Literature summary for 3.4.19.13 extracted from

Terzyan, S.S.; Burgett, A.W.; Heroux, A.; Smith, C.A.; Mooers, B.H.; Hanigan, M.H.
Human gamma-glutamyl transpeptidase 1 structures of the free enzyme, inhibitor-bound tetrahedral transition states, and glutamate-bound enzyme reveal novel movement within the active site during catalysis (2015), J. Biol. Chem., 290, 17576-17586 .

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Cloned(Commentary)

Cloned (Comment)	Organism
the natural variant V272A of the human enzyme is expressed in Pichia pastoris strain X-33	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystals of are grown at room temperature by vapor diffusion with the hanging drop method. For crystallization studies, the natural variant V272A of the human enzyme is expressed in Pichia pastoris strain X-33, purified, and deglycosylated. Crystal structures of human enzyme, including the free enzyme, inhibitor-bound transition states, and glutamate-bound enzyme. Crystal structures of human gamma-glutamyl transpeptidase show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor bound tetrahedral transition states and finally to the glutamate bound structure prior to the release of this final product of the reaction. The structure of the apoenzyme shows flexibility within the active site. The serine-borate-bound enzyme crystal structure demonstrates that serine-borate occupies the active site of the enzyme, resulting in an enzyme-inhibitor complex that replicates the enzyme's tetrahedral intermediate/transition state. The structure of 2-amino-4-[[3-(carboxymethyl)phenyl](methyl)phosphono]-butanoic acid-bound enzyme reveals its interactions with the enzyme and why neutral phosphonate diesters are more potent inhibitors than monoanionic phosphonates	Homo sapiens

Crystallization (Comment)

Organism

crystals of are grown at room temperature by vapor diffusion with the hanging drop method. For crystallization studies, the natural variant V272A of the human enzyme is expressed in Pichia pastoris strain X-33, purified, and deglycosylated. Crystal structures of human enzyme, including the free enzyme, inhibitor-bound transition states, and glutamate-bound enzyme. Crystal structures of human gamma-glutamyl transpeptidase show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor bound tetrahedral transition states and finally to the glutamate bound structure prior to the release of this final product of the reaction. The structure of the apoenzyme shows flexibility within the active site. The serine-borate-bound enzyme crystal structure demonstrates that serine-borate occupies the active site of the enzyme, resulting in an enzyme-inhibitor complex that replicates the enzyme's tetrahedral intermediate/transition state. The structure of 2-amino-4-[[3-(carboxymethyl)phenyl](methyl)phosphono]-butanoic acid-bound enzyme reveals its interactions with the enzyme and why neutral phosphonate diesters are more potent inhibitors than monoanionic phosphonates

Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
V272A	natural variant of the human enzyme	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
2-amino-4-[[3-(carboxymethyl)phenyl](methyl)phosphono]-butanoic acid	-	Homo sapiens
additional information	neutral phosphonate diesters are more potent inhibitors than monoanionic phosphonates	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cell surface	-	Homo sapiens	9986	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P19440	-	-

Purification (Commentary)

Purification (Comment)	Organism
for crystallization studies, the natural variant V272A of the human enzyme is expressed in Pichia pastoris strain X-33, purified, and deglycosylated	Homo sapiens

Synonyms

Synonyms	Comment	Organism
GGT1	-	Homo sapiens

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
additional information	-	inactivating the enzyme with 2-amino-4-[[3-(carboxymethyl)phenyl](methyl)phosphono]-butanoic acid stabilizes the structure of the enzyme. It increases the melting temperature of the enzyme by about 20°C at all pH levels tested independent of the buffer	Homo sapiens
51	-	melting temperature of the enzyme in bicine buffer, pH 10.0	Homo sapiens
55	-	melting temperature of the enzyme in BisTris buffer, pH 5.0	Homo sapiens
58	-	melting temperature of the enzyme in sodium citrate buffer, pH 6.7	Homo sapiens
70.5	-	melting temperature of the enzyme inactivated with 2-amino-4-[[3-(carboxymethyl)phenyl](methyl)phosphono]-butanoic acid in BisTris buffer, pH 5.0	Homo sapiens
71	-	melting temperature of the enzyme inactivated with 2-amino-4-[[3-(carboxymethyl)phenyl](methyl)phosphono]-butanoic acid in bicine buffer, pH 10.0	Homo sapiens
75	-	melting temperature of the enzyme inactivated with 2-amino-4-[[3-(carboxymethyl)phenyl](methyl)phosphono]-butanoic acid in sodium citrate buffer, pH 6.7	Homo sapiens

General Information

General Information	Comment	Organism
metabolism	the enzyme plays a role in asthma, reperfusion injury, and cancer	Homo sapiens
physiological function	gamma-glutamyl transpeptidase 1 is essential in cysteine homeostasis	Homo sapiens