33932-35-3

Basic information

• Product Name: glutathionylspermidine
• Synonyms: glutathionylspermidine
• CAS NO: 33932-35-3
• Molecular Formula: C17H34N6O5S
• Molecular Weight: 434.55406
• Mol File: 33932-35-3.mol

Chemical Properties

• Boiling Point: 643.3°Cat760mmHg
• Flash Point: 342.8°C
• Appearance: /
• Density: 1.256g/cm³
• Vapor Pressure: 1.4E-30mmHg at 25°C
• Refractive Index: 1.546
• CAS DataBase Reference: glutathionylspermidine(CAS DataBase Reference)
• NIST Chemistry Reference: glutathionylspermidine(33932-35-3)
• EPA Substance Registry System: glutathionylspermidine(33932-35-3)

Safety Data

• Hazardous Substances Data: 33932-35-3(Hazardous Substances Data)

Usage

Definition

ChEBI: The spermidine amide of glutathione.

InChI:InChI=1/C17H34N6O5S/c18-6-1-2-7-20-8-3-9-21-15(25)10-22-16(26)13(11-29)23-14(24)5-4-12(19)17(27)28/h12-13,20,29H,1-11,18-19H2,(H,21,25)(H,22,26)(H,23,24)(H,27,28)/t12-,13-/m0/s1

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Relevant articles and documents

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.

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