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・ Glutathione reductase
・ Glutathione S-transferase
・ Glutathione S-transferase A1
・ Glutathione S-transferase Mu 1
・ Glutathione S-transferase, C-terminal domain
・ Glutathione synthase
・ Glutathione synthetase
・ Glutathione synthetase deficiency
・ Glutathione thiolesterase
・ Glutathione-ascorbate cycle
・ Glutathione—CoA-glutathione transhydrogenase
・ Glutathione—cystine transhydrogenase
・ Glutathione—homocystine transhydrogenase
・ Glutathionuria
・ Glutathionylspermidine amidase
Glutathionylspermidine synthase
・ Glutaurine
・ Gluteal aponeurosis
・ Gluteal artery
・ Gluteal gait
・ Gluteal line
・ Gluteal muscles
・ Gluteal nerve
・ Gluteal sulcus
・ Gluteal tuberosity
・ Gluteal vein
・ Glutelin
・ Gluten
・ Gluten challenge test
・ Gluten exorphin


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Glutathionylspermidine synthase : ウィキペディア英語版
Glutathionylspermidine synthase

In enzymology, a glutathionylspermidine synthase () is an enzyme that catalyzes the chemical reaction
:glutathione + spermidine + ATP \rightleftharpoons 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) (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 , , , , and .

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