Information on EC 4.2.1.75 - uroporphyrinogen-III synthase

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

EC NUMBER
COMMENTARY
4.2.1.75
-
RECOMMENDED NAME
GeneOntology No.
uroporphyrinogen-III synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hydroxymethylbilane = uroporphyrinogen III + H2O
show the reaction diagram
-
-
-
-
hydroxymethylbilane = uroporphyrinogen III + H2O
show the reaction diagram
in the presence of hydroxymethylbilane synthase EC 4.3.1.8, enzyme forms uroporphyrinogen III from porphobilinogen, reaction mechanism, does not require acid/base catalysis, active site structure
-
hydroxymethylbilane = uroporphyrinogen III + H2O
show the reaction diagram
in the presence of hydroxymethylbilane synthase EC 4.3.1.8, enzyme forms uroporphyrinogen III from porphobilinogen, Tyr166 is essential for catalysis and/or substrate binding
-
hydroxymethylbilane = uroporphyrinogen III + H2O
show the reaction diagram
reaction mechanism via azafulvene and azofulvene intermediates, the product binds between the two domains and is held in place by a network of hydrogen bonds between the products side chain carboxylates and the proteins main chain amides. Interactions of the product A and B ring carboxylate side chains with both structural domains of U3S appear to dictate the relative orientation of the domains in the closed enzyme conformation and likely remain intact during catalysis. The product C and D rings are less constrained in the structure, consistent with the conformational changes required for the catalytic cyclization with inversion of D ring orientation. A conserved tyrosine residue is potentially positioned to facilitate loss of a hydroxyl from the substrate to initiate the catalytic reaction, overview
Q72KM1, -
hydroxymethylbilane = uroporphyrinogen III + H2O
show the reaction diagram
reaction mechanism, modelling, overview
-
hydroxymethylbilane = uroporphyrinogen III + H2O
show the reaction diagram
reaction mechanism, modeling involving Tyr168, overview
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
cyclization
-
-
elimination
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
Metabolic pathways
-
Porphyrin and chlorophyll metabolism
-
tetrapyrrole biosynthesis I (from glutamate)
-
tetrapyrrole biosynthesis II (from glycine)
-
SYSTEMATIC NAME
IUBMB Comments
hydroxymethylbilane hydro-lyase (cyclizing; uroporphyrinogen-III-forming)
In the presence of EC 2.5.1.61, hydroxymethylbilane synthase, the enzyme forms uroporphyrinogen III from porphobilinogen.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
CobA/HemD
Q50EH6
-
CobA/HemD
Lactobacillus reuteri CRL 1098
Q50EH6
-
-
Hydroxymethylbilane hydrolyase [cyclizing]
-
-
-
-
hydroxymethylbilane hydrolyase, cyclizing
-
-
Isomerase, uroporphyrinogen
-
-
-
-
Porphobilinogenase
-
-
-
-
Synthase, uroporphyrinogen III co-
-
-
-
-
U3S
Pseudomonas syringae DC3000
-
-
-
URO synthase
-
-
URO-synthase
-
-
-
-
URO-synthase
-
-
URO-synthase
-
-
URO-synthase
P51163
-
UROIIIS
-
-
-
-
UROIIIS
P10746
-
UROIIIS
Q88B90
-
Uroporphyrinogen III co-synthase
-
-
-
-
Uroporphyrinogen III cosynthase
-
-
-
-
Uroporphyrinogen III cosynthase
-
-
Uroporphyrinogen III synthase
-
-
-
-
Uroporphyrinogen III synthase
O48721
-
Uroporphyrinogen III synthase
Q1ET39
-
Uroporphyrinogen III synthase
P10746
-
Uroporphyrinogen III synthase
-
-
Uroporphyrinogen III synthase
Q50EH6
-
Uroporphyrinogen III synthase
Lactobacillus reuteri CRL 1098
Q50EH6
-
-
Uroporphyrinogen III synthase
P51163
-
Uroporphyrinogen III synthase
-
-
Uroporphyrinogen III synthase
Pseudomonas syringae DC3000
-
-
-
Uroporphyrinogen III synthase
-
-
Uroporphyrinogen III synthase
Q72KM1
-
Uroporphyrinogen III synthase
Q88B90
-
Uroporphyrinogen isomerase
-
-
-
-
Uroporphyrinogen-III cosynthase
-
-
-
-
Uroporphyrinogen-III cosynthetase
-
-
-
-
uroporphyrinogen-III-synthase
-
-
UROS
-
-
-
-
UROS
Q1ET39
-
UROS
-
-
urogen III synthase
-
-
CAS REGISTRY NUMBER
COMMENTARY
37340-55-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
uroporphyrinogen III synthase/methyltransferase gene cobA/hemD
UniProt
Manually annotated by BRENDA team
Lactobacillus reuteri CRL 1098
uroporphyrinogen III synthase/methyltransferase gene cobA/hemD
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
pv. tomato, gene pspto_0129
-
-
Manually annotated by BRENDA team
Pseudomonas syringae DC3000
pv. tomato, gene pspto_0129
-
-
Manually annotated by BRENDA team
strain HB27
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
congenital erythropoietic porphyria is a rare autosomal disease ultimately related to deleterious mutations in uroporphyrinogen III synthase. In absence or dysfunction of the enzyme, hydroxymethylbilane spontaneously degrades to the by-product uroporphyrinogen I, which cannot lead to the heme group and accumulates in the body, producing some of the symptoms observed in congenital erythropoietic porphyria patients, phenotype, structural and molecular basis, overview
metabolism
-
U3S is one of the key enzymes in the biosynthesis of tetrapyrrole compounds
metabolism
Q50EH6
S-adenosyl-L-methionine uroprophyrinogen III methyltransferase/synthase is a key bifunctional enzyme in the biosynthesis of cobalamin and other tetrapyrrols
metabolism
Lactobacillus reuteri CRL 1098
-
S-adenosyl-L-methionine uroprophyrinogen III methyltransferase/synthase is a key bifunctional enzyme in the biosynthesis of cobalamin and other tetrapyrrols
-
metabolism
Pseudomonas syringae DC3000
-
U3S is one of the key enzymes in the biosynthesis of tetrapyrrole compounds
-
physiological function
-
UROIIIS is the fourth enzyme of the biosynthetic route of the heme group and catalyzes the cyclization of the linear tetrapyrrol hydroxymethylbilane, inverting the configuration in one of the aromatic rings. It accelerates the production of uroporphyrinogen III (an energetically unfavorable chemical reaction) at the same time as it suppresses the spontaneous reaction pathway to yield uroporphyrinogen I
physiological function
-
U3S catalyzes the cyclization of the linear hydroxymethylbilane to uroporphyrinogen III. Arg219 is the key residue important for the catalytic activity of psU3S, Tyr162 is important for activity
physiological function
-
UROIIIS catalyzes the cyclization of the linear tetrapyrrole hydroxymethylbilane to produce uroporphyrin III. A Cys in position 73 is not essential for the catalytic activity of the enzyme but its mutation to Arg speeds up the process of irreversible unfolding and aggregation
physiological function
Pseudomonas syringae DC3000
-
U3S catalyzes the cyclization of the linear hydroxymethylbilane to uroporphyrinogen III. Arg219 is the key residue important for the catalytic activity of psU3S, Tyr162 is important for activity
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Hydroxymethylbilane
Uroporphyrinogen III
show the reaction diagram
-
-
-
-
Hydroxymethylbilane
Uroporphyrinogen III
show the reaction diagram
-
-
-
-
Hydroxymethylbilane
Uroporphyrinogen III
show the reaction diagram
-
-
-
-
Hydroxymethylbilane
Uroporphyrinogen III
show the reaction diagram
-
-
-
-
Hydroxymethylbilane
Uroporphyrinogen III
show the reaction diagram
-
-
-
-
Hydroxymethylbilane
Uroporphyrinogen III
show the reaction diagram
-
-
-
-
Hydroxymethylbilane
Uroporphyrinogen III
show the reaction diagram
-
-
-
-
Hydroxymethylbilane
Uroporphyrinogen III
show the reaction diagram
-
-
-
-
Hydroxymethylbilane
Uroporphyrinogen III
show the reaction diagram
-
-
-
-
Hydroxymethylbilane
Uroporphyrinogen III
show the reaction diagram
-
-
-
-
Hydroxymethylbilane
Uroporphyrinogen III
show the reaction diagram
-
-
-
-
Hydroxymethylbilane
Uroporphyrinogen III
show the reaction diagram
-
-
-
-
Hydroxymethylbilane
Uroporphyrinogen III
show the reaction diagram
-
-
-
-
Hydroxymethylbilane
Uroporphyrinogen III
show the reaction diagram
Q72KM1, -
-
-
-
?
Hydroxymethylbilane
Uroporphyrinogen III
show the reaction diagram
Q72KM1, -
-
enzyme-product structure analysis, overview
-
?
hydroxymethylbilane
uroporphyrinogen-III + H2O
show the reaction diagram
-
-
-
?
hydroxymethylbilane
uroporphyrinogen-III + H2O
show the reaction diagram
P10746
-
-
?
hydroxymethylbilane
uroporphyrinogen-III + H2O
show the reaction diagram
-
-
-
-
?
hydroxymethylbilane
uroporphyrinogen-III + H2O
show the reaction diagram
-
linear tetrapyrrole
-
?
hydroxymethylbilane
uroporphyrinogen-III + H2O
show the reaction diagram
P10746
linear tetrapyrrole, fourth step in the biosynthesis of porphyrin, essential reaction, decreased enzyme activity leads to the autosomal recessive disorder congenital erythropetic porphyria
macrocyclic uroporphyrinogen III is a precurosr for synthesis of diverse compounds, e.g. heme, siroheme, chlorophyll, F430, and vitamin B12
?
hydroxymethylbilane
uroporphyrinogen-III + H2O
show the reaction diagram
-
macrocyclic, role of the enzyme in tetrapyrrole based copound biosynthesis, overview
-
?
hydroxymethylbilane
uroporphyrinogen-III + H2O
show the reaction diagram
-
fourth enzyme in heme biosynthesis. Congenital erythropoietic porphyria is a very rare disease that is inherited as an autosomal recessive trait and results from a profound deficiency of uroporphyrinogen III cosynthase, the fourth enzyme in heme biosynthesis. The degree of severity of clinical symptoms mainly depends on the amount of residual uroporphyrinogen III cosynthase activity
-
-
?
Hydroxymethylbilane
?
show the reaction diagram
-
-
-
-
-
Hydroxymethylbilane
?
show the reaction diagram
-
-
-
-
-
Hydroxymethylbilane
?
show the reaction diagram
-
synthesis of uroporphyrinogen III, key intermediate for biosynthesis of tetrapyrrolic compounds like chlorophylls, hemes, cytochromes and vitamin B12
-
-
-
Hydroxymethylbilane
?
show the reaction diagram
-
synthesis of uroporphyrinogen III, key intermediate for biosynthesis of tetrapyrrolic compounds like chlorophylls, hemes, cytochromes and vitamin B12
-
-
-
hydroxymethylbilane
uroporphyrinogen III + H2O
show the reaction diagram
-
-
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
show the reaction diagram
-
-
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
show the reaction diagram
-
-
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
show the reaction diagram
-
-
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
show the reaction diagram
-, O48721
a step in tetrapyrrole biosynthesis, e.g. of chlorophyll, haem, sirohaem and bilins, overview
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
show the reaction diagram
-
intramolecular rearrangement of the d-pyrrole group and ring closure
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
show the reaction diagram
-
the D-ring of the hydroxymethylbilane substrate binds to the enzyme in a conformation that shields its terminal portion from reacting with ring A and prevents the formation of the biologically useless uroporphyrinogen I, reaction mechanism, overview
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
show the reaction diagram
-
the enzyme catalyzes the cyclization and D-ring isomerization of hydroxymethylbilane to uroporphyrinogen III, the cyclic tetrapyrrole and physiologic precursor of heme, chlorophyl, and corrin
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
show the reaction diagram
-
the enzyme catalyzes the inversion of one of the four heterocyclic rings present in the substrate. Reaction mechanism analysis by high-level quantum mechanical calculations on model systems of the enzyme
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
show the reaction diagram
-, O48721
uroporphyrinogen III synthase catalyses the cyclization of HMB with a concomitant inversion of the fourth ring of the porphyrin macrocycle, giving rise to uroporphyrinogen III
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
show the reaction diagram
-
enzymatic conversion of preuroporphyrinogen. The substrate must bind the enzyme in a conformation that prevents C19 from reacting with C20
-
-
?
Preuroporphyrinogen
Uroporphyrinogen III
show the reaction diagram
-
-
-
-
hydroxymethylbilane
uroporphyrinogen III + H2O
show the reaction diagram
Pseudomonas syringae DC3000
-
-
-
-
?
additional information
?
-
-, Q1ET39
uroporphyrinogen III synthase functions as heme synthesis enzyme during hematopoietic development of Danio rerio
-
-
-
additional information
?
-
-
hydroxymethylbilane synthase and uroporphyrinogen III synthase catalyze two consecutive reactions, the third and fourth step, in the heme biosynthetic pathway, generating the first linear and the first cyclic tetrapyrroles, respectively. Hydroxymethylbilane synthase, 2.5.1.61, and uroporphyrinogen III synthase may function independently and sequentially with hydroxymethylbilane as a free intermediate, heme biosynthetic pathway, overview. Hypoxia downregulates UROS mRNA expression in hepatic cells, reduction of UROS mRNA is associated with the accumulation of hypoxia-inducible factor 1alpha under normoxia. Deferoxamine, cobalt chloride, or hypoxia downregulate UROS mRNA expression in hepatic cells, reduction of UROS mRNA is associated with the accumulation of hypoxia-inducible factor 1alpha under normoxia
-
-
-
additional information
?
-
-, O48721
coupled assay method for UROS activity measurement using purified recombinant Pseudomonas aeruginosa porphobilinogen synthase and Bacillus megaterium porphobilinogen deaminase to generate hydroxymethylbilane, the substrate for UROS, enzymatically from 5-aminolaevulinic acid
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Hydroxymethylbilane
Uroporphyrinogen III
show the reaction diagram
Q72KM1, -
-
-
-
?
hydroxymethylbilane
uroporphyrinogen-III + H2O
show the reaction diagram
P10746
linear tetrapyrrole, fourth step in the biosynthesis of porphyrin, essential reaction, decreased enzyme activity leads to the autosomal recessive disorder congenital erythropetic porphyria
macrocyclic uroporphyrinogen III is a precurosr for synthesis of diverse compounds, e.g. heme, siroheme, chlorophyll, F430, and vitamin B12
?
hydroxymethylbilane
uroporphyrinogen-III + H2O
show the reaction diagram
-
macrocyclic, role of the enzyme in tetrapyrrole based copound biosynthesis, overview
-
?
hydroxymethylbilane
uroporphyrinogen-III + H2O
show the reaction diagram
-
fourth enzyme in heme biosynthesis. Congenital erythropoietic porphyria is a very rare disease that is inherited as an autosomal recessive trait and results from a profound deficiency of uroporphyrinogen III cosynthase, the fourth enzyme in heme biosynthesis. The degree of severity of clinical symptoms mainly depends on the amount of residual uroporphyrinogen III cosynthase activity
-
-
?
Hydroxymethylbilane
?
show the reaction diagram
-
-
-
-
-
Hydroxymethylbilane
?
show the reaction diagram
-
-
-
-
-
Hydroxymethylbilane
?
show the reaction diagram
-
synthesis of uroporphyrinogen III, key intermediate for biosynthesis of tetrapyrrolic compounds like chlorophylls, hemes, cytochromes and vitamin B12
-
-
-
Hydroxymethylbilane
?
show the reaction diagram
-
synthesis of uroporphyrinogen III, key intermediate for biosynthesis of tetrapyrrolic compounds like chlorophylls, hemes, cytochromes and vitamin B12
-
-
-
hydroxymethylbilane
uroporphyrinogen III + H2O
show the reaction diagram
-
-
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
show the reaction diagram
-
-
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
show the reaction diagram
-, O48721
a step in tetrapyrrole biosynthesis, e.g. of chlorophyll, haem, sirohaem and bilins, overview
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
show the reaction diagram
-
intramolecular rearrangement of the d-pyrrole group and ring closure
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
show the reaction diagram
-
the D-ring of the hydroxymethylbilane substrate binds to the enzyme in a conformation that shields its terminal portion from reacting with ring A and prevents the formation of the biologically useless uroporphyrinogen I, reaction mechanism, overview
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
show the reaction diagram
-
the enzyme catalyzes the cyclization and D-ring isomerization of hydroxymethylbilane to uroporphyrinogen III, the cyclic tetrapyrrole and physiologic precursor of heme, chlorophyl, and corrin
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
show the reaction diagram
Pseudomonas syringae DC3000
-
-
-
-
?
additional information
?
-
-, Q1ET39
uroporphyrinogen III synthase functions as heme synthesis enzyme during hematopoietic development of Danio rerio
-
-
-
additional information
?
-
-
hydroxymethylbilane synthase and uroporphyrinogen III synthase catalyze two consecutive reactions, the third and fourth step, in the heme biosynthetic pathway, generating the first linear and the first cyclic tetrapyrroles, respectively. Hydroxymethylbilane synthase, 2.5.1.61, and uroporphyrinogen III synthase may function independently and sequentially with hydroxymethylbilane as a free intermediate, heme biosynthetic pathway, overview. Hypoxia downregulates UROS mRNA expression in hepatic cells, reduction of UROS mRNA is associated with the accumulation of hypoxia-inducible factor 1alpha under normoxia. Deferoxamine, cobalt chloride, or hypoxia downregulate UROS mRNA expression in hepatic cells, reduction of UROS mRNA is associated with the accumulation of hypoxia-inducible factor 1alpha under normoxia
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
activates
Ca2+
-
activates
K+
-
activates
KCl
-
optimal concentration is 100 mM, wild-type enzyme
Mg2+
-
activates
Na+
-
activates
Na+
-
activates
Mg2+
-
activates
additional information
-
no metal ions present in enzyme
additional information
-
no requirement
additional information
-
bivalent ions, such as MgCl2 up to 20 mM, fail to stimulate enzyme activity
additional information
-
bivalent ions fail to activate or stabilize the enzyme significantly
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoate)
-
-
Butane-2,3-dione
-
20% residual activity after 45 min at 40 mM
Butane-2,3-dione
-
-
Coproporphyrins
-
-
-
diethyl dicarbonate
-
10% residual activity after 5 min at 0.41 mM
diethyl dicarbonate
-
-
diethyl dicarbonate
-
-
hydroxylamine
-
-
iodoacetamide
-
-
iodoacetic acid
-
-
Macrocyclic spiro-lactam derivatives
-
-
-
N-ethylmaleimide
-
-
N-ethylmaleimide
-
-
NaN3
-
25-30% residual activity with 1.0 mM
NaN3
-
60% residual activity with 5.0 mM
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
Phenylglyoxal
-
50% residual activity after 1 min at 0.3 mM
Phenylglyoxal
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
Pyridoxal 5'-phosphate and subsequent treatment with NaBH4
sulphydryl reagents
-
-
uroporphyrinogen III
-
product inhibition
uroporphyrinogen III
-
product inhibition
Uroporphyrins
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
no bound cofactor
-
additional information
-
no bound cofactor
-
additional information
-
reduced pteroylpolyglutamate factor associated with enzyme, may function as cofactor
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00015
-
Hydroxymethylbilane
-
pH not specified in the publication, temperature not specified in the publication
0.00033
-
Hydroxymethylbilane
-
-
0.005
0.02
Hydroxymethylbilane
-
-
0.005
-
Hydroxymethylbilane
-
-
0.01
0.02
Hydroxymethylbilane
-
-
0.012
0.04
Hydroxymethylbilane
-
-
1.01
-
Hydroxymethylbilane
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
enzyme kinetics in relation to enzyme stability of wild-type and mutant enzymes, wild-type UROIIIS Is a kinetically stable protein, overview
-
additional information
-
additional information
-
kinetic and thermodynamic analysis, thermodynamic versus kinetic stability, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4.6
-
Hydroxymethylbilane
-
-
5.83
-
Hydroxymethylbilane
-
-
30
-
Hydroxymethylbilane
-
-
500
-
Hydroxymethylbilane
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.25
-
-
purified recombinant mutant Y166F
9.4
-
-
hydroxymethylbilane
25
-
-
hydroxymethylbilane
33.37
-
-
pH not specified in the publication, temperature not specified in the publication
40
-
-
purified recombinant wild-type
54.7
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.4
-
-
-
7.4
-
-
-
7.7
7.9
-
-
7.8
7.95
-
-
8
-
-
in both phosphate and Tris buffer
8
-
-
assay at
8.2
-
-
due to instability of preuroporphyrinogen at lower pH enzyme assay with preuroporphyrinogen at
8.2
-
-
assay at
8.2
-
-
; assay at
8.2
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
9.5
-
-
6.5
8.5
-
at pH 6.5: 10% of optimum activity, at pH 8.5: 30% of optimum activity
7
9
-
at pH 7.0: 60% of optimum activity, at pH 9.0: 60% of optimum activity
7.5
9
-
pH 7.5: about 60% of maximal activity, pH 9.0: about 70% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
enzyme assay at
37
-
-
enzyme assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
52
-
the isothermal unfolding rate is determined in the range of 37C-52C
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-, Q1ET39
uroporphyrinogen III synthase forms pairs of bilateral stripes in the lateral mesoderm at the 15-somite stage. At 24 h post-fertilization, uroporphyrinogen III synthase is predominantly expressed in the intermediate cell mass (ICM) that is the major site of hematopoiesis. The expression is drastically suppressed in the bloodless mutants cloche and vlad tepes/gata 1 from 15-somite to 24hpf stages, indicating that both cloche abd vlad tepes/gata 1 are required for the induction and maitenance of uroporphyrinogen III synthase expression in intermediate cell mass
Manually annotated by BRENDA team
-
erythroleukemia cells
Manually annotated by BRENDA team
-
erythroleukemia cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-, O48721
exclusive localization in chloroplasts, UROS has an N-terminal extension acting as a targeting sequence for import of the precursor protein of 34 kD into chloroplasts, followed by processing to the mature size of 29 kDa
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Helicobacter pylori (strain ATCC 700392 / 26695)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas syringae pv. tomato (strain DC3000)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
26000
-
-
SDS-PAGE
27890
-
-
nucleotide sequence
28000
-
-
SDS-PAGE
28000
-
-
about
28810
-
-
mass spectrometry
29000
-
-
gel filtration
29100
-
-
nucleotide sequence
29500
-
-
SDS-PAGE
30000
-
-
gel filtration
31000
-
-
SDS-PAGE
32000
-
-
SDS-PAGE
36000
-
-
gel filtration
38500
-
-
SDS-PAGE, gel filtration
41500
-
-
gel filtration
42000
-
-
gel filtration
additional information
-
-
enzyme exists in 2 interconvertible forms, separable on HPLC
additional information
-
-
purified enzyme is resolved in two bands, each possessing activity, by polyacrylamide gel electrophoresis
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 28807, MALDI-TOF mass spectrometry
?
-
x * 30000, SDS-PAGE
?
-
x * 28712, calculated from sequence
?
-, O48721
x * 34000, precursor enzyme, x * 29000, mature enzyme
?
-
x * 28000
monomer
-
SDS-PAGE, gel filtration
monomer
-
SDS-PAGE, gel filtration
monomer
-
SDS-PAGE, gel filtration, nucleotide sequence
monomer
-
SDS-PAGE, gel filtration
monomer
-
SDS-PAGE, gel filtration, nucleotide sequence
additional information
-
enzyme structure, model
additional information
-
observed interdomain flexibility might be important for catalysis, the active site is located between the domains
additional information
-
mapping of the URO-synthase active site by NMR perturbation studies, modelling by by in silico docking, active site structure, overview
additional information
-
a helical region in the molecule is essential to retain the kinetic stability of the folded conformation
additional information
-
three-dimensional structure, overview
additional information
Q88B90
three-dimensional structure, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
-, O48721
the N-terminal extension of UROS is processed resulting in the mature enzyme of 29 kDa
additional information
-
UROIIIS is processed via the proteosome pathway, which can be reverted by reversibly inhibiting the proteosome with the aldehyde MG132
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
5 mg/ml purified recombinant wild-type and selenomethionine-enzyme, sitting drop vapour diffusion method, 4C, equal volumes of protein solution, containing 10 mM Tris-HCl, pH 7.5, 1 mM dithiothreitol, and reservoir solution, containing 20% 2-methyl-2,4-pentanediol, 100 mM MES, pH 6.0, X-ray diffraction structure determination and analysis at 1.85-2.1 A resolution
-
purified wild-type recombinant His6-tagged U3S and selenomethionine-substituted derivative, 0.001 ml of 20 mg/ml protein in 20 mM Hepes, pH 7.2, 20 mM NaCl, is mixed with 0.001 ml of reservoir solution containing 20% PEG 3350, 0.2 M tri-Na citrate, and equilibrated against 0.1 ml of reservoir solution, about a month at 8C and followed by microseeding method, X-ray diffraction structure determination and analysis at 2.5 A resolution, single wavelength anomalous dispersion method
-
purified recombinant enzyme, three apoenzyme forms, U3S1, U3S2, U3S3, and one enzyme-product complex form, vapor diffusion in sitting drop method, mixing 0.002 ml of protein with 0.002 ml of precipitant solution and equilibration over 1 mL of precipitant solution of different compositions, for U3S1, 1.2 M NaH2PO4, 0.8 M K2H2PO4, for U3S2, 21-24% PEG 8000, 0.2 M Mg-acetate, 0.1 M MES-HCl, pH 6.5, 0.2 M NaCl, and for U3S3, 18-24% PEG 8000, 0.1 M Tris-HCl, pH 8.5, 0.2 mM MgCl2, 4C, 1-7 days, X-ray diffraction structure determination and analysis at 1.6-2.0 A resolution
Q72KM1, -
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
20% loss of activity in 10 min
30
-
-
retention of 100% activity after 24 h
30
-
-
pH 7.4, t1/2: more than 14 days
35
-
-
enzyme reaction linear up to 30 min
37
-
-
about 20% loss of activity after 48 h, about 50% loss of activity after 72 h, buffer containing 1 mM DTT
45
-
-
retention of 90% activity after 24 h
45
-
-
about 10% loss of activity after 24 h, buffer containing 1 mM DTT
45
-
-
pH 7.4, t1/2: 1.9 days
60
-
-
t1/2: 1 min
60
-
-
completely inactivated in 1 min
60
-
-
completely inactivated in 1 min
60
-
-
about 75% loss of activity after 3 min, buffer containing 1 mM DTT
60
-
-
pH 8.2, t1/2: less than 1 day
additional information
-
-
extremely heat labile
additional information
-
-
more thermostable than enzymes from other sources
additional information
-
-
purified enzyme shows remarkable thermostability, particularly when kept in phosphate buffer containing DTT and EDTA, indicating that the activity may depend on its oxidation state
additional information
-
-
UROIIIS is a thermolabile enzyme undergoing irreversible denaturation, unfolding kinetics of wild-type UROIIIS and mutants, circular dichroism, overview. A helical region in the molecule is essential to retain the kinetic stability of the folded conformation
additional information
-
-
the enzyme is metathermostabile, irreversible denaturation process. At physiological temperature and in vitro, UROIIIS has a half-life time of 61.1 h, a long time for the enzyme to exert its function in the cell, dynamic behavior of the protein, three-state model, overview. Thermodynamic versus kinetic stability, overview
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purification needs to be carried out as close to 0C as possible
-
10% glycerol stabilizes the purified recombinant enzyme in 20 mM sodium phosphate, pH 7.45, 100 mM NaCl, 2 mM DTT, and 0.1 mM EDTA at -80C
-
a helical region in the molecule is essential to retain the kinetic stability of the folded conformation
-
activity does not change after several cycles of freeze-and thawing in potassium phosphate buffer, pH 7.4, containing DTT and glycerol
-
dithiothreitol stabilizes
-
enzyme reaction linear up to 30 min at 35C
-
human erythrocyte enzyme more stable than wheat germ enzyme
-
recombinant enzyme in cell lysate is unstable, glycerol stabilizes
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
photooxidation in presence of Rose Bengal
-
5887
not affected by N-bromosuccinimide oxidation
-
5883
photooxidation in presence of Rose Bengal
-
5883
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-70C, at least two years
-
-20C, stable to freezing
-
-70C, several weeks
-
-20C, several months
-
4 C, stable for one week without significant change of activity
-
80C, stable for at least one year
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography, and gel filtration to homogeneity
-, O48721
expression in Escherichia coli
-
from overproducing strain
-
; recombinant N-terminally His-tagged enzyme from Escherichia coli strain strain BL21(DE3) by ultrafiltration, nickel affinity and anion exchange chromatography, followed by gel filtration to homogeneity
-
partial
-
recombinant
-
recombinant wild-type UROIIIS and 25 point mutants in Escherichia coli to over 97% purity
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography, anion exchange chromatography, and gel filtration
-
recombinant His-tagged enzyme from Escherichia coli
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, the tag is cleaved off by TEV, followed by gel filtration
Q72KM1, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene HEM4, library screening and complementation studies, sequence comparisons, expression of the enzyme in the knockout Saccharomyces cerevisiae S150-2B strain, overvexpression of the His-tagged enzyme in Escherichia coli BL21(DE3) cells
-, O48721
expression in Escherichia coli
-
-
-, Q1ET39
overproduction
-
DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes
-
expression in Escherichia coli
-
expression in Escherichia coli; expression of N-terminally His-tagged enzyme in Escherichia coli strain strain BL21(DE3)
-
expression of the N-terminal His-tagged wild-type and mutant enzymes in Escherichia coli BL21(DE3)
-
expression of wild-type UROIIIS and 25 point mutants in Escherichia coli
-
semi-quantitative real-time PCR analysis of ubiquitous and erythroid-specific UROS mRNAs, expression analysis
-
stably expression of GFP-tagged UROIIIS-WT or UROIIIS-C73R proteins in MLP29cell lines, reduced expression levels of C73R-UROIIIS in the mammalian cells
-
gene cobA/hemD encoding the bifunctional uroporphyrinogen III synthase/methyltransferase, DNA and amino acid sequence determination and analysis, subcloning in Escherichia coli strain DH5alpha, expression in Escherichia coli strain BL21(DE3). Unsuccessful expressionin Lactococcus lactis strain NZ9000
Q50EH6
expression in Escherichia coli
P51163
gene pspto_0129, expression of His6-tagged enzyme in Escherichia coli strain BL21 (DE3). The selenomethionine-substituted derivative is produced by expression in an Escherichia coli methionine auxotrophic strain B834(DE3)
-
expression of His-tagged wild-type and mutant enzymes in Escherichia coli
-
overexpression as N-terminally his-tagged enzyme in Escherichia coli
-
expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
Q72KM1, -
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the hepatic and splenic URO-synthase activities are normal or elevated (1-1.6fold) compared with age and sex-matched feline control activities in the dominantly inherited acute intermittent porphyria lines
-
branchpoint sequence mutation markedly reduces the wild type transcript and enzyme activity
-
the efficiency of Uros gene suppression is developmentally regulated, being most effective in mature seedling leaves compared with newly emergent leaves
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A104V
-
a naturally occuring mutation, 60.6% activity compared to the wild-type enzyme
A104V
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
A66V
-
clinical mutation, altered tertiary structure
A66V
-
a naturally occuring mutation, 95.6% activity compared to the wild-type enzyme
A66V
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
A69T
-
a naturally occuring mutation, 24.4% activity compared to the wild-type enzyme
A69T
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
C73A
-
99% of wild-type activity
C73A
-
computational modeling, structure comparison with the wild-type enzyme and the other C73 mutants
C73D
-
computational modeling, structure comparison with the wild-type enzyme and the other C73 mutants
C73L
-
computational modeling, structure comparison with the wild-type enzyme and the other C73 mutants
C73N
-
computational modeling, structure comparison with the wild-type enzyme and the other C73 mutants
C73R
-
9% of wild-type activity
C73R
-
a frequent, naturally occuring mutation of a residue of the stabilizing helical region, 14.5% activity compared to the wild-type enzyme
C73R
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria, the mutant protein retains partial catalytic activity but shows reduced the enzyme stability
C73R
-
a naturally occuring mutation in the enzyme responsible for more than one-third of all of the reported cases of the rare autosomal disease congenital erythropoietic porphyria. The mutant protein retains partial catalytic activity but shows reduced the enzyme stability
C73S
-
78% of wild-type activity
C73S
-
computational modeling, structure comparison with the wild-type enzyme and the other C73 mutants
C73Y
-
computational modeling, structure comparison with the wild-type enzyme and the other C73 mutants
E127A
-
site-directed mutagenesis, unaltered activity level compared to the wild-type enzyme
E249stop
-
clinical mutation, truncated protein, loss of helix 12
E81D
-
a naturally occuring mutation, unaltered activity compared to the wild-type enzyme
E81D
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
G188R
-
a naturally occuring mutation, 41.4% activity compared to the wild-type enzyme
G188R
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
G188W
-
a naturally occuring mutation, 31.6% activity compared to the wild-type enzyme
G188W
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
G225S
-
clinical mutation, altered tertiary structure
G225S
-
a naturally occuring mutation, 32.4% activity compared to the wild-type enzyme
G225S
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
G236V
-
a naturally occuring mutation, 34.0% activity compared to the wild-type enzyme
G236V
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
H173Y
-
a naturally occuring mutation, 72.6% activity compared to the wild-type enzyme
H173Y
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
I129T
-
clinical mutation, altered tertiary structure
I129T
-
a naturally occuring mutation, 20.0% activity compared to the wild-type enzyme
I129T
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
I219S
-
a naturally occuring mutation, 85.0% activity compared to the wild-type enzyme
I219S
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
K220A
-
site-directed mutagenesis, slightly increased activity compared to the wild-type enzyme
L237P
-
a naturally occuring mutation, 57.9% activity compared to the wild-type enzyme
L237P
-
the mutation is associated with congenital erythropoietic porphyria
L237P
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
L4F
-
clinical mutation, altered tertiary structure
L4F
-
a naturally occuring mutation, 20.2% activity compared to the wild-type enzyme
P248Q
-
clinical mutation, altered tertiary structure
P248Q
-
a naturally occuring mutation, 29.2% activity compared to the wild-type enzyme
P248Q
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
P53L
-
clinical mutation, altered tertiary structure
P53L
-
a naturally occuring mutation, inactive mutant, no purification of the recombinant mutant
P53L
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
Q187P
-
a naturally occuring mutation, 15.0% activity compared to the wild-type enzyme
Q187P
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
Q249X
-
the mutation is associated with congenital erythropoietic porphyria
R65A
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
S197A
-
site-directed mutagenesis, unaltered activity level compared to the wild-type enzyme
S212P
-
clinical mutation, altered tertiary structure
S212P
-
a naturally occuring mutation, 20.0% activity compared to the wild-type enzyme
S212P
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
S47P
-
a naturally occuring mutation, unaltered activity compared to the wild-type enzyme
S47P
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
S63A
-
site-directed mutagenesis, unaltered activity level compared to the wild-type enzyme
T103A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
T227A
-
site-directed mutagenesis, slightly increased activity compared to the wild-type enzyme
T228A
-
site-directed mutagenesis, conserved residue near to the active site cleft, reduced activity compared to the wild-type enzyme
T228M
-
clinical mutation, altered tertiary structure
T228M
-
a naturally occuring mutation, 97.5% activity compared to the wild-type enzyme
T228M
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
T62A
-
site-directed mutagenesis, conserved residue near to the active site cleft, unaltered activity level compared to the wild-type enzyme
T62A
-
a naturally occuring mutation, 1.2% activity compared to the wild-type enzyme
T62A
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
V3F
-
clinical mutation, altered tertiary structure
V3F
-
a naturally occuring mutation, 19.3% activity compared to the wild-type enzyme
V3F
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
V82F
-
a naturally occuring mutation, 93.8% activity compared to the wild-type enzyme
V82F
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
V99A
-
a naturally occuring mutation, 88.2% activity compared to the wild-type enzyme
V99A
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
Y168A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
Y19C
-
clinical mutation, altered tertiary structure
Y19C
-
a naturally occuring mutation, 13.1% activity compared to the wild-type enzyme
Y19C
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
C73R
P51163
0.24% of wild-type activity, homozygous mice are fetal lethals
V99A
P51163
5.9% of wild-type activity, homozygous mice are fetal lethals
V99L
P51163
14.8% of wild-type activity
E114A
-
site-directed mutagenesis, the mutant shows activity slightly reduced compared to the wild-type enzyme
E38A
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
L116A
-
site-directed mutagenesis, the mutant shows activity slightly reduced compared to the wild-type enzyme
R164A
-
site-directed mutagenesis, the mutation causes a decrease in enzymatic activity to about 70% that of the wild-type enzyme
R219A
-
site-directed mutagenesis, the mutation causes a decrease in enzymatic activity to about 25% that of the wild-type enzyme
E114A
Pseudomonas syringae DC3000
-
site-directed mutagenesis, the mutant shows activity slightly reduced compared to the wild-type enzyme
-
E38A
Pseudomonas syringae DC3000
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
-
L116A
Pseudomonas syringae DC3000
-
site-directed mutagenesis, the mutant shows activity slightly reduced compared to the wild-type enzyme
-
R164A
Pseudomonas syringae DC3000
-
site-directed mutagenesis, the mutation causes a decrease in enzymatic activity to about 70% that of the wild-type enzyme
-
R219A
Pseudomonas syringae DC3000
-
site-directed mutagenesis, the mutation causes a decrease in enzymatic activity to about 25% that of the wild-type enzyme
-
D17A
-
60.3% of wild-type activity
E68A
-
82.8% of wild-type activity
H173L
-
106.9% of wild-type activity
K10Q
-
39.7% of wild-type activity
K147Q
-
34.5% of wild-type activity
N121D
-
93.1% of wild-type activity
Y168F
-
1.7% of wild-type activity
Y97F
-
74.1% of wild-type activity
D112G
-
site-directed mutagenesis, 50% reduced activity compared to the wild-type enzyme
R15Q
-
site-directed mutagenesis, unaltered activity level compared to the wild-type enzyme
S68A
-
site-directed mutagenesis, unaltered activity level compared to the wild-type enzyme
T100A
-
site-directed mutagenesis, 75% reduced activity compared to the wild-type enzyme
Y166F
-
site-directed mutagenesis, more than 99% reduced activity compared to the wild-type enzyme
L4F
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
additional information
-
16 known mutations causing congenital erythropoietic porphyria in humans via alterations of the tertiary enzyme structure
additional information
-
the naturally occuring clinical mutations lead to loss in activity due to structural alterations in the enzymes, overview
additional information
-
identification of mutations in the uroporphyrinogen III cosynthase gene in German patients with congenital erythropoietic porphyria. Identification of four different mutations: C73R, a hotspot mutation, the promoter mutation 86A, and two missense mutations, designated G236V and L237P, the latter one encounters in the homozygous state in one of the patients
additional information
-
changes in the unfolding rate, relative to wild type, overview. Cloning, expression, and analysis of 25 missense mutants from congenital erythropoietic porphyria, CEP, patients, genotyping, overview
additional information
-
genotype/phenotype analysis of the studied cases of congenital erythropoietic porphyria, overview
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant His-tagged wild-type enzyme from Escherichia coli, to homogeneity
-