6710-20-9

Basic information

• Product Name: N-(4-fluorobenzylidene)-3-[(4-methylbenzyl)sulfanyl]-4H-1,2,4-triazol-4-amine
• CAS NO: 6710-20-9
• Molecular Formula: C₁₇H₁₅FN₄S
• Molecular Weight: 326.3912
• Mol File: 6710-20-9.mol
• Article Data: 10

Chemical Properties

• Boiling Point: 506°C at 760 mmHg
• Flash Point: 259.8°C
• Density: 1.24g/cm³
• Vapor Pressure: 2.3E-10mmHg at 25°C
• Refractive Index: 1.634
• CAS DataBase Reference: N-(4-fluorobenzylidene)-3-[(4-methylbenzyl)sulfanyl]-4H-1,2,4-triazol-4-amine(CAS DataBase Reference)
• NIST Chemistry Reference: N-(4-fluorobenzylidene)-3-[(4-methylbenzyl)sulfanyl]-4H-1,2,4-triazol-4-amine(6710-20-9)
• EPA Substance Registry System: N-(4-fluorobenzylidene)-3-[(4-methylbenzyl)sulfanyl]-4H-1,2,4-triazol-4-amine(6710-20-9)

Safety Data

• Hazardous Substances Data: 6710-20-9(Hazardous Substances Data)

Upstream product

• 23052-19-9 (γEC)2 
• 4510-09-2 N-benzyloxycarbonyl-L-glutamic acid-5-hydrazide 
• 953-18-4 S-benzyl-L-cysteine ethyl ester 
• 100051-89-6 (R)-3-L-γ-glutamyl-2,2-dimethyl-thiazolidine-4-carboxylic acid 
• 52-90-4 L-Cysteine 
• 142-47-2 monosodium L-glutamate 
• 95014-75-8 H-γ-L-Glu-L-Cys-γ-L-Glu-L-Cys-Gly-OH (cadystin B <2>) 
• 190063-00-4 (R)-3-((S)-4-Amino-4-carboxy-butyryl)-2-methyl-thiazolidine-4-carboxylic acid 
• 70-18-8 GLUTATHIONE 
• 56-41-7 L-alanin 
• 56-45-1 L-serin 
• 25830-77-7 N-phthaloyl-L-glutamic anhydride 
• 27025-41-8 Oxidized glutathione 
• 142-47-2 monosodium glutamate 

Relevant articles and documents

Redox-dependent stability of the γ-glutamylcysteine synthetase enzyme of Escherichia coli: A novel means of redox regulation

Glutathione is a thiol-containing tripeptide that plays important roles in redox-related processes. The first step in glutathione biosynthesis is catalysed by γ-GCS (γ-glutamylcysteine synthetase). The crystal structure of Escherichia coli γ-GCS has revealed the presence of a disulfide bond. As the disulfide-bonding cysteine residues Cys372 and Cys395 are not well conserved among γ-GCS enzymes in this lineage, we have initiated a biochemical genetic strategy to investigate the functional importance of these and other cysteine residues. In a cysteine-free γ-GCS that was non-functional, suppressor analysis yielded combinations of cysteine and aromatic residues at the position of the disulfide bond, and one mutant that lacked any cysteine residues. Kinetic analysis of the wild-type and mutant enzymes revealed that the disulfide bond was not involved in determining the affinity of the enzyme towards its substrate, but had an important role in determining the stability of the protein, and its catalytic efficiency. We showthat in vivo the γ-GCS enzyme can also exist in a reduced form and that the mutants lacking the disulfide bond show a decreased half-life. These results demonstrate a novel means of regulation of γ-GCS by the redox environment that works by an alteration in its stability. The Authors Journal compilation

A novel catalytic ability of γ-glutamylcysteine synthetase of Escherichia coli and its application in theanine production

γ-Glutamylcysteine synthetase (γGCS, EC 6.3.2.2) catalyzes the formation of γ-glutamylcysteine from L-glutamic acid (Glu) and L-cysteine (Cys) in an ATP-dependent manner. While γGCS can use various amino acids as substrate, little is known about whether it can use non-amino acid compounds in place of Cys. We determined that γGCS from Escherichia coli has the ability to combine Glu and amines to form γ-glutamylamides. The reaction rate depended on the length of the methylene chain of the amines in the following order: n-propylamine > butylamine > ethylamine methylamine. The optimal pH for the reaction was narrower and more alkaline than for the reaction with an amino acid. The newly found catalytic ability of γGCS was used in the production of theanine (γ-glutamylethylamine). The resting cells of E. coli expressing γGCS, in which ATP was regenerated through glycolysis, synthesized 12.1 mm theanine (18 h) from 429 mm ethylamine.

Conversion of Glutathione into Cadystins and Their Analogs Catalyzed by Carboxypeptidase Y

Cadystins induced in a fission yeast treated with Cd2+ are the higher homologs of glutathione. In the present work, glutathione was incubated with Carboxypeptidase Y at a high substrate concentration. The reaction afforded not only the degraded product, but also cadystins and their analogs. A possible transformation pathway for glutathione by this enzyme is proposed.