanistic study on this complex enzyme that led us to identify (1) the hydrogen atoms abstracted from the substrate by the two radical SAM domains, (2) the second tyrosine-derived product, (3) the reaction product of the CofH-catalyzed reaction, (4) the demonstration that this product is a substrate for CofG, and (5) a stereochemical study that is consistent with the formation of a p-hydroxybenzyl radical at the CofH active site. These results enable us to propose a mechanism for Fo synthase and uncover a new catalytic motif in radical SAM enzymology involving the use of two 5′-deoxyadenosyl radicals to mediate the formation of a complex heterocycle.

Biosynthesis of F0, precursor of the F420 cofactor, requires a unique two radical-SAM domain enzyme and tyrosine as substrate

Cofactors play key roles in metabolic pathways. Among them F420 has proved to be a very attractive target for the selective inhibition of archaea and actinobacteria. Its biosynthesis, in a unique manner, involves a key enzyme, F0-synthase. This enzyme is a large monomer in actinobacteria, while it is constituted of two subunits in archaea and cyanobacteria. We report here the purification of both types of F 0-synthase and their in vitro activities. Our study allows us to establish that F0-synthase, from both types, uses 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione and tyrosine as substrates but not 4-hydroxylphenylpyruvate as previously suggested. Furthermore, our data support the fact that F0-synthase generates two 5′- deoxyadenosyl radicals for catalysis which is unprecedented in reaction catalyzed by radical SAM enzymes.