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1750-45-4 Usage

Chemical Properties

Off-White Solid

Uses

Different sources of media describe the Uses of 1750-45-4 differently. You can refer to the following data:
1. 6-Hydroxychlorzoxazone has been used for HPLC-based metabolic assays of chlorzoxazone.
2. A major metabolite of chlorzoxazone. Formed by the actions of cytochrome P450IIE1

Biochem/physiol Actions

6-hydroxy Chlorzoxazone is a novel metabolite of chlorzoxazone. It is formed by the hydroxylation of chlorzoxazone by cytochrome P450 family 2 subfamily E member 1 (CYP2E1) enzyme. The determination of formation and clearance of 6-hydroxychlorzoxazone is used as a reliable marker of CYP2E1 metabolic activity.

Check Digit Verification of cas no

The CAS Registry Mumber 1750-45-4 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 1,7,5 and 0 respectively; the second part has 2 digits, 4 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 1750-45:
(6*1)+(5*7)+(4*5)+(3*0)+(2*4)+(1*5)=74
74 % 10 = 4
So 1750-45-4 is a valid CAS Registry Number.
InChI:InChI=1/C7H4ClNO3/c8-3-1-4-6(2-5(3)10)12-7(11)9-4/h1-2,10H,(H,9,11)

1750-45-4 Well-known Company Product Price

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  • Sigma

  • (UC148)  6-Hydroxychlorzoxazone  ≥98% (HPLC)

  • 1750-45-4

  • UC148-5MG

  • 7,458.75CNY

  • Detail
  • Sigma

  • (UC148)  6-Hydroxychlorzoxazone  ≥98% (HPLC)

  • 1750-45-4

  • UC148-10MG

  • 13,759.20CNY

  • Detail

1750-45-4SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 12, 2017

Revision Date: Aug 12, 2017

1.Identification

1.1 GHS Product identifier

Product name 6-Hydroxy Chlorzoxazone

1.2 Other means of identification

Product number -
Other names 5-chloro-6-hydroxy-3H-1,3-benzoxazol-2-one

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:1750-45-4 SDS

1750-45-4Downstream Products

1750-45-4Relevant articles and documents

Solar-Powered Whole-Cell P450 Catalytic Platform for C-Hydroxylation Reactions

Le, Thien-Kim,Kim, Jinhyun,Anh Nguyen, Ngoc,Huong Ha Nguyen, Thi,Sun, Eun-Gene,Yee, Su-Min,Kang, Hyung-Sik,Yeom, Soo-Jin,Beum Park, Chan,Yun, Chul-Ho

, p. 3054 - 3058 (2021)

Photobiocatalysis is a green platform for driving redox enzymatic reactions using solar energy, not needing high-cost cofactors and redox partners. Here, a visible light-driven whole-cell platform for human cytochrome P450 (CYP) photobiocatalysis was developed using natural flavins as a photosensitizer. Photoexcited flavins mediate NADPH/reductase-free, light-driven biocatalysis by human CYP2E1 both in vitro and in the whole-cell systems. In vitro tests demonstrated that the photobiocatalytic activity of CYP2E1 is dependent on the substrate type, the presence of catalase, and the acid type used as a sacificial electron donor. A protective effect of catalase was found against the inactivation of CYP2E1 heme by H2O2 and the direct transfer of photo-induced electrons to the heme iron not by peroxide shunt. Furthermore, the P450 photobiocatalysis in whole cells containing human CYPs 1A1, 1A2, 1B1, and 3A4 demonstrated the general applicability of the solar-powered, flavin-mediated P450 photobiocatalytic system.

A diversified library of bacterial and fungal bifunctional cytochrome P450 enzymes for drug metabolite synthesis

Weis, Roland,Winkler, Margit,Schittmayer, Matthias,Kambourakis, Spiros,Vink, Mandy,David Rozzell,Glieder, Anton

, p. 2140 - 2146 (2009)

Innovative biohydroxylation catalysts for the preparation of drug metabolites were developed from scratch. A set of bacterial and fungal sequences of putative and already known bifunctional P450 enzymes was identified by protein sequence alignments, expre

Chlorzoxazone metabolism by porcine cytochrome P450 enzymes and the effect of cytochrome b5

Wiercinska,Squires

, p. 857 - 862 (2010)

Chlorzoxazone (CLZ) is a commonly used nontoxic in vivo and in vitro probe for the assessment of CYP2E1 activity. Human CYP1A1 and CYP3A4 have also been shown to contribute to CLZ metabolism. For pigs to be a potential model system for humans, it is necessary that human and pig cytochromes P450 (P450) have similar metabolizing capabilities. Therefore, CLZ metabolizing capabilities and specificities of porcine P450s were investigated. In this study, the complete coding regions of six porcine P450s were amplified from liver cDNA and cloned into pcDNA3.1/V5-His TOPO vector. Expression vectors for the individual P450s and microsomal cytochrome b5 (CYB5A) were expressed in the human embryonic kidney HEK-293FT cell line to investigate their role in CLZ metabolism. As with the human enzymes, porcine CYP2E1 (Km = 290.3 μM and Vmax = 4980 pmol/h/mg total protein) and CYP1A1 (Km = 159.5 μM and Vmax = 1650 pmol/h/mg total protein) both contribute to CLZ metabolism. In addition, porcine CYP2A19 and CYP2C33v4 also metabolize the substrate, with Km = 212.1 μM and Vmax = 6680 pmol/h/mg total protein and Km = 126.3 μM and Vmax = 2100 pmol/h/mg total protein, respectively, whereas CYP3A does not. CYB5A augmented CYP2E1 and CYP2C33v4 activity in the pig, with a significant increase in activity of 85 and 73% compared with control, respectively. Thus, CLZ should be used with caution as a probe for CYP2E1 activity in the pig. However, further information regarding the abundance of different P450 isoforms is needed to fully understand their contribution in microsomal, hepatocyte, and in vivo systems in the pig. Copyright

Functional characterization of human and cynomolgus monkey cytochrome P450 2E1 enzymes

Hanioka, Nobumitsu,Yamamoto, Maki,Iwabu, Hiroyuki,Jinno, Hideto,Tanaka-Kagawa, Toshiko,Naito, Shinsaku,Shimizu, Takefumi,Masuda, Kazufumi,Katsu, Takashi,Narimatsu, Shizuo

, p. 1436 - 1445 (2007)

Cytochrome P450 2E1 (CYP2E1) is an enzyme of major toxicological interest because it metabolizes various drugs, precarcinogens and solvents to reactive metabolites. In this study, human and cynomolgus monkey CYP2E1 cDNAs (humCYP2E1 and monCYP2E1, respectively) were cloned, and the corresponding proteins were heterologously expressed in yeast cells to identify the functions of primate CYP2E1s. The enzymatic properties of CYP2E1 proteins were characterized by kinetic analysis of chlorzoxazone 6-hydroxylation and 4-nitrophenol 2-hydroxylation. humCYP2E1 and monCYP2E1 enzymes showed 94.3% identity in their amino acid sequences. The functional CYP content in yeast cell microsomes expressing humCYP2E1 was 38.4 pmol/mg protein. The level of monCYP2E1 was 42.7% of that of humCYP2E1, although no significant differences were statistically observed. The Km values of microsomes from human livers and yeast cells expressing humCYP2E1 for CYP2E1-dependent oxidation were 822 and 627 μM for chlorzoxazone 6-hydroxylation, and 422 and 514 μM for 4-nitrophenol 2-hydroxylation, respectively. The Km values of microsomes from cynomolgus monkey livers and yeast cells expressing monCYP2E1 were not significantly different from those of humans in any enzyme source. Vmax and Vmax / Km values of human liver microsomes for CYP2E1-dependent oxidation were 909 pmol/min/mg protein and 1250 nl/min/mg protein for chlorzoxazone 6-hydroxylation, and 1250 pmol/min/mg protein and 2990 nl/min/mg protein for 4-nitrophenol 2-hydroxylation, respectively. The kinetic parameter values of cynomolgus monkey livers were comparable to or lower than those of human liver microsomes (49.5-102%). In yeast cell microsomes expressing humCYP2E1, Vmax and Vmax / Km values for CYP2E1-dependent oxidation on the basis of CYP holoprotein level were 170 pmol/min/pmol CYP and 272 nl/min/pmol CYP for chlorzoxazone 6-hydroxylation, and 139 pmol/min/pmol CYP and 277 nl/min/pmol CYP for 4-nitrophenol 2-hydroxylation, respectively, and the kinetic parameters of monCYP2E1 exhibited similar values. These findings suggest that human and cynomolgus monkey CYP2E1 enzymes have high homology in their amino acid sequences, and that their enzymatic properties are considerably similar. The information gained in this study should help with in vivo extrapolation and to assess the toxicity of xenobiotics.

Method for promoting iron-catalyzed oxidation of aromatic compound carbon - hydrogen bond to synthesize phenol by ligand

-

Paragraph 0112-0113; 0129, (2021/09/21)

The method comprises the following steps: iron is used as - a catalyst metal; a sulfur-containing amino acid or cystine-derived dipeptide is a ligand; and under the common action of hydrogen peroxide as an oxidizing agent, an aromatic compound is synthesized to prepare a phenol. Under the action of an acid as an accelerant and hydrogen peroxide as an oxidizing agent, the aryl carbon - hydrogen bond is directly hydroxylated to form a phenolic compound, and the method for preparing the phenol by the catalytic oxidation reaction has a plurality of advantages. The reaction raw materials, the oxidant and the promoter are wide in source, low in price, environment-friendly and good in stability. The aromatic compound carbon - hydrogen bonds directly participate in the reaction to react in one step to form phenol. The reaction condition is mild, the functional group compatibility and the application range are wide. The reaction selectivity is good; under the optimized reaction conditions, the target product separation yield can reach 85%.

Evaluation of MTBH, a novel hesperetin derivative, on the activity of hepatic cytochrome P450 isoform in?vitro and in?vivo using a cocktail method by HPLC-MS/MS

Chen, Guanjun,Dong, Haijun,Fan, Yuru,Huang, Xiaohui,Li, Jun,Qin, Yan,Shen, Chenlin,Song, Shuai,Sun, Jiayin,Wang, Jie,Wang, Sheng,Wang, Wei,Zhang, Tianci,Zhang, Yilong

, p. 1389 - 1399 (2022/01/11)

1. 8-methylene-tert-butylamine-3′,5,7-trihydroxy-4′-methoxyflavanone (MTBH), a novel hesperidin derivative, has potential in the prevention of hepatic disease, however, its effects on cytochrome P450 isoforms (CYP450s) remains unexplored. The purpose was to investigate the effects of MTBH on the mRNA, protein levels, and activities of six CYP450s (1A2, 2C11/9, 2D2/6, 3A1/4, 2C13/19, and 2E1) in?vitro and in?vivo. 2. In vitro study, rat and human liver microsomes were adopted to elucidate the inhibitory effect of MTBH on six CYP450s using probe drugs. In vivo study, Sprague-Dawley male rats were treated with MTBH (25, 50, or 100 mg/kg for 28 consecutive days), phenobarbital (80 mg/kg for 12 consecutive days), or 0.5% CMC-Na solution (control group) by intragastric administration, then, the mRNA, protein levels and activities of liver CYP450s were analysed by real-time PCR, western blotting and probe-drug incubation systems, respectively. 3. The in?vitro study indicated that MTBH inhibits the activities of CYP3A1/4 and CYP2E1 in rat and human liver microsomes. In vivo data showed that MTBH inhibits mRNA, protein levels, and activities of CYP3A1 and CYP2E1 in medium- and high-dose MTBH groups. 4. MTBH has the potential to cause drug-drug interactions when co-administered with drugs that are metabolised by CYP3A1/4 and CYP2E1.

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