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102579-72-6

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102579-72-6 Usage

Chemical Properties

off-white to beige crystalline powder

Check Digit Verification of cas no

The CAS Registry Mumber 102579-72-6 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,0,2,5,7 and 9 respectively; the second part has 2 digits, 7 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 102579-72:
(8*1)+(7*0)+(6*2)+(5*5)+(4*7)+(3*9)+(2*7)+(1*2)=116
116 % 10 = 6
So 102579-72-6 is a valid CAS Registry Number.

102579-72-6SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 18, 2017

Revision Date: Aug 18, 2017

1.Identification

1.1 GHS Product identifier

Product name (1S,4R)-4-azaniumylcyclopent-2-ene-1-carboxylate

1.2 Other means of identification

Product number -
Other names cis-4-Amino-2-cyclopentene-1-carboxylic acid

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:102579-72-6 SDS

102579-72-6Relevant articles and documents

Chemical preparation method of 2-azabicyclo [2.2.1] hept-5-ene-3-one with optical activity

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Paragraph 0023; 0029-0031; 0041; 0047-0049; 0059; 0065-0067, (2020/05/08)

The invention discloses a chemical preparation method of 2-azabicyclo [2.2.1] hept-5-ene-3-one with optical activity. The chemical preparation method comprises the following steps: racemic 2-azabicyclo [2.2.1] hept-5-ene-3-one which is easily available on the market is used as a raw material and is subjected to chemical resolution to obtain (+/-) 4-aminocyclopent-2-ene-1-carboxylic acid methyl ester with optical activity, (+/-) 4-aminocyclopent-2-ene-1-carboxylic acid is prepared by hydrolysis, and the (+/-) 4-aminocyclopent-2-ene-1-carboxylic acid is subjected to intramolecular condensation to obtain the 2-azabicyclo [2.2.1] hept-5-ene-3-one with optical activity. The method has the advantages that the use of an enzyme fermentation method is avoided, the repeatability is good, and the yield is high.

Method for synthesizing (1R,4S)-1-amino-4-hydroxymethyl-2-cyclopentene hydrochloride

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Paragraph 0017; 0018, (2017/07/23)

The invention relates to a method for synthesizing (1R,4S)-1-amino-4-hydroxymethyl-2-cyclopentene hydrochloride. According to the method, the reaction conditions are mild, (1S,4R)-(-)-2-azabicyalo[2,2,1]hepta-5-alkene-3-ketone is directly used, (1R,4S)-1-amino-4-hydroxymethyl-2-cyclopentene hydrochloride is obtained through the reactions of hydrolysis and reducing, the yield is high, and the optical purity is high.

Catalytic Promiscuity of Ancestral Esterases and Hydroxynitrile Lyases

Devamani, Titu,Rauwerdink, Alissa M.,Lunzer, Mark,Jones, Bryan J.,Mooney, Joanna L.,Tan, Maxilmilien Alaric O.,Zhang, Zhi-Jun,Xu, Jian-He,Dean, Antony M.,Kazlauskas, Romas J.

supporting information, p. 1046 - 1056 (2016/02/05)

Catalytic promiscuity is a useful, but accidental, enzyme property, so finding catalytically promiscuous enzymes in nature is inefficient. Some ancestral enzymes were branch points in the evolution of new enzymes and are hypothesized to have been promiscuous. To test the hypothesis that ancestral enzymes were more promiscuous than their modern descendants, we reconstructed ancestral enzymes at four branch points in the divergence hydroxynitrile lyases (HNL's) from esterases ~100 million years ago. Both enzyme types are α/β-hydrolase-fold enzymes and have the same catalytic triad, but differ in reaction type and mechanism. Esterases catalyze hydrolysis via an acyl enzyme intermediate, while lyases catalyze an elimination without an intermediate. Screening ancestral enzymes and their modern descendants with six esterase substrates and six lyase substrates found higher catalytic promiscuity among the ancestral enzymes (P 0.01). Ancestral esterases were more likely to catalyze a lyase reaction than modern esterases, and the ancestral HNL was more likely to catalyze ester hydrolysis than modern HNL's. One ancestral enzyme (HNL1) along the path from esterase to hydroxynitrile lyases was especially promiscuous and catalyzed both hydrolysis and lyase reactions with many substrates. A broader screen tested mechanistically related reactions that were not selected for by evolution: decarboxylation, Michael addition, γ-lactam hydrolysis and 1,5-diketone hydrolysis. The ancestral enzymes were more promiscuous than their modern descendants (P = 0.04). Thus, these reconstructed ancestral enzymes are catalytically promiscuous, but HNL1 is especially so.

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