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2.3.2.2: gamma-glutamyltransferase

This is an abbreviated version!
For detailed information about gamma-glutamyltransferase, go to the full flat file.

Word Map on EC 2.3.2.2

Reaction

a (5-L-glutamyl)-peptide
+
an amino acid
=
a peptide
 +
a 5-L-glutamyl amino acid

Synonyms

(5-L-glutamyl) peptide: amino-acid 5-glutamyl transferase, alpha-glutamyl transpeptidase, AngammaGT, AsGGT1, At1g69820, At4g29210, At4g39640, At4g39650, BaGGT, BaGGT42, BaGGT469, BlGGT, BlGGT13, BsGGT168, Cgl0954, eqGGT, gamma glutamyl transferase, gamma-glutamyl peptidyltransferase, gamma-glutamyl transferase, gamma-glutamyl transferase 1, gamma-glutamyl transferase 5, gamma-glutamyl transferase/transpeptidase, gamma-glutamyl transferases, gamma-glutamyl transpeptidase, gamma-glutamyl transpeptidase 1, gamma-glutamyl transpeptidase 4, gamma-glutamyl transpeptidase-1, gamma-glutamyl-transpeptidase, gamma-glutamyltransferase, gamma-glutamyltranspeptidase, gamma-GPT, gamma-GT, gamma-GTase, gamma-GTP, gammaGT, GGT, GGT A, GGT I, GGT-1, GGT1, GGT2, GGT3, GGT4, GGT5, ggtB, GGTII protein, GGTLA1, glutamyl transpeptidase, glutamyltransferase, gamma-, HGGT, L-gamma-glutamyl transpeptidase, L-gamma-glutamyltransferase, L-glutamyltransferase, More, PnGGT, SBLGGT, VvGGT3

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.2 gamma-glutamyltransferase

Engineering

Engineering on EC 2.3.2.2 - gamma-glutamyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G481A
site-directed mutagenesis, the mutation affects both autocatalytic processing and catalytic activity of the enzyme, and causes a significant change in the functional integrity of the enzyme, the fluorescence and circular dichroism properties of the mutant proteins are basically consistent with those of BlGGT. The mutant shows increased catalytic activity
G481E
site-directed mutagenesis, the mutation affects both autocatalytic processing and catalytic activity of the enzyme, and causes a significant change in the functional integrity of the enzyme, the fluorescence and circular dichroism properties of the mutant proteins are basically consistent with those of BlGGT. The mutant shows increased catalytic activity
G481R
site-directed mutagenesis, the mutant shows increased catalytic activity, but abolished processing
G482A
site-directed mutagenesis, the mutant shows increased catalytic activity
G482E
site-directed mutagenesis, the mutant shows increased catalytic activity
G482R
site-directed mutagenesis, the mutation leads to a marked reduction in the autocatalytic processing and results in an unprocessed enzyme with insignificant catalytic activity, the fluorescence and circular dichroism properties of the mutant proteins are basically consistent with those of BlGGT. The mutant shows increased catalytic activity
N450A
Q62WE3
site-directed mutagenesis, the mutant shows about 4.7fold increased catalytic efficiency compared to wild-type
N450D
N450K
Q62WE3
site-directed mutagenesis, N450K exhibits 81% increase in KM and 44.3% decrease in kcat compared to wild-type, leading to a profound reduction in its catalytic efficiency
N450Q
site-directed mutagenesis, the mutant's theanine biosynthetic activity is similar to wild-type
N450R
Q62WE3
site-directed mutagenesis, the mutant shows a significant reduction in the catalytic activity compared to wild-type
R109E
site-directed mutagenesis, the mutation reduces the enzyme's affinity for L-Gln
R109F
site-directed mutagenesis, the mutation reduces the enzyme's affinity for L-Gln
R109K
site-directed mutagenesis of the catalytic residue results in low enzyme consumption, the mutation reduces the enzyme's affinity for L-Gln. The Arg109Lys mutant has increased transpeptidation activity and catalytic efficiency compared to the other R109 mutants. The Arg109Lys mutant shows high conversion rates for L-theanine synthesis as well
R109L
site-directed mutagenesis, the mutation reduces the enzyme's affinity for L-Gln, highly reduced transpeptidase activity compared to wild-type
R109M
site-directed mutagenesis of the catalytic residue results in reduced activity and high salt stability of the mutant, the mutation reduces the enzyme's affinity for L-Gln. The Arg109Met mutant shows increased hydrolytic activity as it completely alters the binding of L-Gln at the active site. Also, the salt stability of the mutant enzyme is significantly improved. Highly reduced transpeptidase activity compared to wild-type
R109S
site-directed mutagenesis, the mutation reduces the enzyme's affinity for L-Gln
T399A
T399C
-
complete loss of enzymatic activity
T399S
T417A
T417K
-
complete loss of enzymatic activity
T417S
N450A
-
site-directed mutagenesis, the mutant shows about 4.7fold increased catalytic efficiency compared to wild-type
-
N450K
-
site-directed mutagenesis, N450K exhibits 81% increase in KM and 44.3% decrease in kcat compared to wild-type, leading to a profound reduction in its catalytic efficiency
-
N450R
-
site-directed mutagenesis, the mutant shows a significant reduction in the catalytic activity compared to wild-type
-
T399A
-
site-directed mutagenesis, mutant structure analysis and comparison
-
R109E
-
site-directed mutagenesis, the mutation reduces the enzyme's affinity for L-Gln
-
R109K
-
site-directed mutagenesis of the catalytic residue results in low enzyme consumption, the mutation reduces the enzyme's affinity for L-Gln. The Arg109Lys mutant has increased transpeptidation activity and catalytic efficiency compared to the other R109 mutants. The Arg109Lys mutant shows high conversion rates for L-theanine synthesis as well
-
R109L
-
site-directed mutagenesis, the mutation reduces the enzyme's affinity for L-Gln, highly reduced transpeptidase activity compared to wild-type
-
R109M
-
site-directed mutagenesis of the catalytic residue results in reduced activity and high salt stability of the mutant, the mutation reduces the enzyme's affinity for L-Gln. The Arg109Met mutant shows increased hydrolytic activity as it completely alters the binding of L-Gln at the active site. Also, the salt stability of the mutant enzyme is significantly improved. Highly reduced transpeptidase activity compared to wild-type
-
R109S
-
site-directed mutagenesis, the mutation reduces the enzyme's affinity for L-Gln
-
R109E
-
site-directed mutagenesis, the mutation reduces the enzyme's affinity for L-Gln
-
R109K
-
site-directed mutagenesis of the catalytic residue results in low enzyme consumption, the mutation reduces the enzyme's affinity for L-Gln. The Arg109Lys mutant has increased transpeptidation activity and catalytic efficiency compared to the other R109 mutants. The Arg109Lys mutant shows high conversion rates for L-theanine synthesis as well
-
R109L
-
site-directed mutagenesis, the mutation reduces the enzyme's affinity for L-Gln, highly reduced transpeptidase activity compared to wild-type
-
R109M
-
site-directed mutagenesis of the catalytic residue results in reduced activity and high salt stability of the mutant, the mutation reduces the enzyme's affinity for L-Gln. The Arg109Met mutant shows increased hydrolytic activity as it completely alters the binding of L-Gln at the active site. Also, the salt stability of the mutant enzyme is significantly improved. Highly reduced transpeptidase activity compared to wild-type
-
R109S
-
site-directed mutagenesis, the mutation reduces the enzyme's affinity for L-Gln
-
D445A
-
mutation abolishes transpeptidation activity, specific activity for hydrolysis is 40.2% of that of the wild-type enzyme, salt tolerant like the wild-type enzyme
D445E
-
transpeptidation activity is 40% of hydrolysis activity, in wild-type enzyme the transpeptidation activity is 2.38times higher than the hydrolysis activity
D445N
-
transpeptidation activity is 42% of hydrolysis activity, in wild-type enzyme the transpeptidation activity is 2.38times higher than the hydrolysis activity
D445Y
-
transpeptidation activity is 40% of hydrolysis activity, in wild-type enzyme the transpeptidation activity is 2.38times higher than the hydrolysis activity
R113K
-
transpeptidation activity is 72% of hydrolysis activity, in wild-type enzyme the transpeptidation activity is 2.38times higher than the hydrolysis activity
D433N
-
mutation enables gamma-glutamyltranspeptidase to deacylate glutaryl-7-aminocepha-losporanic acid, producing 7-aminocephalosporanic acid, which is a starting material for the synthesis of semisynthetic cephalosporins
S463D
complete loss of activity, impaired autoproteolytic processing, increase in the critical bond distance of residues Q390-T391
S463K
complete loss of activity, impaired autoproteolytic processing, increase in the critical bond distance of residues Q390-T391
S463T
40% decrease in ratio kcat/KM
T391A
mutant protein without intramolecular autocatalytic processing activity
T353A
T380A
-
mutant enzyme can not process even after 30 days at 37 °C, no enzymatic activity
T380S
-
mutant enzyme is strongly impaired with respect to processing. Prolonged incubation (more than 30 days) at 37°C leads to complete maturation of the T380S mutant. Vmax for hydrolysis of 5-L-glutamyl-4-nitroanilide is 8.8fold lower than wild-type enzyme. Vmax for transpeptidation of 5-L-glutamyl-4-nitroanilide of Gly-Gly
H383A
-
site-directed mutagenesis of conserved His383 residue, 3fold reduced activity and 62% reduced Vmax, altered binding of acceptor
H383A/H505A
-
site-directed mutagenesis, 37fold reduced activity
H505A
-
site-directed mutagenesis, 10fold reduced activity
K562S
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type: the mutant's affinity towards Gly-Gly dramatically decreases to 2.0% of wild-type level, whereas it retains 45% of wild-type hydrolytic activity
K568S
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
N120Q
the mutant exhibits a Km value for the transpeptidation reaction that is not significantly different from that of wild type enzyme. The mutation results in a decreased maximal rate of 5-L-glutamyl-4-nitroanilide turnover
N230Q
the mutant exhibits a Km value for the transpeptidation reaction that is not significantly different from that of wild type enzyme. The mutation results in a decreased maximal rate of 5-L-glutamyl-4-nitroanilide turnover
N266Q
the mutant exhibits a Km value for the transpeptidation reaction that is not significantly different from that of wild type enzyme. The mutation results in a decreased maximal rate of 5-L-glutamyl-4-nitroanilide turnover
N297Q
the mutant exhibits a Km value for the transpeptidation reaction that is not significantly different from that of wild type enzyme. The mutation results in a slightly decreased maximal rate of 5-L-glutamyl-4-nitroanilide turnover
N344Q
the mutant exhibits a Km value for the transpeptidation reaction that is not significantly different from that of wild type enzyme. The mutation results in a decreased maximal rate of 5-L-glutamyl-4-nitroanilide turnover
N511Q
the mutant exhibits a Km value for the transpeptidation reaction that is not significantly different from that of wild type enzyme. The mutation results in a decreased maximal rate of 5-L-glutamyl-4-nitroanilide turnover
N95Q
the mutation results in an 8fold decrease in the cleavage efficiency of the propeptide
N95Q/N120Q/N230Q/N266Q/N297Q/N344Q/N511Q
total N-glycosylation knock-out mutant
V272A
structure analysis
H369N
mutation introduces significant transpeptidase activity. Mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate
R346A
mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate
R346E
mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate
Y327E
mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate
Y327N
mutation introduces significant transpeptidase activity. Mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate. The mutant enzyme retains more than 90% transpeptidase activity in the presence of Ba2+, Ca2+, Cu2+, Mg2+, Mn2+, and Zn2+ and is completely inhibited by Cd2+, Co2+, Fe2+, Hg2+, Ni2+ and Pb2+
Y349D
mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate
H369N
-
mutation introduces significant transpeptidase activity. Mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate
-
R346A
-
mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate
-
R346E
-
mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate
-
Y327E
-
mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate
-
Y327N
-
mutation introduces significant transpeptidase activity. Mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate. The mutant enzyme retains more than 90% transpeptidase activity in the presence of Ba2+, Ca2+, Cu2+, Mg2+, Mn2+, and Zn2+ and is completely inhibited by Cd2+, Co2+, Fe2+, Hg2+, Ni2+ and Pb2+
-
F417Y
site-directed mutagenesis, the mutant shows decreased hydrolysis and increased transfer activity, i.e. gamma-glutamyl-p-nitroanilide hydrolysis and gamma-L-glutamylhydroxamate synthesis, compared to wild-type
W385T
site-directed mutagenesis, the mutant shows decreased hydrolysis and increased transfer activity, i.e. gamma-glutamyl-p-nitroanilide hydrolysis and gamma-L-glutamylhydroxamate synthesis, compared to wild-type
W525A
site-directed mutagenesis, the mutant shows decreased hydrolysis and increased transfer activity, i.e. gamma-glutamyl-p-nitroanilide hydrolysis and gamma-L-glutamylhydroxamate synthesis, compared to wild-type
F417Y
-
site-directed mutagenesis, the mutant shows decreased hydrolysis and increased transfer activity, i.e. gamma-glutamyl-p-nitroanilide hydrolysis and gamma-L-glutamylhydroxamate synthesis, compared to wild-type
-
W385T
-
site-directed mutagenesis, the mutant shows decreased hydrolysis and increased transfer activity, i.e. gamma-glutamyl-p-nitroanilide hydrolysis and gamma-L-glutamylhydroxamate synthesis, compared to wild-type
-
W525A
-
site-directed mutagenesis, the mutant shows decreased hydrolysis and increased transfer activity, i.e. gamma-glutamyl-p-nitroanilide hydrolysis and gamma-L-glutamylhydroxamate synthesis, compared to wild-type
-
additional information