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Escherichia coli K-12 substr. MG1655 Reaction: 6.3.1.8/6.3.1.9


Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number: 6.3.1.8, 6.3.1.9

Enzymes and Genes:
fused glutathionylspermidine amidase / glutathionylspermidine synthetaseInferred from experiment: gss

In Pathway: glutathionylspermidine biosynthesis

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name for 6.3.1.8: glutathionylspermidine synthase

Enzyme Commission Synonyms for 6.3.1.8: glutathione:spermidine ligase (ADP-forming)

Enzyme Commission Primary Name for 6.3.1.9: trypanothione synthase

Enzyme Commission Synonyms for 6.3.1.9: glutathionylspermidine:glutathione ligase (ADP-forming)

Summary:
This reaction synthesizes glutathionylspermidine.

Enzyme Commission Summary for 6.3.1.8:
Involved in the synthesis of trypanothione in trypanosomatids. The enzyme from Escherichia coli is bifunctional and also catalyzes the EC 3.5.1.78 reaction, resulting in a net hydrolysis of ATP.

Enzyme Commission Summary for 6.3.1.9:
The enzyme, characterized from several trypanosomatids (e.g. Trypanosoma cruzi) catalyses two subsequent reactions, leading to production of trypanothione from glutathione and spermidine. Some trypanosomatids (e.g. Crithidia species and some Leishmania species) also contain an enzyme that only carries out the first reaction (cf. EC 6.3.1.8, glutathionylspermidine synthase). The enzyme is bifunctional, and also catalyses the hydrolysis of glutathionylspermidine and trypanothione (cf. EC 3.5.1.78, glutathionylspermidine amidase).

Citations: [Bollinger95, Smith92]

Gene-Reaction Schematic

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:6.3.1.8, BRENDA:EC:6.3.1.9, ENZYME:EC:6.3.1.8, ENZYME:EC:6.3.1.9, IUBMB-ExplorEnz:EC:6.3.1.8, IUBMB-ExplorEnz:EC:6.3.1.9


References

Bollinger95: Bollinger JM, Kwon DS, Huisman GW, Kolter R, Walsh CT (1995). "Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase/amidase." J Biol Chem 1995;270(23);14031-41. PMID: 7775463

Smith92: Smith K, Nadeau K, Bradley M, Walsh C, Fairlamb AH (1992). "Purification of glutathionylspermidine and trypanothione synthetases from Crithidia fasciculata." Protein Sci 1(7);874-83. PMID: 1304372


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by Pathway Tools version 19.5 (software by SRI International) on Fri Feb 12, 2016, biocyc13.