Information on EC 2.1.2.5 - glutamate formimidoyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
2.1.2.5
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RECOMMENDED NAME
GeneOntology No.
glutamate formimidoyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5-formimidoyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formimidoyl-L-glutamate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
formimino group transfer
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Histidine metabolism
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L-histidine degradation III
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Metabolic pathways
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One carbon pool by folate
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histidine metabolism
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SYSTEMATIC NAME
IUBMB Comments
5-formimidoyltetrahydrofolate:L-glutamate N-formimidoyltransferase
A pyridoxal-phosphate protein. Also catalyses formyl transfer from 5-formyltetrahydrofolate to L-glutamate (a reaction formerly listed as EC 2.1.2.6). In eukaryotes, it occurs as a bifunctional enzyme that also has formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4) activity.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-83-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
chicken, several isoforms of p60, bifunctional formiminotransferase cyclodeaminase
Uniprot
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
no activity in Herpetosiphon aurantiacus
the gene encoding glycine formimidoyltransferase is an inactive pseudogene, the histidine utilization hut operon in Herpetosiphon aurantiacus is entirely broken up, suggesting that this pathway no longer functions
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-formimidoyltetrahydrofolate + L-glutamate
tetrahydrofolate + N-formimidoyl-L-glutamate
show the reaction diagram
5-formyltetrahydrofolate + L-glutamate
N-formyl-L-glutamate + tetrahydrofolate
show the reaction diagram
N-formimidoyl-L-Glu-L-Glu-L-Glu + tetrahydrofolate
N-formimidoyl-L-Glu-L-Glu + 5-formimidoyltetrahydrofolate
show the reaction diagram
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
show the reaction diagram
tetrahydrofolate + N-formimidoyl-L-glutamate
5-formimidoyltetrahydrofolate + L-glutamate
show the reaction diagram
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
show the reaction diagram
tetrahydropteroic acid + N-formimino-L-glutamate
5-formiminotetrahydropteroic acid + L-glutamate
show the reaction diagram
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tetrahydropteroic acid is a good alternate substrate
-
?
tetrahydropteroylpentaglutamate + N-formimino-L-glutamate
5-formiminotetrahydropteroylpentaglutamate + L-glutamate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5-formimidoyltetrahydrofolate + L-glutamate
tetrahydrofolate + N-formimidoyl-L-glutamate
show the reaction diagram
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
show the reaction diagram
tetrahydrofolate + N-formimidoyl-L-glutamate
5-formimidoyltetrahydrofolate + L-glutamate
show the reaction diagram
O05954
FTCD in the centrosome may be associated with polyglutamylated residues of centriole microtubules and may play a role in providing centrioles with glutamate produced by cyclodeaminase domains of FTCD
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
tetrahydrofolate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
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weak stimulation by low concentrations
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetate
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inhibition in decreasing order: fumarate, succinate, citrate, acetate
acetyl-L-glutamate
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0.015 mM, 30% inhibition
aminopterin
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0.0005 mM, 53% inhibition
arsenate
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weak
barium acetate
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0.1 M, 90% inhibition
Ca2+
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0.1 M, strong inhibition in decreasing order: La3+, Ca2+, Mg2+, Li+, Na+, K+
CaCl2
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0.1 M, 72% inhibition
citrate
D-glutamate
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0.015 mM, 47% inhibition
folic acid
formyl-L-glutamate
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0.015 mM, 53% inhibition
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fumarate
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inhibition in decreasing order: fumarate, succinate, citrate, acetate
imidazole
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K+
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0.1 M, strong inhibition in decreasing order: La3+, Ca2+, Mg2+, Li+, Na+, K+
K2SO4
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0.1 M, 30% inhibition
KNO3
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0.1 M, 65% inhibition
L-aspartate
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0.015 mM, 26% inhibition
L-glutamate
La3+
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0.1 M, strong inhibition in decreasing order: La3+, Ca2+, Mg2+, Li+, Na+, K+
Li+
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0.1 M, strong inhibition in decreasing order: La3+, Ca2+, Mg2+, Li+, Na+, K+
Maleate
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methotrexate
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0.0005 mM: 33% inhibition, 0.001 mM: 83% inhibition
Mg2+
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0.1 M, strong inhibition in decreasing order: La3+, Ca2+, Mg2+, Li+, Na+, K+
MnCl2
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0.1 M: 98% inhibition, 0.01 M: 65% inhibition
N-formiminoaspartate
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Na+
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0.1 M, strong inhibition in decreasing order: La3+, Ca2+, Mg2+, Li+, Na+, K+
NH4Cl
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high concentrations
p-acetylaminobenzoylglutamate
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0.3 mM, 50% inhibition
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p-Aminobenzoylglutamate
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2.5 mM, 50% inhibition
p-formylaminobenzoylglutamate
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0.3 mM, 50% inhibition
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p-iodobenzoylglutamate
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1.5 mM, 50% inhibition
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phosphate
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weak
proteinase K
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degradation of bifunctional formiminotransferase cyclodeaminase
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succinate
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inhibition in decreasing order: fumarate, succinate, citrate, acetate
Tris
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ZnCl2
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0.01 M, 99% inhibition
additional information
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not inhibited by formamidinoacetic acid, gamma-benzyl-formamidinoglutaric acid, formic acid, formamide, formylglutamine, formylisoglutamine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.111 - 0.148
(6R,S)-tetrahydrofolate
0.0017 - 0.075
(6S)-tetrahydropteroylpentaglutamate
0.0004 - 0.0054
5-formimidoyltetrahydrofolate
0.034 - 1.03
L-glutamate
0.0007 - 0.0058
N-formimidoyl-L-Glu-L-Glu-L-Glu
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2 - 12
N-formimino-L-glutamate
0.1
tetrahydrofolate
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2.5
tetrahydropteroic acid
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0022 - 0.0193
5-formimidoyltetrahydrofolate
0.0022 - 0.0193
L-glutamate
additional information
additional information
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
60
citrate
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0.1
folic acid
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10
formiminoaspartate
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6
imidazole
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0.9
L-glutamate
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30
Maleate
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4
Tris
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39 - 41
recombinant enzyme, expressed in Escherichia coli
43 - 45
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additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.6
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phosphate buffer
6.5 - 9
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unbuffered solution
7 - 8
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additional information
pI: 6.13
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9.8
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about 50% of activity maximum at pH 6 and 9.8
6.2 - 9
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about 50% of activity maximum at pH 6.2 and 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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assay at
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
DU249 chicken hepatoma cells, contain p60 but no measurable formiminotransferase activity, may be due to the low expression of p60
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
more abundantly around the mother centriole. The centrosome localization of FTCD continues throughout the cell cycle and is not disrupted after Golgi fragmentation, which is induced by colcemid and brefeldin A. FTCD in the centrosome may be associated with polyglutamylated residues of centriole microtubules and may play a role in providing centrioles with glutamate produced by cyclodeaminase domains of FTCD
Manually annotated by BRENDA team
localized on Golgi membranes as well as on some potentially Golgi complex-derived vesicular structures
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Manually annotated by BRENDA team
additional information
no interaction of enzyme with liver-specific cytoskeleton proteins
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
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2 * 37000, recombinant His-tagged N-terminal formiminotransferase domain of bifunctional formiminotransferase cyclodeaminase, calculated from the amino acid sequence
58000
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2 * 58000, bifunctional formiminotransferase cyclodeaminase exists as dimeric, tetrameric and octameric complexes, SDS-PAGE, a single 35 kDa protein is cross-linked to each dimer, it may play a role in the association of the protein to the Golgi membrane, functional formiminotransferase activity unit of FTCD is a dimer with binding sites for glutamate and folate; 4 * 58000, bifunctional formiminotransferase cyclodeaminase exists as dimeric, tetrameric and octameric complexes, SDS-PAGE; 8 * 58000, bifunctional formiminotransferase cyclodeaminase exists as dimeric, tetrameric and octameric complexes, SDS-PAGE
58926
8 * 58926, recombinant bifunctional enzyme with formiminotransferase and cyclodeaminase activity, EC 2.1.2.5 and EC 4.3.1.4, calculated from cDNA sequence
59100
x * 59100, calculated from the amino acid sequence
62000
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8 * 62000, bifunctional formiminotransferase cyclodeaminase, arranged as a circular tetramer of dimers
83000
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recombinant His-tagged N-terminal formiminotransferase domain of bifunctional formiminotransferase cyclodeaminase, gel filtration
380000
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recombinant His-tagged bifunctional formiminotransferase cyclodeaminase, gel filtration
438000
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wild-type bifunctional formiminotransferase cyclodeaminase, gel filtration
480000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 59100, calculated from the amino acid sequence
homodimer
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N-terminal formiminotransferase domain of bifunctional formiminotransferase cyclodeaminase, dimer interface is important for the function of the domain
homooctamer
octamer
tetramer
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4 * 58000, bifunctional formiminotransferase cyclodeaminase exists as dimeric, tetrameric and octameric complexes, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
p60, bifunctional formiminotransferase cyclodeaminase, is post-translationally modified
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
arrangement of subunits like a square doughnut, coupling of three subunits governs the octamer-dependent sequential enzyme activities
crystal structure of the monofunctional formiminotransferase domain of FTCD, hanging-drop method
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dimeric, tetrameric and octameric complexes are resistant to proteolysis
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formiminoglutamate prevents inactivation of enzyme
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no loss of activity after dialysis against phosphate buffer or 0.05 M EDTA, pH 7.4
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, crude extract, 1 year, stable
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-20C, several weeks, stable
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-80C, purified desalted recombinant enzyme, 100 mM K-phosphate, pH 7.3, 10% v/v glycerol, flash frozen in liquid N2, loss of 80% activity after 8 weeks
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-80C, purified desalted recombinant enzyme, 100 mM K-phosphate, pH 7.3, 10% v/v glycerol, flash frozen in liquid N2, stable for at least 8 weeks
2C, 2 months, 16-45% loss of activity
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2C, several weeks, stable
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
60-80fold purification
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700fold purification
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purification from liver
purification of recombinant bifunctional enzyme with formiminotransferase and cyclodeaminase activity, EC 2.1.2.5 and EC 4.3.1.4, expressed in Escherichia coli
purification of recombinant hexahistidine-tagged formiminotransferase domain of FTCD
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purification of twin enzyme EC 2.1.2.5 and formiminotetrahydrofolate cyclodeaminase EC 4.3.1.4, combination of affinity chromatography and isoelectric focusing
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purification of wild type bifunctional formiminotransferase cyclodeaminase, 150fold purification of His-tagged recombinant enzyme, 60fold purification of His-tagged transferase domain, expressed in Escherichia coli BL21/DE3
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recombinant enzyme from Escherichia coli strain BL21-CodonPlus (DE3)-RIPL by affinity chormatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA encoding formiminotransferase cyclodeaminase is cloned and sequenced
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cDNA encoding formiminotransferase cyclodeaminase is cloned, characterized and partially sequenced
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cloning and sequencing of the cDNA coding for p60, the chicken homologue of bifunctional formiminotransferase cyclodeaminase, a protein of 541 amino acids; expressed in HeLa cells
expression of full-length formiminotransferase cyclodeaminase and of isolated N-terminal transferase and C-terminal deaminase domains in Escherichia coli BL21/DE3 as His-tagged proteins
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glutamate formiminotransferase, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus (DE3)-RIPL, functional complementation of an Escherichia coli DELTAygfA 5-CHO-THF cycloligase deletion mutant with strain MG1655 background
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glutamate formiminotransferase, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus (DE3)-RIPL, functional complementation of an Escherichia coli DELTAygfA 5-formimidoyltetrahydrofolate cycloligase deletion mutant with strain MG1655 background
glutamate formiminotransferase, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus (DE3)-RIPL, functional complementation of an Escherichia coli DELTAygfA 5-N-formimidoyltetrahydrofolate cycloligase deletion mutant with strain MG1655 background
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isolation and sequencing of cDNA clones encoding bifunctional enzyme with formiminotransferase and cyclodeaminase activity, EC 2.1.2.5 and EC 4.3.1.4, cDNA encodes an amino acid sequence of 541 residues, expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R135C
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mutation naturally occuring in patient with mild form of putative glutamate formiminotransferase deficiency
R299P
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mutation naturally occuring in patient with mild form of putative glutamate formiminotransferase deficiency
R135C
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mutation analogous to mutant found in patient with glutamate formiminotransferase deficiency, reduction of enzyme activity to 61% of wild-type
R299P
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mutation analogous to mutant found in patient with glutamate formiminotransferase deficiency, reduction of enzyme activity to 57% of wild-type
additional information
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deletion mutants of formiminotransferase cyclodeaminase with transferase activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
subcellular localization of protein may influence production of autoantibodies and their role in the pathogenesis of type 2 autoimmune hepatitis
molecular biology
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bifunctional formiminotransferase cyclodeaminase provides a novel marker to study ER-Golgi dynamics
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