Gamma-glutamyl transferases: A structural, mechanistic and physiological perspective

doi:10.1007/s11515-014-1288-0

Front. Biol.

2014, Vol. 9

Issue (1) : 51-65 https://doi.org/10.1007/s11515-014-1288-0

REVIEW

Gamma-glutamyl transferases: A structural, mechanistic and physiological perspective

Sharath BALAKRISHNA,Asmita A. PRABHUNE(

)

Division of Biochemical Sciences, National Chemical Laboratory, Dr. Homi Bhabha Road, Pune 411008, Maharashtra, India

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Abstract

Gamma glutamyl transferases (GGT) are highly conserved enzymes that occur from bacteria to humans. They remove terminal γ-glutamyl residue from peptides and amides. GGTs play an important role in the homeostasis of glutathione (a major cellular antioxidant) and in the detoxification of xenobiotics in mammals. They are implicated in diseases like diabetes, inflammation, neurodegenerative diseases and cardiovascular diseases. The physiological role of GGTs in bacteria is still unclear. Nothing is known about the basis for the strong conservation of the enzyme across the living system. The review focuses on the enzyme’s physiology, chemistry and structural properties of the enzyme with emphasis on the evolutionary relationships. The available data indicate that the members of the GGT family share common structural features but are functionally heterogenous.

Keywords Gamma glutamyl transferase Ntn hydrolase structure catalysis function

Corresponding Author(s): Asmita A. PRABHUNE

Issue Date: 09 October 2014

Cite this article:

Sharath BALAKRISHNA,Asmita A. PRABHUNE. Gamma-glutamyl transferases: A structural, mechanistic and physiological perspective[J]. Front. Biol., 2014, 9(1): 51-65.

URL:

https://academic.hep.com.cn/fib/EN/10.1007/s11515-014-1288-0
https://academic.hep.com.cn/fib/EN/Y2014/V9/I1/51

Fig.1 Multiple sequence alignment of GGT from different organisms. The sequence numbering corresponds to B. subtilis GGT. Identical residues are shaded, and similar residues are boxed. The residues representing catalytic nucleophile, substrate binding, and oxyanion hole are marked with the letters N, B, and O, respectively (residue identity as in Ref X). Sequences shown are for GGTs of, B. subtilis (P54422), E. coli (P18956), rat (Q9QWE9), human (P36269), Culex mosquito (B0XE48), Arabidopsis thaliana (Q39078) and yeast (Q05902). The respective UniProtKB accession number is given in the parenthesis. The figure was prepared with CLUSTALW (Thompson et al., 1994) and ESPRIPT (Gouet et al., 1999).

Fig.2 Structures of GGTs from (A) B. subtilis (PDB Code 2v36) and (B) humans (PDB Code 4GDX.α-Helices and β-strands are represented as cylinders and arrows respectively. (C) Superposition of Cα trace of GGTs from B. subtilis (red) and humans (blue). The figures were prepared using PyMOL (The PyMOL Molecular Graphics System, Version 1.6 Schr?dinger, LLC).

Fig.3 Diagrammatic representation of interactions that bind the γ-glutamyl moiety of the substrate to the active site. Interactions with the catalytic nucleophile and stabilization of the tetrahedral intermediate by oxyanion hole are also shown.

Fig.4 Schematic representation of the mechanism of GGT catalyzed hydrolysis of a γ-glutamyl amide.

Fig.5 Schematic representation of γ-Glutamyl Cycle.

Tab.1 Physiological role of some GGT members

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