118395-73-6 Usage
Uses
Used in Pharmaceutical Industry:
Chloroorienticin A is used as an antibiotic for the treatment of various bacterial infections. Its potent antimicrobial activity makes it a valuable compound in the development of new antibiotics to combat drug-resistant bacteria.
Used in Research and Development:
Chloroorienticin A serves as a valuable research tool for studying the mechanisms of antibiotic action and resistance. Its unique structure and properties can provide insights into the development of new antimicrobial agents and strategies to overcome antibiotic resistance.
Used in Drug Discovery:
Due to its potent antimicrobial properties, chloroorienticin A is used as a starting point for the development of new drugs. Researchers can modify its structure to create derivatives with improved properties, such as increased potency, selectivity, or reduced side effects.
Check Digit Verification of cas no
The CAS Registry Mumber 118395-73-6 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,1,8,3,9 and 5 respectively; the second part has 2 digits, 7 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 118395-73:
(8*1)+(7*1)+(6*8)+(5*3)+(4*9)+(3*5)+(2*7)+(1*3)=146
146 % 10 = 6
So 118395-73-6 is a valid CAS Registry Number.
InChI:InChI=1/C73H88Cl2N10O26/c1-26(2)14-38(79-7)64(96)84-54-56(91)30-9-12-42(36(74)16-30)106-44-18-32-19-45(60(44)111-71-61(58(93)57(92)46(25-86)108-71)110-49-24-73(6,78)63(95)28(4)105-49)107-43-13-10-31(17-37(43)75)59(109-48-23-72(5,77)62(94)27(3)104-48)55-69(101)83-53(70(102)103)35-20-33(87)21-41(89)50(35)34-15-29(8-11-40(34)88)51(66(98)85-55)82-67(99)52(32)81-65(97)39(22-47(76)90)80-68(54)100/h8-13,15-21,26-28,38-39,46,48-49,51-59,61-63,71,79,86-89,91-95H,14,22-25,77-78H2,1-7H3,(H2,76,90)(H,80,100)(H,81,97)(H,82,99)(H,83,101)(H,84,96)(H,85,98)(H,102,103)/t27-,28-,38+,39-,46+,48-,49-,51+,52+,53+,54+,55-,56+,57+,58?,59+,61+,62-,63-,71-,72-,73-/m0/s1
118395-73-6Relevant articles and documents
A systematic investigation of the synthetic utility of glycopeptide glycosyltransferases
Oberthuer, Markus,Leimkuhler, Catherine,Kruger, Ryan G.,Lu, Wei,Walsh, Christopher T.,Kahne, Daniel
, p. 10747 - 10752 (2007/10/03)
Glycosyltransferases involved in the biosynthesis of bacterial secondary metabolites may be useful for the generation of sugar-modified analogues of bioactive natural products. Some glycosyltransferases have relaxed substrate specificity, and it has been assumed that promiscuity is a feature of the class. As part of a program to explore the synthetic utility of these enzymes, we have analyzed the substrate selectivity of glycosyltransferases that attach similar 2-deoxy-L-sugars to glycopeptide aglycons of the vancomycin-type, using purified enzymes and chemically synthesized TDP β-2-deoxy-L-sugar analogues. We show that while some of these glycopeptide glycosyltransferases are promiscuous, others tolerate only minor modifications in the substrates they will handle. For example, the glycosyltransferases GtfC and GtfD, which transfer 4-epi-L-vancosamine and L-vancosamine to C-2 of the glucose unit of vancomycin pseudoaglycon and chloroorienticin B, respectively, show moderately relaxed donor substrate specificities for the glycosylation of their natural aglycons. In contrast, GtfA, a transferase attaching 4-epi-L-vancosamine to a benzylic position, only utilizes donors that are closely related to its natural TDP sugar substrate. Our data also show that the spectrum of donors utilized by a given enzyme can depend on whether the natural acceptor or an analogue is used, and that GtfD is the most versatile enzyme for the synthesis of vancomycin analogues.
