Information on EC 6.3.4.3 - formate-tetrahydrofolate ligase

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

EC NUMBER
COMMENTARY hide
6.3.4.3
-
RECOMMENDED NAME
GeneOntology No.
formate-tetrahydrofolate ligase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
formylation
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Carbon fixation pathways in prokaryotes
-
-
folate polyglutamylation
folate transformations I
-
-
folate transformations II
-
-
formate assimilation into 5,10-methylenetetrahydrofolate
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
One carbon pool by folate
-
-
reductive acetyl coenzyme A pathway
-
-
reductive acetyl coenzyme A pathway I (homoacetogenic bacteria)
-
-
SYSTEMATIC NAME
IUBMB Comments
formate:tetrahydrofolate ligase (ADP-forming)
In eukaryotes occurs as a trifunctional enzyme also having methylenetetrahydrofolate dehydrogenase (NADP+) (EC 1.5.1.5) and methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) activity.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-66-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
W168
-
-
Manually annotated by BRENDA team
W168
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
Clostridium acidi-urici
Clostridium acidi-urici 9a
9a
-
-
Manually annotated by BRENDA team
fragment; isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
-
-
Manually annotated by BRENDA team
19433
-
-
Manually annotated by BRENDA team
19433
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
Eubacterium sp. VPI 12708
strain VPI 12708
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
-
-
Manually annotated by BRENDA team
Mesorhizobium sp.
isolated from environmental samples collected from different sites in Wux, China, gene fths
-
-
Manually annotated by BRENDA team
Mesorhizobium sp. BNC1
isolated from environmental samples collected from different sites in Wux, China, gene fths
-
-
Manually annotated by BRENDA team
strain AM1
SwissProt
Manually annotated by BRENDA team
4698
-
-
Manually annotated by BRENDA team
4698
-
-
Manually annotated by BRENDA team
25238, weak activity
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
trifunctional enzyme with 10-formyltetrahydrofolate synthetase, EC 6.3.4.3, 5,10-methenyltetrahydrofolate cyclohydrolase, EC 3.5.4.9, and 5,10-methylenetetrahydrofolate dehydrogenase activity, EC 1.5.1.5
-
-
Manually annotated by BRENDA team
27337
-
-
Manually annotated by BRENDA team
Pigeon
-
-
-
Manually annotated by BRENDA team
25433
-
-
Manually annotated by BRENDA team
25433
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
-
-
Manually annotated by BRENDA team
spinach
-
-
Manually annotated by BRENDA team
fragment; isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
14990
-
-
Manually annotated by BRENDA team
14990
-
-
Manually annotated by BRENDA team
trifunctional enzyme with 10-formyltetrahydrofolate synthetase, EC 6.3.4.3, 5,10-methenyltetrahydrofolate cyclohydrolase, EC 3.5.4.9, and 5,10-methylenetetrahydrofolate dehydrogenase activity, EC 1.5.1.5
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
complete loss of synthetase activity is incompatible with life. Embryos die shortly after 10.5 days gestation, and are developmentally delayed or abnormal. Female synthetase-deficient mice have decreased neutrophil counts during pregnancy and increased incidence of developmental defects in embryos. Synthetase deficiency may lead to pregnancy complications through decreased purine synthesis and reduced cellular proliferation
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R,S)-tetrahydrofolate + ATP + formate
?
show the reaction diagram
-
-
-
-
r
ADP + carbamoylphosphate + tetrahydrofolate
ATP + ?
show the reaction diagram
-
-
-
?
ADP + phosphate + 10-formyltetrahydrofolate
?
show the reaction diagram
ATP + (6R,S)-tetrahydrofolate pteroylpentaglutamate
ADP + phosphate + 10-formyltetrahydrofolate pteroylpentaglutamate
show the reaction diagram
-
-
-
-
?
ATP + (6R,S)-tetrahydrofolate pteroyltriglutamate
ADP + phosphate + 10-formyltetrahydrofolate pteroyltriglutamate
show the reaction diagram
-
-
-
-
?
ATP + formate
ADP + HCOOPO32-
show the reaction diagram
ATP + formate + (6R,S)-tetrahydrofolate monoglutamate
ADP + phosphate + 10-formyltetrahydrofolate monoglutamate
show the reaction diagram
-
-
-
-
?
ATP + formate + tetrahydrofolate
?
show the reaction diagram
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
ATP + formate + tetrahydropteroyl-(Glu)n
ADP + phosphate + 10-formyltetrahydropteroyl-(Glu)n
show the reaction diagram
Carbamoyl phosphate + ADP
? + ATP
show the reaction diagram
dATP + formate + tetrahydrofolate
dADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
37% of the activity relative to ATP
-
-
-
formate + ATP + tetrahydrofolate
10-formyltetrahydrofolate + ADP + phosphate
show the reaction diagram
-
synthetase activity of MTHFD1
-
-
-
tetrahydrofolate + formate + ATP
10-formyltetrahydrofolate + ADP + phosphate
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
ADP + phosphate + 10-formyltetrahydrofolate
?
show the reaction diagram
ATP + formate + tetrahydrofolate
?
show the reaction diagram
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
formate + ATP + tetrahydrofolate
10-formyltetrahydrofolate + ADP + phosphate
show the reaction diagram
-
synthetase activity of MTHFD1
-
-
-
tetrahydrofolate + formate + ATP
10-formyltetrahydrofolate + ADP + phosphate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Divalent metal ion
Li+
-
specific monovalent cations required for maximal activity, order of effectiveness: NH4+, Tl+, Rb+ ~ K+, Cs+, Na+ ~ Li+
Monovalent cations
Tl+
-
specific monovalent cations required for maximal activity, order of effectiveness: NH4+, Tl+, Rb+ ~ K+, Cs+, Na+ ~ Li+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2S)-2-[[4-[(6aR)-3-amino-1,9-dioxo-5,6,6a,7-tetrahydro-4H-imidazol[3,4-f]pteridin-8-yl]benzoyl]amino]pentanedioate
-
5,10-formyltetrahydrofolate substrate analogue inhibits dehydrogenase activity
2,2'-dipyridyl disulfide
-
-
2,4-diamino-6-(3,4-dichlorophenoxy)-quinazoline
-
-
2,4-diamino-6-benzyl-5-(3-phenylpropyl)-pyrimidine
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
acetyl phosphate
-
inhibits ATP synthesis reaction from carbamoyl phosphate and ADP, and synthesis of 10-formyltetrahydrofolate
Adenylyl imidodiphosphate
-
competitive to ATP
alpha,beta-methyleneadenosine 5'-triphosphate
-
competitive to ATP
beta,gamma-methyleneadenosine 5'-triphosphate
-
competitive to ATP
Ca2+
-
in presence of Mg2+
Carbamoyl phosphate
-
-
Fluorescein mercuric acetate
-
-
formate
-
inhibits ATP synthesis reaction from carbamoyl phosphate and ADP
Formyltetrahydrofolate
-
-
Heminordihydroguaiaretic acid
methotrexate
-
-
Mn2+
-
in presence of Mg2+
nordihydroguaiaretic acid
Norisoguaiacin
p-hydroxymercuribenzoate
-
-
phosphate
Phosphonoacetate
-
inhibits ATP synthesis reaction from carbamoyl phosphate and ADP, and synthesis of 10-formyltetrahydrofolate
pteroylpentaglutamate
-
-
Tetranitromethane
-
-
Zn2+
-
in presence of Mg2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
spermine
-
stimulates activity only in absence of NH4+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
(6R,S)-tetrahydrofolate monoglutamate
-
above, recombinant enzyme, 30C
0.0036
(6R,S)-tetrahydrofolate pteroylpentaglutamate
-
recombinant enzyme, 30C
0.016
(6R,S)-tetrahydrofolate pteroyltriglutamate
-
recombinant enzyme, 30C
0.032 - 0.13
ADP
0.012 - 0.22
ATP
11.9
Carbamoyl phosphate
-
-
0.035 - 38
formate
0.056 - 0.59
MgATP2-
10
N10-formyltetrahydrofolate
-
-
0.015 - 2.3
tetrahydrofolate
0.0055 - 0.029
tetrahydropteroyl-Glu2
0.0003 - 0.025
tetrahydropteroyl-Glu3
0.0001
tetrahydropteroyl-Glu4
-
tetrahydropteroyl-Glu5
0.003
tetrahydropteroyl-Glu5
-
-
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16
(6R,S)-tetrahydrofolate monoglutamate
Homo sapiens
-
above, recombinant enzyme, 30C
2.6
(6R,S)-tetrahydrofolate pteroylpentaglutamate
Homo sapiens
-
recombinant enzyme, 30C
10
(6R,S)-tetrahydrofolate pteroyltriglutamate
Homo sapiens
-
recombinant enzyme, 30C
0.39 - 6.08
ATP
0.4 - 6.08
formate
additional information
additional information
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0338 - 0.0364
ADP
0.0296 - 0.0328
pteroylpentaglutamate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0033 - 0.0037
(2S)-2-[[4-[(6aR)-3-amino-1,9-dioxo-5,6,6a,7-tetrahydro-4H-imidazol[3,4-f]pteridin-8-yl]benzoyl]amino]pentanedioate
0.00054
2,4-diamino-6-(3,4-dichlorophenoxy)-quinazoline
Leishmania major
-
dhch1-/pXNG4-FTL mutant, FV1 line
0.00042
2,4-diamino-6-benzyl-5-(3-phenylpropyl)-pyrimidine
Leishmania major
-
dhch1-/pXNG4-FTL mutant, FV1 line
0.00004
methotrexate
Leishmania major
-
dhch1-/pXNG4-FTL mutant, FV1 line
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23
-
synthetase activity of the wild type enzyme
23.8
-
synthetase activity of the mutant R653Q
40
-
-
780
-
recombinant FTHFS
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
higher expression level
Manually annotated by BRENDA team
2fold increased expression of gene DKFZp586G1517 compared to normal colon tissue
Manually annotated by BRENDA team
low expression level
Manually annotated by BRENDA team
-
low expression
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
higher expression level
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Moorella thermoacetica (strain ATCC 39073)
Moorella thermoacetica (strain ATCC 39073)
Moorella thermoacetica (strain ATCC 39073)
Moorella thermoacetica (strain ATCC 39073)
Moorella thermoacetica (strain ATCC 39073)
Moorella thermoacetica (strain ATCC 39073)
Moorella thermoacetica (strain ATCC 39073)
Moorella thermoacetica (strain ATCC 39073)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
-
recombinant short isoform, SDS-PAGE
107000
110000
-
gel filtration
130000
-
gel filtration
143000
-
recombinant mitochondrial isozyme, gel filtration
150000
-
gel filtration
201000
-
gel filtration
226000
-
gel filtration
240000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
-
4 * 60000, X-ray crystallography
tetramer
additional information
-
a tryptic fragment that contains 10-formyltetrahydrofolate synthetase activity is a dimer, MW 66000
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals of FTHFS complexed with NH4+, K+ or Cs+ are grown by vapor diffusion from 46% saturated ammonium sulfate, 1 mM dithiothreitol and 1% polyehtylene glycol 1000 in 50 mM potassium maleate buffer, pH 7.6, crystals diffract to 3.0-3.2 A resolution
-
native protein, folate complex, ADP-formylphosphate complex, and ZD9331-formylphosphate complex, hanging drop vapor diffusion method. High salt conditions contain 38-46% (w/v) saturated ammonium sulfate, 1 mM , and dithiohtreitol, 1-3.5% (w/v) PEG 1000 or PEG 1450, in 50-75 mM KMB (pH 7.0-8.0). Low salt conditions contain 18-22% (w/v) PEG 6-8K, 0.2 M ammonium sulfate, 1 mM dithiothreitol, in 75 mM KMB pH 7.0-8.5
-
Se-Met FTHFS is crystallized by hanging-drop vapor-diffusion, crystals diffract to 2.5 A
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
-
unstable below pH 6.5 and above pH 9.0
1506
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23
-
,the large domain of the multifuncional enzyme, that contains the active site for the 10-formyltetrahydrofolate synthetase is more stable at 23C than at 0C
47
-
transition at 47C is due to the denaturation of a domain which binds MgATP2- and contains the synthetase active site
69
-
in the absence of monovalent cation
75
-
rapid denaturation
79
-
in the presence of 200 mM K+
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of monovalent cations to the dissociated enzyme causes the inactive monomers to reassociate to the active tetramer. The order of cation effectiveness is NH4+ > Tl+ > Rb+ ~ K+ > Cs+ > Na+ ~ Li+. The rate and extent of reactivation is influenced by the counter ion: sulfate and phosphate stimulate reassociation, thiocyanate, trichloroacetate, and perchlorate completly inhibit reassociation. The extent of reactivation is dependent upon protein concentration. The optimum protein concentration depends on the pH at which reactivation is performed
-
enzyme is unstable in phosphate buffers in the absence of high concentrations of salt
-
K+ or NH4+ increase stability of the large domain of the multifuncional enzyme, that contains the active site for the 10-formyltetrahydrofolate synthetase
-
photooxidation in presence of methylene blue results in a pseudo-first order loss of enzymatic activity and destruction of histidine residues
Clostridium acidi-urici
-
purified enzyme as crystalline suspension, 15% loss of activity after 1 month
-
tetramer is stabilized by 0.1 M sulfate in absence of an active monovalent cation
-
the binding of tetrahydropteroylpolyglutamate, MgATP2-, and NH4+ alters the susceptibility to digestion by chymotrypsin
-
unstable in absence of monovalent cations
-
unstable in presence of urea and guanidinium chloride
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, in presence of PMSF, minimal loss of activity after several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, Phenyl Sepharose, Source15Q, hydroxyapatite, Resource Q
by anion-exchange chromatography
-
heparin agarose column chromatography and phenyl Sepharose column chromatography
-
large-scale purification
-
recombinant enzyme is partially purified from HEK-293 cells by subcellular fractionation
recombinant FTHFS
-
recombinant FTHFS, heparin Agarose, Phenyl Sepharose
recombinant maltose-binding protein fusion mitochondrial isozyme from Escherichia coli by metal affinity chromatography and gel filtration, the MBP-tag is cleaved off by TEV protease
-
TALON cobalt metal affinity resin chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
deletion of the MIS1 gene has little effect
DNA sequence determination and analysis
expressed in CHO cells and Escherichia coli
expressed in Escherichia coli
-
expressed in Escherichia coli strain Y1
-
expression in CHO cells and Saccharomyces cerevisiae
expression in Escherichia coli
expression in Escherichia coli, localization of the interdomain region of the trifunctional enzyme by site-directed mutagenesis
-
expression of the mitochondrial isozyme as maltose-binding protein fusion protein in Escherichia coli, overexpression in yeast
-
gene DKFZp586G1517, DNA and amino acid sequence determination and analysis, overexpression of mitochondrial enzyme in HEK-293 cells, unlabeled or FLAG-tagged, stimulates cell growth
gene FTHFS, DNA and amino acid sequence determination and analysis, phylogenetic analysis, genetic clusters, overview. Cloning and expression in Escherichia coli
gene fths, DNA and amino acid sequence determination and analysis, quantitative expression analysis by real-time PCR, phylogenetic analysis, cloning and expression in Escherichia coli strain JM109
gene fths, DNA and amino acid sequence determination and analysis, quantitative expression analysis by real-time PCR, phylogenetic analysis, cloning and expression in Escherichia coli strain JM109; gene fths, DNA and amino acid sequence determination and analysis, quantitative expression analysis by real-time PCR, phylogenetic analysis, cloning and expression in Escherichia coli strain JM109
overexpression of FTL using the multicopy episomal vector pXNG4-FTL
-
the wild type and R653Q mutant pBKeDCS constructs are transformed into Escherichia coli BL21 DE3 to express the full-length protein
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H125S
-
site-directed mutant enzymes H125S, H131S, and H268S do not fold properly and/or do not associate to the active tetramer and, as a consequence are susceptible to intracellular proteolytic digestion
H131S
-
site-directed mutant enzymes H125S, H131S, and H268S do not fold properly and/or do not associate to the active tetramer and, as a consequence are susceptible to intracellular proteolytic digestion
H268S
-
site-directed mutant enzymes H125S, H131S, and H268S do not fold properly and/or do not associate to the active tetramer and, as a consequence are susceptible to intracellular proteolytic digestion
G1958A
-
the mutation is not associated with depression in postmenopausal women
E98D
-
36% of wild-type activity
E98Q
-
93% of wild-type activity, slight increase in thermal stability in the absence of monovalent cation
E98S
-
61% of wild-type activity
R97E
-
no activity
R97S
-
35% of wild-type kcat
K386E
-
the mutation completely abrogates synthetase activity
R653Q
-
the mutation reduces metabolic activity in cells by about 26%
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzymes denatured in 6 M urea and 4 M guanidinium chloride refold upon dilution of the denaturant-protein solution to give final concentrations of 0.5 M urea or 0.1 M guanidinium chloride. In presence of NH4+, but not in its absence the refolded proteins associate to produce the catalytically active tetramer. 80% of the enzymatic acitivity is recovered
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
the enzyme might be a target for colorectal cancer therapy
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