Glutathione synthetase (Q08220)

Identification
NameGlutathione synthetase
Synonyms
  • GSH synthetase
  • GSH-S
  • Glutathione synthase
Gene NameGSH2
Enzyme Class
Biological Properties
General FunctionInvolved in ATP binding
Specific FunctionATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
Cellular LocationNot Available
SMPDB Pathways
Glutathione metabolismPW002395 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Glutathione metabolismec00480 Map00480
SMPDB Reactions
Gamma-Glutamylcysteine + Glycine + Adenosine triphosphate → ADP + phosphate + hydron + Glutathione
KEGG Reactions
Adenosine triphosphate + Glycine + Gamma-Glutamylcysteine → phosphate + Glutathione + hydron + ADP
Metabolites
YMDB IDNameView
YMDB00016GlycineShow
YMDB00109Adenosine triphosphateShow
YMDB00160GlutathioneShow
YMDB00252Gamma-GlutamylcysteineShow
YMDB00862hydronShow
YMDB00907phosphateShow
YMDB00914ADPShow
GO Classification
Component
Not Available
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
acid-amino acid ligase activity
glutathione synthase activity
catalytic activity
ligase activity
ligase activity, forming carbon-nitrogen bonds
binding
nucleoside binding
purine nucleoside binding
Process
peptide metabolic process
glutathione metabolic process
glutathione biosynthetic process
metabolic process
cellular metabolic process
Gene Properties
Chromosome Locationchromosome 15
LocusYOL049W
Gene Sequence>1476 bp ATGGCACACTATCCACCTTCCAAGGATCAATTGAATGAATTGATCCAGGAAGTTAACCAA TGGGCTATCACTAATGGATTATCCATGTATCCTCCTAAATTCGAGGAGAACCCATCAAAT GCATCGGTGTCACCAGTAACTATCTATCCAACCCCAATTCCTAGGAAATGTTTTGATGAG GCCGTTCAAATACAACCGGTATTCAATGAATTATACGCCCGTATTACCCAAGATATGGCC CAACCTGATTCTTATTTACATAAAACAACTGAAGCGTTAGCTCTATCAGATTCCGAGTTT ACTGGAAAACTGTGGTCTCTATACCTTGCTACCTTAAAATCTGCACAGTACAAAAAGCAG AATTTTAGGCTAGGTATATTTAGATCAGATTATTTGATTGATAAGAAAAAGGGTACTGAA CAGATTAAGCAAGTCGAGTTTAATACAGTGTCAGTGTCATTTGCAGGCCTTAGCGAGAAA GTTGATAGATTGCACTCTTATTTAAATAGGGCAAACAAGTACGATCCTAAAGGACCAATT TATAATGATCAAAATATGGTCATTTCTGATTCAGGATACCTTTTGTCTAAGGCATTGGCC AAAGCTGTGGAATCGTATAAGTCACAACAAAGTTCTTCTACAACTAGTGATCCTATTGTC GCATTCATTGTGCAAAGAAACGAGAGAAATGTGTTTGATCAAAAGGTCTTGGAATTGAAT CTGTTGGAAAAATTCGGTACCAAATCTGTTAGGTTGACGTTTGATGATGTTAACGATAAA TTGTTCATTGATGATAAAACGGGAAAGCTTTTCATTAGGGACACAGAGCAGGAAATAGCG GTGGTTTATTACAGAACGGGTTACACAACCACTGATTACACGTCCGAAAAGGACTGGGAG GCAAGACTATTCCTCGAAAAAAGTTTCGCAATAAAGGCCCCAGATTTACTCACTCAATTA TCTGGCTCCAAGAAAATTCAGCAATTGTTGACAGATGAGGGCGTATTAGGTAAATACATC TCCGATGCTGAGAAAAAGAGTAGTTTGTTAAAAACTTTTGTCAAAATATATCCCTTGGAT GATACGAAGCTTGGCAGGGAAGGCAAGAGGCTGGCATTAAGTGAGCCCTCTAAATACGTG TTAAAACCACAGCGGGAAGGTGGCGGAAACAATGTTTATAAAGAAAATATTCCTAATTTT TTGAAAGGTATCGAAGAACGTCACTGGGATGCATATATTCTCATGGAGTTGATTGAACCA GAGTTGAATGAAAATAATATTATATTACGTGATAACAAATCTTACAACGAACCAATCATC AGTGAACTAGGAATTTATGGTTGCGTTCTATTTAACGACGAGCAAGTTTTATCGAACGAA TTTAGTGGCTCATTACTAAGATCCAAATTTAATACTTCAAATGAAGGTGGAGTGGCGGCA GGATTCGGATGTTTGGACAGTATTATTCTTTACTAG
Protein Properties
Pfam Domain Function
Protein Residues491
Protein Molecular Weight55814.69922
Protein Theoretical pI5.32
PDB Fileshow
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Glutathione synthetase MAHYPPSKDQLNELIQEVNQWAITNGLSMYPPKFEENPSNASVSPVTIYPTPIPRKCFDE AVQIQPVFNELYARITQDMAQPDSYLHKTTEALALSDSEFTGKLWSLYLATLKSAQYKKQ NFRLGIFRSDYLIDKKKGTEQIKQVEFNTVSVSFAGLSEKVDRLHSYLNRANKYDPKGPI YNDQNMVISDSGYLLSKALAKAVESYKSQQSSSTTSDPIVAFIVQRNERNVFDQKVLELN LLEKFGTKSVRLTFDDVNDKLFIDDKTGKLFIRDTEQEIAVVYYRTGYTTTDYTSEKDWE ARLFLEKSFAIKAPDLLTQLSGSKKIQQLLTDEGVLGKYISDAEKKSSLLKTFVKIYPLD DTKLGREGKRLALSEPSKYVLKPQREGGGNNVYKENIPNFLKGIEERHWDAYILMELIEP ELNENNIILRDNKSYNEPIISELGIYGCVLFNDEQVLSNEFSGSLLRSKFNTSNEGGVAA GFGCLDSIILY
References
External Links
ResourceLink
Saccharomyces Genome Database GSH2
Uniprot IDQ08220
Uniprot NameGSHB_YEAST
GenBank Gene IDAY723864
Genebank Protein ID51830516
PDB ID
1M0W
General Reference
  • Inoue, Y., Sugiyama, K., Izawa, S., Kimura, A. (1998). "Molecular identification of glutathione synthetase (GSH2) gene from Saccharomyces cerevisiae." Biochim Biophys Acta 1395:315-320.9512666
  • Dujon, B., Albermann, K., Aldea, M., Alexandraki, D., Ansorge, W., Arino, J., Benes, V., Bohn, C., Bolotin-Fukuhara, M., Bordonne, R., Boyer, J., Camasses, A., Casamayor, A., Casas, C., Cheret, G., Cziepluch, C., Daignan-Fornier, B., Dang, D. V., de Haan, M., Delius, H., Durand, P., Fairhead, C., Feldmann, H., Gaillon, L., Kleine, K., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Nature 387:98-102.9169874
  • Hu, Y., Rolfs, A., Bhullar, B., Murthy, T. V., Zhu, C., Berger, M. F., Camargo, A. A., Kelley, F., McCarron, S., Jepson, D., Richardson, A., Raphael, J., Moreira, D., Taycher, E., Zuo, D., Mohr, S., Kane, M. F., Williamson, J., Simpson, A., Bulyk, M. L., Harlow, E., Marsischky, G., Kolodner, R. D., LaBaer, J. (2007). "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Genome Res 17:536-543.17322287
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956
  • Gogos, A., Shapiro, L. (2002). "Large conformational changes in the catalytic cycle of glutathione synthase." Structure 10:1669-1676.12467574