1. Badenhorst, C. P. S., Van Der Sluis, R., Erasmus, E. & van Dijk, A. A. Glycine conjugation: Importance in metabolism, the role of glycine N-acyltransferase, and factors that influence interindividual variation. Expert Opin. Drug Metab. Toxicol. 9, 1139–1153 (2013).
2. Badenhorst, C. P. S., Erasmus, E., Van Der Sluis, R., Nortje, C. & Van Dijk, A. A. A new perspective on the importance of glycine conjugation in the metabolism of aromatic acids. Drug Metab. Rev. 46, 343–361 (2014).
3. Oginawati, K., Hanif Anka, A.A., Susetyo, S.H., Febriana, S.A., Tanziha, I., Prakoeswa, C.R.S. Urinary hippuric acid level as a biological indicator of toluene exposure on batik workers. Heliyon 7 10.1016/j.heliyon.2021.e07775 (2021).
4. Tian, X. et al. Downregulation of GLYAT facilitates tumor growth and metastasis and poor clinical outcomes through the PI3K/AKT/Snail pathway in human breast cancer. Front. Oncol. 11, 1–12 (2021).
5. Ud-Din, A. I. M. S., Tikhomirova, A. & Roujeinikova, A. Structure and functional diversity of GCN5-related N-acetyltransferases (GNAT). Int. J. Mol. Sci. 17, (2016).
6. Dian, C. et al. High-resolution snapshots of human N-myristoyltransferase in action illuminate a mechanism promoting N-terminal Lys and Gly myristoylation. Nat. Commun. 11, 1–15 (2020).
7. Badenhorst, C. P. S., Jooste, M. & Van Dijk, A. A. Enzymatic characterization and elucidation of the catalytic mechanism of a recombinant bovine glycine N-acyltransferase. Drug Metab. Dispos. 40, 346–352 (2012).
8. Van der Sluis, R., Badenhorst, C. P. S., Van der Westhuizen, F. H. & Van Dijk, A. A. Characterisation of the influence of genetic variations on the enzyme activity of a recombinant human glycine N-acyltransferase. Gene 515, 447–453 (2013).
9. Schulke, D. & Sass, J. O. Frequent sequence variants of human glycine N-acyltransferase (GLYAT) and inborn errors of metabolism. Biochimie 183, 30–34 (2021).
10. Rohwer, J. M., Schutte, C. & van der Sluis, R. Functional characterisation of three glycine N-acyltransferase variants and the effect on glycine conjugation to benzoyl–CoA. Int. J. Mol. Sci. 22, 1–19 (2021).
11. van der Sluis, R. et al. Conservation of the coding regions of the glycine N-acyltransferase gene further suggests that glycine conjugation is an essential detoxification pathway. Gene 571, 126–134 (2015).
12. Waluk, D. P., Sucharski, F., Sipos, L., Silberring, J. & Hunt, M. C. Reversible lysine acetylation regulates activity of human glycine N-acyltransferase-like 2 (hGLYATL2): Implications for production of glycine-conjugated signaling molecules. J. Biol. Chem. 287, 16158–16167 (2012).
13. Butt, T. R., Edavettal, S. C., Hall, J. P. & Mattern, M. R. SUMO fusion technology for difficult-to-express proteins. Protein Expr. Purif. 43, 1–9 (2005).
14. Studier, F. W. Protein production by auto-induction in high density shaking cultures. Protein Expr. Purif. 41, 207–234 (2005).
15. Kabsch, W. XDS. Acta Crystallogr., Sect. D: Biol. Crystallogr. 66, 125–132 (2010).
16. Winter, G. Xia2: An expert system for macromolecular crystallography data reduction. J. Appl. Crystallogr. 43, 186–190 (2010).
17. Diederichs, K., McSweeney, S. & Ravelli, R. B. G. Zero-dose extrapolation as part of macromolecular synchrotron data reduction. Acta Crystallogr., Sect. D: Biol. Crystallogr. 59, 903–909 (2003).
18. Usón, I. & Sheldrick, G. M. An introduction to experimental phasing of macromolecules illustrated by SHELX; New autotracing features. Acta Crystallogr., Sect. D: Struct. Biol. 74, 106–116 (2018).
19. Pannu, N. S. et al. Recent advances in the CRANK software suite for experimental phasing. Acta Crystallogr., Sect. D: Biol. Crystallogr. 67, 331–337 (2011).
20. Baek, M. et al. Accurate prediction of protein structures and interactions using a 3-track network. Science (80-. ). 373, 871-876 (2021).
21. McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658–674 (2007).
22. Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr., Sect. D: Biol. Crystallogr. 66, 486–501 (2010).
23. Murshudov, G. N. et al. REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr., Sect. D: Biol. Crystallogr. 67, 355–367 (2011).