Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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Escherichia coli K-12 substr. MG1655 Reaction: 6.3.1.8/6.3.1.9

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 6.3.1.8 , 6.3.1.9

Enzymes and Genes:
fused glutathionylspermidine amidase / glutathionylspermidine synthetase Inferred from experiment : gss

In Pathway: glutathionylspermidine biosynthesis

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. 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: ?

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 SRI International Pathway Tools version 18.5 on Wed Dec 17, 2014, BIOCYC14B.