Glutamate—methylamine ligase: Difference between revisions

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{{enzyme
| Name = glutathionylspermidine synthase
| EC_number = 6.3.1.8
| CAS_number = 9077-09-2
| IUBMB_EC_number = 6/3/1/8
| GO_code = 0008885
| image =
| width =
| caption =  
}}
In [[enzymology]], a '''glutathionylspermidine synthase''' ({{EC number|6.3.1.8}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
 
:glutathione + spermidine + ATP <math>\rightleftharpoons</math> glutathionylspermidine + ADP + phosphate
 
The 3 [[substrate (biochemistry)|substrates]] of this enzyme are [[glutathione]], [[spermidine]], and [[adenosine triphosphate|ATP]], whereas its 3 [[product (chemistry)|products]] are [[glutathionylspermidine]], [[adenosine diphosphate|ADP]], and [[phosphate]].
 
This enzyme belongs to the family of [[ligase]]s, 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) [spermidine 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]]. It employs one [[cofactor (biochemistry)|cofactor]], [[magnesium]].
 
==Structural studies==
 
As of late 2007, 5 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|2IO7}}, {{PDB link|2IO8}}, {{PDB link|2IO9}}, {{PDB link|2IOA}}, and {{PDB link|2IOB}}.
 
==References==
{{reflist|1}}
* {{cite journal | author = Smith K, Nadeau K, Bradley M, Walsh C, Fairlamb AH | year = 1992 | title = Purification of glutathionylspermidine and trypanothione synthetases from Crithidia fasciculata | journal = Protein. Sci. | volume = 1 | pages = 874&ndash;83  | pmid = 1304372 | doi = 10.1002/pro.5560010705 | issue = 7 | pmc = 2142158 }}
* {{cite journal | author = Bollinger JM Jr, Kwon DS, Huisman GW, Kolter R, Walsh CT | year = 1995 | title = Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase/amidase | journal = J. Biol. Chem. | volume = 270 | pages = 14031&ndash;41  | pmid = 7775463 | issue = 23 | doi=10.1074/jbc.270.23.14031}}
 
[[Category:EC 6.3.1]]
[[Category:Magnesium enzymes]]
[[Category:Enzymes of known structure]]
 
 
{{ligase-stub}}

Latest revision as of 13:54, 21 August 2013

Template:Enzyme In enzymology, a glutathionylspermidine synthase (Air Transportation Experts Kull from Wingham, has many interests that include butterflies, property developers in singapore and digital photography. Is a travel freak and in recent past made buy a house in singapore journey to Paleochristian and Byzantine Monuments of Thessalonika.) is an enzyme that catalyzes the chemical reaction

glutathione + spermidine + ATP glutathionylspermidine + ADP + phosphate

The 3 substrates of this enzyme are glutathione, spermidine, and ATP, whereas its 3 products are glutathionylspermidine, ADP, 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) [spermidine 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. 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 Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, and Template:PDB link.

References

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Template:Ligase-stub