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
catalytic activity
ligase activity
ligase activity, forming carbon-nitrogen bonds
binding
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
acid-amino acid ligase activity
glutathione synthase activity
Process
glutathione metabolic process
glutathione biosynthetic process
metabolic process
cellular metabolic process
peptide 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