151266-48-7

Basic information

• Product Name: H-3,5-DIIODO-TYR-OME HCL
• Synonyms: L-TYROSINE, 3,5-DIIODO-, METHYL ESTER, HYDROCHLORIDE;D-3,5-DIIODOTYROSINE METHYL ESTER HYDROCHLORIDE;H-D-3,5-DIIODO-TYR-OME HCL;H-3,5-DIIODO-TYR-OME HCL;H-TYR(3,5-I2)-OME HCL;L-3,5-DIIODOTYROSINE METHYL ESTER HYDROCHLORIDE;N-ALPHA-T-BUTOXYCARBONYL-3,5-DI-IODO-L-TYROSINE METHYL ESTER HYDROCHLORIDE;Methyl 3,5-diiodo-L-tyrosinate hydrochloride 98%
• CAS NO: 151266-48-7
• Molecular Formula: C₁₀H₁₁I₂NO₃*ClH
• Molecular Weight: 483.47
• Mol File: 151266-48-7.mol
• Article Data: 1

Chemical Properties

• Boiling Point: 403.1 °C at 760 mmHg
• Flash Point: 197.6 °C
• Appearance: /
• Vapor Pressure: 4.47E-07mmHg at 25°C
• Storage Temp.: -15°C
• CAS DataBase Reference: H-3,5-DIIODO-TYR-OME HCL(CAS DataBase Reference)
• NIST Chemistry Reference: H-3,5-DIIODO-TYR-OME HCL(151266-48-7)
• EPA Substance Registry System: H-3,5-DIIODO-TYR-OME HCL(151266-48-7)

Safety Data

• Hazardous Substances Data: 151266-48-7(Hazardous Substances Data)

Usage

Uses

H-3,5-Diiodo-tyr-ome hcl

InChI:InChI=1/C10H11I2NO3.ClH/c1-16-10(15)8(13)4-5-2-6(11)9(14)7(12)3-5;/h2-3,8,14H,4,13H2,1H3;1H/t8-;/m1./s1

Upstream product

• 67-56-1 methanol 
• 300-39-0 3,5-diiodo-l-tyrosine 

Downstream Products

• 192377-03-0 (S)-2-{2-[2-(2,6-Dichloro-phenylamino)-phenyl]-acetylamino}-3-(4-hydroxy-3,5-diiodo-phenyl)-propionic acid methyl ester 
• 208330-96-5 N-[N-(3,4-dichlorophenyl)-D,L-alanyl]-(3,5-diiodo)-L-tyrosine methyl ester 

Relevant articles and documents

Structure-Activity Relationships of cyclo(l -Tyrosyl- l -tyrosine) Derivatives Binding to Mycobacterium tuberculosis CYP121: Iodinated Analogues Promote Shift to High-Spin Adduct

A series of analogues of cyclo(l-tyrosyl-l-tyrosine), the substrate of the Mycobacterium tuberculosis enzyme CYP121, have been synthesized and analyzed by UV-vis and electron paramagnetic resonance spectroscopy and by X-ray crystallography. The introduction of iodine substituents onto cyclo(l-tyrosyl-l-tyrosine) results in sub-μM binding affinity for the CYP121 enzyme and a complete shift to the high-spin state of the heme FeIII. The introduction of halogens that are able to interact with heme groups is thus a feasible approach to the development of next-generation, tight binding inhibitors of the CYP121 enzyme, in the search for novel antitubercular compounds.