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

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

Structural basis for feedback and pharmacological inhibition of Saccharomyces cerevisiae glutamate cysteine ligase

Structural characterization of glutamate cysteine ligase (GCL), the enzyme that catalyzes the initial, rate-limiting step in glutathione biosynthesis, has revealed many of the molecular details of substrate recognition. To further delineate the mechanistic details of this critical enzyme, we have determined the structures of two inhibited forms of Saccharomyces cerevisiae GCL (ScGCL), which shares significant sequence identity with the human enzyme. In vivo, GCL activity is feedback regulated by glutathione. Examination of the structure of ScGCL-glutathione complex (2.5 A ; R = 19.9%, Rfree = 25.1%) indicates that the inhibitor occupies both the glutamate- and the presumed cysteine-binding site and disrupts the previously observed Mg2+ coordination in the ATP-binding site. L-Buthionine-S-sulfoximine (BSO) is a mechanism-based inhibitor of GCL and has been used extensively to deplete glutathione in cell culture and in vivo model systems. Inspection of the ScGCL-BSO structure (2.2 A ; R = 18.1%, Rfree = 23.9%) confirms that BSO is phosphorylated on the sulfoximine nitrogen to generate the inhibitory species and reveals contacts that likely contribute to transition state stabilization. Overall, these structures advance our understanding of the molecular regulation of this critical enzyme and provide additional details of the catalytic mechanism of the enzyme.

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.

Synthesis of hydroxymethylglutathione from glutathione and L-serine catalyzed by carboxypeptidase Y.

Hydroxymethylglutathione (gamma-L-glutamyl-L-cysteinyl-L-serine; hmGSH) occurs in many species belonging to the family Gramineae, but the biosynthetic pathway for hmGSH has not been identified. We found that carboxypeptidase Y (CPY), but not carboxypeptidase A, catalyzed hmGSH synthesis from glutathione and L-serine in vitro at acidic pH. CPY also catalyzed methylglutathione synthesis from glutathione and L-alanine. These findings suggested that a carboxypeptidase-like enzyme may be involved in hmGSH synthesis in vivo.

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.

Augmentation of human and rat lenticular glutathione in vitro by prodrugs of γ-L-glutamyl-L-cysteine

A marked age-related decrease in glutathione (GSH) levels as well as depression of γ-glutamyl-cysteine synthetase activity are factors that are believed to render the aged lens more susceptible to oxidative stress and, therefore, to cataractogenesis. Providing γ-L-glutamyl-L-cysteine, the dipeptide precursor of GSH, would effectively bypass the compromised first step in its biosynthesis and should protect the lens from GSH depletion. Accordingly, some bioreversible sulfhydryl-, amino-, and C-terminal carboxyl- protected prodrug forms of this dipeptide were prepared. Sulfhydryl protection was in the form of an acetyl thioester, while the carboxyl group was protected as the ethyl ester. These prodrugs were evaluated for their GSH-enhancing activity in cultured human and rat lenses in vitro using an assay that measured the incorporation of [14C]glycine into lens GSH. Ethyl S-acetyl-γ-L-glutamyl-L-cysteinate (2) raised GSH levels in human lenses by 25% and in rat lenses by >150%. These data suggest that 2 may have potential as an anticataract agent since ethyl γ-L-glutamyl-L-cysteinate (1a), the des-S-acetyl analog of 2, had been shown (by others) to protect against experimental rodent cataracts. GSH augmentation by 1a was 2% in human lenses and 25% in rat lenses, considerably less than that shown by 2.

CADYSTIN A AND B, MAJOR UNIT PEPTIDES COMPRISING CADMIUM BINDING PEPTIDES INDUCED IN A FISSION YEAST-----SEPARATION, REVISION OF STRUCTURES AND SYNTHESIS

The unit peptide, cadystin, of the cadmium-binding peptides occuring in a fission yeast was further separated into two major components, cadystin A and B, structures of which were determined to be 1 and 2, respectively, and confirmed by synthesis.The structure previously reported for cadystin was thus revised.

Synthesis of γ-Glutamylpeptides by γ-Glutamylcysteine Synthetase from Proteus mirabilis

Syntheses of various γ-glutamylpeptides were examined taking use of the highly purified γ-glutamylcysteine synthetase from Proteus mirabilis.The accumulation of each peptide was measured after long time incubation, and good formation was observed in the synthesis of peptides of following amino acids, L-cysteine, L-α-aminobutyrate, L-serine, L-homoserine, glycine, L-alanine, L-norvaline, L-lysine, L-threonine, taurine and L-valine.Peptide syntheses were confirmed by analyses of the component amino acids, after hydrolysis of the peptides.The structure of the glutamylpeptides, especially the peptide-linkage at the γ-carbonyl residue of L-glutamate, was determined by mass spectrometry of the N-trifluoroacetyl methylester derivatives of the glutamylpeptides.Enzymatic synthesis of γ-glutamyl-L-α-aminobutyrate was also confirmed by PMR spectrometry in the comparison with chemically synthesized compound.