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EC Tree
IUBMB Comments The animal enzyme also acts on beta-citryl-L-glutamate and beta-citryl-L-glutamine.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
fgase, beta-cghe, formylglutamate hydrolase, formylglutamate amidohydrolase, beta-citryl-l-glutamate-hydrolysing enzyme,
more
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amidase, beta-citrylglutamate
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beta-citryl-L-glutamate amidase
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beta-citryl-L-glutamate amidohydrolase
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beta-citryl-L-glutamate hydrolase
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beta-citryl-L-glutamate-hydrolysing enzyme
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beta-citryl-L-glutamate-hydrolyzing enzyme
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beta-citrylglutamate amidase
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beta-citrylglutamate amidohydrolase
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citrylglutamate amidohydrolase
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citrylglutamate-hydrolysing enzyme
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deformylase, formylglutamate
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formylglutamate amidohydrolase
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formylglutamate deformylase
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formylglutamate hydrolase
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hydrolase, N-formylglutamate
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N-formylglutamate hydrolase
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N-formyl-L-glutamate + H2O = formate + L-glutamate
N-formyl-L-glutamate + H2O = formate + L-glutamate
regulation, induction and catabolite repression of formylglutamate amidohydrolase
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N-formyl-L-glutamate + H2O = formate + L-glutamate
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hydrolysis of linear amides
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N-formyl-L-glutamate amidohydrolase
The animal enzyme also acts on beta-citryl-L-glutamate and beta-citryl-L-glutamine.
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beta-citryl-L-glutamate + H2O
citrate + L-glutamate
beta-citryl-L-glutamine + H2O
citrate + L-glutamine
N-acetyl-alpha-L-aspartylglutamate + H2O
acetate + alpha-L-aspartylglutamate
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poor substrate
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?
N-acetyl-L-aspartate + H2O
acetate + L-aspartate
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poor substrate
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?
N-acetyl-L-methionine + H2O
acetate + L-methionine
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poor substrate
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?
N-formyl-L-glutamate + H2O
formate + L-glutamate
additional information
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beta-citryl-L-glutamate + H2O
citrate + L-glutamate
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at about 30% the rate of formylglutamate hydrolysis
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ir
beta-citryl-L-glutamate + H2O
citrate + L-glutamate
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deacylation of beta-citryl-L-glutamate
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ir
beta-citryl-L-glutamate + H2O
citrate + L-glutamate
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deacylation of beta-citryl-L-glutamate
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ir
beta-citryl-L-glutamate + H2O
citrate + L-glutamate
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best substrate, high substrate specificity for beta-citryl-L-glutamate
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ir
beta-citryl-L-glutamate + H2O
citrate + L-glutamate
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at about 30% the rate of formylglutamate hydrolysis
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ir
beta-citryl-L-glutamine + H2O
citrate + L-glutamine
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at about 1/30 of that for beta-citryl-L-glutamate
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ir
beta-citryl-L-glutamine + H2O
citrate + L-glutamine
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at about 13% the rate of formylglutamate hydrolysis
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ir
N-formyl-L-glutamate + H2O
formate + L-glutamate
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terminal reaction in the five-step pathway for histidine utilization
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?
N-formyl-L-glutamate + H2O
formate + L-glutamate
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terminal reaction in the five-step pathway for histidine utilization
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N-formyl-L-glutamate + H2O
formate + L-glutamate
Pseudomonas spp.
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terminal reaction in the five-step pathway for histidine utilization
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N-formyl-L-glutamate + H2O
formate + L-glutamate
Pseudomonas spp.
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terminal reaction in the five-step pathway for histidine utilization
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?
N-formyl-L-glutamate + H2O
formate + L-glutamate
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poor substrate
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?
N-formyl-L-glutamate + H2O
formate + L-glutamate
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best substrate
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N-formyl-L-glutamate + H2O
formate + L-glutamate
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best substrate
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N-formyl-L-glutamate + H2O
formate + L-glutamate
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poor substrate
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additional information
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substrate specificity
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additional information
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little or no activity with N-acetyl-L-glutamate
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additional information
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substrate specificity
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additional information
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substrate specificity
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additional information
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little or no activity with N-formyl-L-aspartate, N-formyl-L-glutamine, N-acetyl-L-glutamate, alpha-citryl-L-glutamate, alpha- and beta-citryl-alpha-L-glutamylglutamate
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?
additional information
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little or no activity with N-formyl-L-aspartate, N-formyl-L-glutamine, N-acetyl-L-glutamate, alpha-citryl-L-glutamate, alpha- and beta-citryl-alpha-L-glutamylglutamate
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?
additional information
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no activity with N-acetyl-alpha-aspartylglutamate
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additional information
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little or no activity with N-acetyl-L-glutamate
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additional information
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little or no activity with N-acetyl-L-glutamate
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additional information
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substrate specificity
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additional information
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little or no activity with N-formyl-L-aspartate, N-formyl-L-glutamine, N-acetyl-L-glutamate, alpha-citryl-L-glutamate, alpha- and beta-citryl-alpha-L-glutamylglutamate
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additional information
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little or no activity with N-acetyl-L-glutamate
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additional information
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substrate specificity
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additional information
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little or no activity with N-formyl-L-aspartate, N-formyl-L-glutamine, N-acetyl-L-glutamate, alpha-citryl-L-glutamate, alpha- and beta-citryl-alpha-L-glutamylglutamate
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additional information
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no activity with N-acetyl-alpha-aspartylglutamate
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additional information
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little or no activity with N-acetyl-L-glutamate
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N-formyl-L-glutamate + H2O
formate + L-glutamate
N-formyl-L-glutamate + H2O
formate + L-glutamate
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terminal reaction in the five-step pathway for histidine utilization
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?
N-formyl-L-glutamate + H2O
formate + L-glutamate
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terminal reaction in the five-step pathway for histidine utilization
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N-formyl-L-glutamate + H2O
formate + L-glutamate
Pseudomonas spp.
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terminal reaction in the five-step pathway for histidine utilization
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?
N-formyl-L-glutamate + H2O
formate + L-glutamate
Pseudomonas spp.
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terminal reaction in the five-step pathway for histidine utilization
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?
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CaCl2
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5 mM: high activation
Co2+
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activation, most effective, 0.8 mM: 4fold activation
MnCl2
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5 mM: most effective activation
Ca2+
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no activation
Ca2+
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required for full activity, can replace Mn2+ to some extent
Divalent metal ions
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activation
Divalent metal ions
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required
Fe2+
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activation below 0.1 mM, slight inhibition above 0.1 mM
Mg2+
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no activation
Mg2+
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required for full activity, can replace Mn2+ to some extent
Mn2+
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no activation
Mn2+
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required for full activity
Mn2+
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maximal activity at 0.5-1 mM
additional information
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no activation by Cd2+
additional information
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no activation by Ni2+, Zn2+
additional information
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enzyme is a metalloenzyme
additional information
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no activation by Ni2+, Zn2+
additional information
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no activation by Cu2+
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adenine
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1 mM: about 30% inhibition
ADP
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0.1 mM: about 30% inhibition, 1 mM: about 90% inhibition
dithiothreitol
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5 mM: very slight inhibition
Fe2+
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slight inhibition above 0.1 mM, activation below 0.1 mM
FeCl3
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5 mM: strong inhibition
GDP
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1 mM: about 62% inhibition
guanine
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0.1 mM: about 11% inhibition, 1 mM: about 4% inhibition
L-Quisqualate
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0.1 mM: 80% inhibition, 1 mM: 96% inhibition; non-competitive potent inhibitor
N-acetyl-L-glutamate
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kinetics, competitive inhibition, Ki: 6 mM
N-acetyl-L-glutamine
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slight inhibition
N-formyl-L-aspartate
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kinetics, competitive inhibition, Ki: 9 mM
nucleotides
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strong inhibition
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S-adenosyl-L-methionine
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0.1 mM: about 6% inhibition, 1 mM: about 30% inhibition
AMP
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1 mM: about 30% inhibition
AMP
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no or slight inhibition
ATP
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0.1 mM: about 40% inhibition, 1 mM: about 95% inhibition; strong competitive inhibition
ATP
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0.1 mM: 78% inhibition, 1 mM: 97% inhibition; strong competitive inhibition
citrate
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0.1 mM: about 30% inhibition, 1 mM: 90% inhibition; inhibitory activity almost completely counteracted by 6 mM of Mn2+: inhibitory effect attributable to chelation of Mn2+
citrate
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0.1 mM: 77% inhibition, 1 mM: 98% inhibition
EDTA
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EDTA
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inhibition completely reversed by Mn2+, activity 30% restored by Ca2+ and 13% restored by Mg2+
glutamate
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1 mM: about 12% inhibition
glutamate
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0.1 mM: 34% inhibition, 1 mM: 81% inhibition
GMP
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0.1 mM: about 16% inhibition, 1 mM: about 83% inhibition
GMP
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no or slight inhibition
GTP
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0.1 mM: about 66% inhibition, 1 mM: about 98% inhibition; strong competitive inhibition
GTP
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0.1 mM: 90% inhibition, 1 mM: 99% inhibition; strong competitive inhibition
phosphate
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1 mM: slight inhibition; activity completely suppressed in phosphate buffer
additional information
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no or very slight inhibition by adenosine, guanosine, cAMP, cGMP, S-adenosyl-L-homocysteine
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additional information
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no or very slight inhibition by kinate, N-methyl-D-aspartate
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histidine
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induction and activation
Lubrol Px
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enzyme solubilized, activation
N-formyl-L-glutamate
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induction and activation
Triton X-100
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enzyme solubilized, activation
Urocanate
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induction and activation
additional information
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sulfhydryl reagent not required
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0.0025 - 0.0088
beta-Citryl-L-glutamate
14
N-formyl-L-glutamate
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0.0025
beta-Citryl-L-glutamate
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0.0088
beta-Citryl-L-glutamate
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6
N-acetyl-L-glutamate
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kinetics, competitive inhibition
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N-formyl-L-aspartate
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kinetics, competitive inhibition
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100
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in the presence of 5 mM substrate, N-formyl-L-glutamate, and 0.8 mM CoCl2, 30°C
380
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calculated specific activity, with saturating substrate
additional information
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6.5 - 7
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in the presence of Mn2+
7 - 8
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maximally active at
additional information
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pI of about pH 4.3
7.5
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assay at
7.5
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100 mM potassium phosphate buffer
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6.6 - 8.5
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more than 65% of maximal activity between pH 6.6 and 8.5
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Wistar
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brenda
Wistar
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brenda
ATCC 12633
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brenda
wild-type strain PRS1, ATCC 12633 and several mutants
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brenda
Pseudomonas spp.
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brenda
Pseudomonas spp.
present in all species of Pseudomonas studied
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brenda
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low activity
brenda
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moderate activity
brenda
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high activity, about 40% of the level in testis
brenda
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low activity
brenda
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low activity
brenda
additional information
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tissue distribution, highest activity in testes and lung
brenda
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moderate activity
brenda
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moderate activity
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brenda
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moderate activity
brenda
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moderate activity
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brenda
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very low activity
brenda
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very low activity
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brenda
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low activity
brenda
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low activity
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brenda
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very low activity
brenda
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very low activity
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brenda
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brenda
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highest activity
brenda
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brenda
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present in soluble fractions
brenda
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localized in particulate fractions
brenda
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localized in particulate fractions
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brenda
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about 28% of total enzyme activity located in microsomal fractions
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brenda
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about 28% of total enzyme activity located in microsomal fractions
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brenda
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about 70% of total enzyme activity located in mitochondrial fractions
brenda
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about 70% of total enzyme activity located in mitochondrial fractions
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brenda
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350000
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PAGE, after digestion with N-glycosidase F
420000
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PAGE, before digestion with N-glycosidase F
50000
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1 * 50000, SDS-PAGE
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monomer
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1 * 50000, SDS-PAGE
multimer
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composed of 90000, 100000, 115000 and 130000 Da subunits, SDS-PAGE
multimer
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composed of 90000, 100000, 115000 and 130000 Da subunits, SDS-PAGE
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glycoprotein
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100
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boiling, 2 min: 100% loss of activity
50
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2 min: 5% loss of activity, 5 min: 10% loss of activity
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from recombinant Escherichia coli strain RDP145, pLH4
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solubilized by 0.5% Lubrol PX, most effective detergent
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expression in Escherichia coli RDP210
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hutG , formylglutamate amidohydrolase gene, subcloned on a multicopy plasmid in Escherichia coli
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hutG, formylglutamate amidohydrolase gene, expressed in Escherichia coli RDP145
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Consevage, M.W.; Porter, R.D.; Phillips, A.T.
Cloning and expression in Escherichia coli of histidine utilization genes from Pseudomonas putida
J. Bacteriol.
162
138-146
1985
Pseudomonas putida, Pseudomonas spp.
brenda
Miyake, M; Innami, T; Kakimoto, Y.
A beta-citryl-L-glutamate-hydrolysing enzyme in rat testes
Biochim. Biophys. Acta
760
206-214
1983
Rattus norvegicus, Rattus norvegicus Wistar
brenda
Asakura, M; Nagahashi, Y.; Hamada, M.; Kawai, M.; Kadobayashi, K.; Narahara, M.; Nakagawa, S.; Kawai, Y.; Hama, T.; Miyake, M.
Purification and properties of beta-citryl-L-glutamate-hydrolysing enzyme from rat testis particulate
Biochim. Biophys. Acta
1250
35-42
1995
Rattus norvegicus, Rattus norvegicus Wistar
brenda
Hu, L.; Mulfinger, L.M.; Phillips, A.T.
Purification and properties of formylglutamate amidohydrolase from Pseudomonas putida
J. Bacteriol.
169
4696-4702
1987
Pseudomonas putida, Pseudomonas spp.
brenda
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