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Identification and characterization of gamma-glutamylamine cyclotransferase, an enzyme responsible for gamma-glutamyl-epsilon-lysine catabolism.

Oakley AJ, Coggan M, Board PG
J Biol Chem 285 9642-9648 (2010)
Related entries: 3juc, 3jud

Cited: 24 times
EuropePMC logo PMID: 20110353

Abstract

Gamma-glutamylamine cyclotransferase (GGACT) is an enzyme that converts gamma-glutamylamines to free amines and 5-oxoproline. GGACT shows high activity toward gamma-glutamyl-epsilon-lysine, derived from the breakdown of fibrin and other proteins cross-linked by transglutaminases. The enzyme adopts the newly identified cyclotransferase fold, observed in gamma-glutamylcyclotransferase (GGCT), an enzyme with activity toward gamma-glutamyl-alpha-amino acids (Oakley, A. J., Yamada, T., Liu, D., Coggan, M., Clark, A. G., and Board, P. G. (2008) J. Biol. Chem. 283, 22031-22042). Despite the absence of significant sequence identity, several residues are conserved in the active sites of GGCT and GGACT, including a putative catalytic acid/base residue (GGACT Glu(82)). The structure of GGACT in complex with the reaction product 5-oxoproline provides evidence for a common catalytic mechanism in both enzymes. The proposed mechanism, combined with the three-dimensional structures, also explains the different substrate specificities of these enzymes. Despite significant sequence divergence, there are at least three subfamilies in prokaryotes and eukaryotes that have conserved the GGCT fold and GGCT enzymatic activity.

Reviews - 3jub mentioned but not cited (1)

  1. γ-Glutamylamines and neurodegenerative diseases. Jeitner TM, Battaile K, Cooper AJ. Amino Acids 44 129-142 (2013)

Articles - 3jub mentioned but not cited (1)

  1. Identification and characterization of gamma-glutamylamine cyclotransferase, an enzyme responsible for gamma-glutamyl-epsilon-lysine catabolism. Oakley AJ, Coggan M, Board PG. J Biol Chem 285 9642-9648 (2010)


Reviews citing this publication (4)

  1. Emerging regulatory paradigms in glutathione metabolism. Liu Y, Hyde AS, Simpson MA, Barycki JJ. Adv Cancer Res 122 69-101 (2014)
  2. The glutathione cycle: Glutathione metabolism beyond the γ-glutamyl cycle. Bachhawat AK, Yadav S. IUBMB Life 70 585-592 (2018)
  3. Glutathione Degradation. Bachhawat AK, Kaur A. Antioxid Redox Signal 27 1200-1216 (2017)
  4. Transglutaminse 2 and EGGL, the protein cross-link formed by transglutaminse 2, as therapeutic targets for disabilities of old age. Bains W. Rejuvenation Res 16 495-517 (2013)

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  1. Mammalian proapoptotic factor ChaC1 and its homologues function as γ-glutamyl cyclotransferases acting specifically on glutathione. Kumar A, Tikoo S, Maity S, Sengupta S, Sengupta S, Kaur A, Bachhawat AK. EMBO Rep 13 1095-1101 (2012)
  2. Defining the cytosolic pathway of glutathione degradation in Arabidopsis thaliana: role of the ChaC/GCG family of γ-glutamyl cyclotransferases as glutathione-degrading enzymes and AtLAP1 as the Cys-Gly peptidase. Kumar S, Kaur A, Chattopadhyay B, Bachhawat AK. Biochem J 468 73-85 (2015)
  3. ChaC2, an Enzyme for Slow Turnover of Cytosolic Glutathione. Kaur A, Gautam R, Srivastava R, Chandel A, Kumar A, Karthikeyan S, Bachhawat AK. J Biol Chem 292 638-651 (2017)
  4. Morphology, physiological characteristics, and complete sequence of marine bacteriophage ϕRIO-1 infecting Pseudoalteromonas marina. Hardies SC, Hwang YJ, Hwang CY, Jang GI, Cho BC. J Virol 87 9189-9198 (2013)
  5. Helicobacter pylori induces somatic mutations in TP53 via overexpression of CHAC1 in infected gastric epithelial cells. Wada Y, Takemura K, Tummala P, Uchida K, Kitagaki K, Furukawa A, Ishige Y, Ito T, Hara Y, Suzuki T, Mimuro H, Board PG, Eishi Y. FEBS Open Bio 8 671-679 (2018)
  6. Structure and function of allophanate hydrolase. Fan C, Li Z, Yin H, Xiang S. J Biol Chem 288 21422-21432 (2013)
  7. A Cystine-Cysteine Intercellular Shuttle Prevents Ferroptosis in xCTKO Pancreatic Ductal Adenocarcinoma Cells. Meira W, Daher B, Parks SK, Cormerais Y, Durivault J, Tambutte E, Pouyssegur J, Vučetić M. Cancers (Basel) 13 1434 (2021)
  8. The acetaminophen metabolite N-acetyl-p-benzoquinone imine (NAPQI) inhibits glutathione synthetase in vitro; a clue to the mechanism of 5-oxoprolinuric acidosis? Walker V, Mills GA, Anderson ME, Ingle BL, Jackson JM, Moss CL, Sharrod-Cole H, Skipp PJ. Xenobiotica 47 164-175 (2017)
  9. Tn-Seq reveals hidden complexity in the utilization of host-derived glutathione in Francisella tularensis. Ramsey KM, Ledvina HE, Tresko TM, Wandzilak JM, Tower CA, Tallo T, Schramm CE, Peterson SB, Skerrett SJ, Mougous JD, Dove SL. PLoS Pathog 16 e1008566 (2020)
  10. Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites. Serrano P, Pedrini B, Geralt M, Jaudzems K, Mohanty B, Horst R, Herrmann T, Elsliger MA, Wilson IA, Wüthrich K. Acta Crystallogr Sect F Struct Biol Cryst Commun 66 1393-1405 (2010)
  11. Structural and Functional Analyses of Human ChaC2 in Glutathione Metabolism. Nguyen YTK, Park JS, Jang JY, Kim KR, Vo TTL, Kim KW, Han BW. Biomolecules 10 E31 (2019)
  12. Association of epigenetic alterations in the human C7orf24 gene with the aberrant gene expression in malignant cells. Ohno Y, Hattori A, Yoshiki T, Kakeya H. J Biochem 154 355-362 (2013)
  13. AIG2A and AIG2B limit the activation of salicylic acid-regulated defenses by tryptophan-derived secondary metabolism in Arabidopsis. Wang Z, Yang L, Jander G, Bhawal R, Zhang S, Liu Z, Oakley A, Hua J. Plant Cell 34 4641-4660 (2022)
  14. Probing the specificity of gamma-glutamylamine cyclotransferase: an enzyme involved in the metabolism of transglutaminase-catalyzed protein crosslinks. Bowser TE, Trawick ML. Amino Acids 44 143-150 (2013)
  15. The Combined Use of in Silico, in Vitro, and in Vivo Analyses to Assess Anti-cancerous Potential of a Bioactive Compound from Cyanobacterium Nostoc sp. MGL001. Niveshika, Verma E, Maurya SK, Mishra R, Mishra AK. Front Pharmacol 8 873 (2017)
  16. Keep calm and carry on: AIG2A/B prevent over-activation of TDSM-mediated defense response. Chan C. Plant Cell 34 4126-4127 (2022)
  17. The ChaC family of γ-glutamyl cyclotransferases is required for Leishmania to switch to a slow growth state and for long-term survival of the parasite. Das S, Panja P, Chowdhury G, Biswas S, Dholey Y, Adak S. J Biol Chem 298 102510 (2022)
  18. Urinary Metabolomic Profiling after Administration of Corydalis Tuber and Pharbitis Seed Extract in Healthy Korean Volunteers. Jeong HC, Park JE, Seo Y, Kim MG, Shin KH. Pharmaceutics 13 522 (2021)


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