28038-02-0

Basic information

• Product Name: N-[({3-[(4-aminobutyl)amino]propyl}amino)acetyl]-N-[(2R)-2-amino-3-sulfanylpropanoyl]-L-glutamine
• CAS NO: 28038-02-0
• Molecular Formula: C₁₇H₃₄N₆O₅S
• Molecular Weight: 434.5541
• Mol File: 28038-02-0.mol

Chemical Properties

• Boiling Point: 643.3°C at 760 mmHg
• Flash Point: 342.8°C
• Density: 1.256g/cm³
• Vapor Pressure: 3.34E-18mmHg at 25°C
• Refractive Index: 1.559
• CAS DataBase Reference: N-[({3-[(4-aminobutyl)amino]propyl}amino)acetyl]-N-[(2R)-2-amino-3-sulfanylpropanoyl]-L-glutamine(CAS DataBase Reference)
• NIST Chemistry Reference: N-[({3-[(4-aminobutyl)amino]propyl}amino)acetyl]-N-[(2R)-2-amino-3-sulfanylpropanoyl]-L-glutamine(28038-02-0)
• EPA Substance Registry System: N-[({3-[(4-aminobutyl)amino]propyl}amino)acetyl]-N-[(2R)-2-amino-3-sulfanylpropanoyl]-L-glutamine(28038-02-0)

Safety Data

• Hazardous Substances Data: 28038-02-0(Hazardous Substances Data)

Upstream product

• 70374-98-0 Gly-di-Boc-Spe(3,4) 
• 81659-82-7 N-α-tert-butoxycarbonyl-L-glutamic acid γ-N-succinimidyl ester α-tert-butyl ester 
• 108081-91-0 (S)-2-tert-Butoxycarbonylamino-4-[(R)-2-tert-butylsulfanyl-1-(2,5-dioxo-pyrrolidin-1-yloxycarbonyl)-ethylcarbamoyl]-butyric acid tert-butyl ester 
• 1002754-96-2 C₂₀H₃₈N₆O₇S 

Relevant articles and documents

Synthesis of the Trypanosomatid Metabolites Trypanothione, and N1-Mono- and N8-Mono-glutathionylspermidine

The trypanosomatid metabolite trypanothione 1,N8-bis(glutathionyl)spermidine> and its biosynthetic co-metabolites the isomeric N1- and N8-mono-glutathionylspermidines have been synthesised by a mild route whic

Ni2 +-activated glyoxalase i from Escherichia coli: Substrate specificity, kinetic isotope effects and evolution within the βαβββ superfamily

The Escherichia coli glyoxalase system consists of the metalloenzymes glyoxalase I and glyoxalase II. Little is known regarding Ni 2 +-activated E. coli glyoxalase I substrate specificity, its thiol cofactor preference, the presence or absence of any substrate kinetic isotope effects on the enzyme mechanism, or whether glyoxalase I might catalyze additional reactions similar to those exhibited by related βαβ ββ structural superfamily members. The current investigation has shown that this two-enzyme system is capable of utilizing the thiol cofactors glutathionylspermidine and trypanothione, in addition to the known tripeptide glutathione, to convert substrate methylglyoxal to non-toxic d-lactate in the presence of Ni2 + ion. E. coli glyoxalase I, reconstituted with either Ni2 + or Cd2 +, was observed to efficiently process deuterated and non-deuterated phenylglyoxal utilizing glutathione as cofactor. Interestingly, a substrate kinetic isotope effect for the Ni 2 +-substituted enzyme was not detected; however, the proton transfer step was observed to be partially rate limiting for the Cd 2 +-substituted enzyme. This is the first non-Zn 2 +-activated GlxI where a metal ion-dependent kinetic isotope effect using deuterium-labelled substrate has been observed. Attempts to detect a glutathione conjugation reaction with the antibiotic fosfomycin, similar to the reaction catalyzed by the related superfamily member FosA, were unsuccessful when utilizing the E. coli glyoxalase I E56A mutein.