51093-55-1 Usage
Description
ROSEOFLAVIN, also known as a benzopteridine derivative of riboflavin, is a dark reddish/brown crystalline solid. It is characterized by the substitution of the methyl group at position 8 of riboflavin with a dimethylamino group. This unique structure grants ROSEOFLAVIN various applications in different fields, particularly in the biological and pharmaceutical industries.
Uses
Used in Antimicrobial Applications:
ROSEOFLAVIN is used as an antibacterial agent, particularly effective against certain gram-positive bacteria such as Staphylococcus aureus, Sarcina latea, Bacillus cereus, and Bacillus subtilis. Its weak antibacterial activity makes it a valuable compound in the development of new antimicrobial strategies.
Used in Biochemical Research:
In the field of biochemical research, ROSEOFLAVIN serves as an analog that competes with riboflavin in Lactobacillus casei. It acts as a riboflavin kinase substrate and inhibitor, which aids in understanding the mechanisms of riboflavin metabolism and its role in various biological processes.
Used in Flavin Biosynthesis:
ROSEOFLAVIN is utilized as a substrate to mimic riboflavin in flavin biosynthesis. However, it leads to the formation of inactive flavin co-factors, which can be useful in studying the effects of these co-factors on cellular processes and their potential applications in drug development.
Used in Gene Expression Regulation:
More recently, ROSEOFLAVIN has been identified as an important regulator of bacterial gene expression. It binds to untranslated regions of RNA, known as ribo-switching sites, which allows for the manipulation of gene expression in various bacterial species. This discovery opens up new possibilities for the development of targeted antibacterial therapies and a deeper understanding of gene regulation mechanisms.
Biochem/physiol Actions
Roseoflavin is an analog of flavin mononucleotide (FMN) and riboflavin with antimicrobial activity. Roseoflavin is converted to the flavin mononucleotide (FMN) analog roseoflavin mononucleotide (RoFMN) by flavokinase and to the flavin adenine dinucleotide (FAD) analog roseoflavin adenine dinucleotide (RoFAD) by FAD synthetase, and acts as a riboflavin antagonist. Roseoflavin is an inhibitor of bacterial riboflavin riboswitches, cis regulatory elements present in non-coding RNA that specifically bind to natural ligands to regulate gene expression. Roseoflavin, converted to RoFMN, blocks the flavin mononucleotide riboswitch-mediated expression of the ribB gene, which is required for riboflavin biosynthesis.
Check Digit Verification of cas no
The CAS Registry Mumber 51093-55-1 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 5,1,0,9 and 3 respectively; the second part has 2 digits, 5 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 51093-55:
(7*5)+(6*1)+(5*0)+(4*9)+(3*3)+(2*5)+(1*5)=101
101 % 10 = 1
So 51093-55-1 is a valid CAS Registry Number.
InChI:InChI=1/C18H23N5O6/c1-8-4-9-11(5-10(8)22(2)3)23(6-12(25)15(27)13(26)7-24)16-14(19-9)17(28)21-18(29)20-16/h4-5,12-13,15,24-27H,6-7H2,1-3H3,(H,21,28,29)
51093-55-1Relevant articles and documents
Graham et al.ng
, p. 1274 (1977)
Structural and kinetic studies on RosA, the enzyme catalysing the methylation of 8-demethyl-8-amino- d -riboflavin to the antibiotic roseoflavin
Tongsook, Chanakan,Uhl, Michael K.,Jankowitsch, Frank,Mack, Matthias,Gruber, Karl,Macheroux, Peter
, p. 1531 - 1549 (2016/04/26)
N,N-8-demethyl-8-amino-d-riboflavin dimethyltransferase (RosA) catalyses the final dimethylation of 8-demethyl-8-amino-d-riboflavin (AF) to the antibiotic roseoflavin (RoF) in Streptomyces davawensis. In the present study, we solved the X-ray structure of RosA, and determined the binding properties of substrates and products. Moreover, we used steady-state and rapid reaction kinetic studies to obtain detailed information on the reaction mechanism. The structure of RosA was found to be similar to that of previously described S-adenosylmethionine (SAM)-dependent methyltransferases, featuring two domains: a mainly α-helical 'orthogonal bundle' and a Rossmann-like domain (α/β twisted open sheet). Bioinformatics studies and molecular modelling enabled us to predict the potential SAM and AF binding sites in RosA, suggesting that both substrates, AF and SAM, bind independently to their respective binding pocket. This finding was confirmed by kinetic experiments that demonstrated a random-order 'bi-bi' reaction mechanism. Furthermore, we determined the dissociation constants for substrates and products by either isothermal titration calorimetry or UV/Vis absorption spectroscopy, revealing that both products, RoF and S-adenosylhomocysteine (SAH), bind more tightly to RosA compared with the substrates, AF and SAM. This suggests that RosA may contribute to roseoflavin resistance in S. davawensis. The tighter binding of products is also reflected by the results of inhibition experiments, in which RoF and SAH behave as competitive inhibitors for AF and SAM, respectively. We also showed that formation of a ternary complex of RosA, RoF and SAH (or SAM) leads to drastic spectral changes that are indicative of a hydrophobic environment. Database Structural data are available in the Protein Data Bank under accession number 4D7K. 8-demethyl-N,N-8-amino-D-riboflavin dimethyltransferase (RosA) catalyzes the dimethylation of 8-demethyl-8-amino-D-riboflavin (AF) to the antibiotic roseoflavin (RoF) in Streptomyces davawensis via a random-order mechanism. RosA has a structural topology similar to other S-adenosylmethionine (SAM)-dependent methyltransferases. Slow synthesis of RoF and the tight binding of the products, RoF and SAH, suggest that RosA may contribute to a mechanism for RoF resistance.
