In
enzymology
Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. A ...
, a glutathionylspermidine synthase () is an
enzyme that
catalyzes
Catalysis () is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst (). Catalysts are not consumed in the reaction and remain unchanged after it. If the reaction is rapid and the catalyst recyc ...
the
chemical reaction
:glutathione + spermidine + ATP
glutathionylspermidine + ADP + phosphate
The 3
substrates of this enzyme are
glutathione,
spermidine, and
ATP
ATP may refer to:
Companies and organizations
* Association of Tennis Professionals, men's professional tennis governing body
* American Technical Publishers, employee-owned publishing company
* ', a Danish pension
* Armenia Tree Project, non ...
, whereas its 3
products are
glutathionylspermidine,
ADP
Adp or ADP may refer to:
Aviation
* Aéroports de Paris, airport authority for the Parisian region in France
* Aeropuertos del Perú, airport operator for airports in northern Peru
* SLAF Anuradhapura, an airport in Sri Lanka
* Ampara Air ...
, and
phosphate.
This enzyme belongs to the family of
ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthases). The
systematic name of this enzyme class is gamma-L-glutamyl-L-cysteinyl-glycine:spermidine ligase (ADP-forming)
permidine is numbered so that atom N-1 is in the amino group of the aminopropyl part of the molecule''. This enzyme is also called glutathione:spermidine ligase (ADP-forming). This enzyme participates in
glutathione metabolism
Glutathione (GSH, ) is an antioxidant in plants, animals, fungi, and some bacteria and archaea. Glutathione is capable of preventing damage to important cellular components caused by sources such as reactive oxygen species, free radicals, pe ...
. It employs one
cofactor,
magnesium.
Structural studies
As of late 2007, 5
structures have been solved for this class of enzymes, with
PDB accession codes , , , , and .
References
*
*
EC 6.3.1
Magnesium enzymes
Enzymes of known structure
{{6.3-enzyme-stub