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Information on EC 4.2.1.24 - porphobilinogen synthase and Organism(s) Homo sapiens and UniProt Accession P13716
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4.2.1.24 porphobilinogen synthaseIUBMB Comments
The enzyme catalyses the asymmetric condensation and cyclization of two 5-aminolevulinate molecules, which is the first common step in the biosynthesis of tetrapyrrole pigments such as porphyrin, chlorophyll, vitamin B12, siroheme, phycobilin, and cofactor F430. The enzyme is widespread, being essential in organisms that carry out respiration, photosynthesis, or methanogenesis. The enzymes from most organisms utilize metal ions (Zn2+, Mg2+, K+, and Na+) as cofactors that reside at multiple sites, including the active site and allosteric sites. Enzymes from archaea, yeast, and metazoa (including human) contain Zn2+ at the active site. In humans, the enzyme is a primary target for the environmental toxin Pb. The enzymes from some organisms utilize a dynamic equilibrium between architecturally distinct multimeric assemblies as a means for allosteric regulation.
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Word Map
- 4.2.1.24
- erythrocyte
- heme
- protoporphyrin
- urinary
-
poison
- catalase
-
workers
- hemoglobin
- porphyria
-
intoxication
- urine
- anemia
- deaminase
-
thiobarbituric
- gsh
-
tbars
- succinylacetone
-
hematocrit
- cadmium
-
hematological
- uroporphyrinogen
-
ferrochelatase
- tetrapyrrole
- diselenide
-
octamer
-
lead-induced
-
delta-aminolaevulinic
-
lead-exposed
-
diphenyl
- coproporphyria
-
cutanea
- uroporphyrins
- tarda
-
dimercaptosuccinic
- coproporphyrinogen
-
smelter
- tyrosinemia
-
peribiliary
-
occupationally
-
erythropoietic
- medicine
-
bandgaps
-
porphyrinogenic
-
arsenic-induced
- synthesis
- analysis
-
organoselenium
-
proto
-
toxicokinetics
-
micrograms/100
-
furnace
- environmental protection
- diagnostics
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
delta-aminolevulinic acid dehydratase, ala-d, pbgs, delta-ala-d, delta-aminolevulinate dehydratase, ala dehydratase, porphobilinogen synthase, ala synthetase, 5-aminolevulinic acid dehydratase, delta-alad, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5-aminolevulinate dehydrase
-
-
-
-
5-aminolevulinate dehydratase
-
-
-
-
5-aminolevulinate hydro-lyase (adding 5-aminolevulinate and cyclizing)
-
-
-
-
5-aminolevulinic acid dehydrase
-
-
-
-
5-aminolevulinic acid dehydratase
-
-
-
-
5-levulinic acid dehydratase
-
-
-
-
ALAD
ALADH
-
-
-
-
aminolevulinate dehydrase
-
-
-
-
aminolevulinate dehydratase
-
-
-
-
aminolevulinic dehydratase
-
-
-
-
delta-ALAD
delta-aminolevulinate dehydrase
-
-
-
-
delta-aminolevulinate dehydratase
delta-aminolevulinic acid dehydrase
-
-
-
-
delta-aminolevulinic acid dehydratase
delta-aminolevulinic dehydratase
-
-
-
-
gamma-aminolevulinic acid dehydratase
-
-
-
-
Porphobilinogen synthase
-
-
-
-
porphobilinogen synthetase
-
-
-
-
synthase, porphobilinogen
-
-
-
-
ALAD
-
-
-
-
delta-ALAD
-
-
-
-
delta-aminolevulinate dehydratase
-
-
-
-
delta-aminolevulinic acid dehydratase
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -
SYSTEMATIC NAME
IUBMB Comments
5-aminolevulinate hydro-lyase (adding 5-aminolevulinate and cyclizing; porphobilinogen-forming)
The enzyme catalyses the asymmetric condensation and cyclization of two 5-aminolevulinate molecules, which is the first common step in the biosynthesis of tetrapyrrole pigments such as porphyrin, chlorophyll, vitamin B12, siroheme, phycobilin, and cofactor F430. The enzyme is widespread, being essential in organisms that carry out respiration, photosynthesis, or methanogenesis. The enzymes from most organisms utilize metal ions (Zn2+, Mg2+, K+, and Na+) as cofactors that reside at multiple sites, including the active site and allosteric sites. Enzymes from archaea, yeast, and metazoa (including human) contain Zn2+ at the active site. In humans, the enzyme is a primary target for the environmental toxin Pb. The enzymes from some organisms utilize a dynamic equilibrium between architecturally distinct multimeric assemblies as a means for allosteric regulation.
CAS REGISTRY NUMBER
COMMENTARY
9036-37-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5-aminolevulinic acid + 5-aminolevulinic acid
porphobilinogen + 2 H2O
-
-
-
?
5-aminolevulinate + 5-aminolevulinate
porphobilinogen + 2 H2O
the enzyme catalyzes the first common step in the biosynthesis of tetrapyrroles
-
?
5-aminolevulinate + 5-aminolevulinate
porphobilinogen + 2 H2O
the enzyme functions in the first common step in tetrapyrrole biosynthesis
-
?
5-aminolevulinate
?
-
during erythropoiesis in chordates the enzyme functions as a part of the heme synthesizing machinery
-
-
?
5-aminolevulinate
?
-
second enzyme in the heme biosynthetic pathway
-
-
?
5-aminolevulinate + 5-aminolevulinate
porphobilinogen + 2 H2O
-
incubations of erythrocytes for 24 h with glucose result in an increase of delta-ALA-D activity. Incubations of erythrocytes with 100 to 200 mM glucose for 48 h inhibit delta-ALA-D activity
-
-
?
additional information
?
-
-
the enzyme has a dual role: 1. as 5-aminolevulinate dehydatase, the second enzyme in the pathway of heme synthesis, 2. as CF-2 proteasome inhibitor
-
-
?
additional information
?
-
-
direct assay method development with incubation of erythrocyte lysate with the natural substrate, 5-aminolevulinate, followed by quantitative in situ conversion of porphobilinogen to its butyramide and mass spectrometric determination, overview. Using a carbonate buffer rather than phosphate causes nearly a 90% drop in activity and addition of zinc results in a further decrease by up to 35%
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the enzyme has a dual role: 1. as 5-aminolevulinate dehydatase, the second enzyme in the pathway of heme synthesis, 2. as CF-2 proteasome inhibitor
-
-
?
5-aminolevulinate + 5-aminolevulinate
porphobilinogen + 2 H2O
the enzyme catalyzes the first common step in the biosynthesis of tetrapyrroles
-
?
5-aminolevulinate + 5-aminolevulinate
porphobilinogen + 2 H2O
the enzyme functions in the first common step in tetrapyrrole biosynthesis
-
?
5-aminolevulinate
?
-
during erythropoiesis in chordates the enzyme functions as a part of the heme synthesizing machinery
-
-
?
5-aminolevulinate
?
-
second enzyme in the heme biosynthetic pathway
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
chimeric proteins are constructed that contain the aspartate-rich sequences of the pea enzyme or the enzyme from Pseudomonas aeruginosa in place of the naturally occuring cysteine-rich sequence of the human enzyme. The chimeric enzymes are substantially activated by both magnesium and potassium, but not by zinc
Zn2+
the cysteines of the metal switch sequence of the wild-type enzyme bind a catalytic zinc. Chimeric proteins are constructed that contain the aspartate-rich sequences of the pea enzyme or the enzyme from Pseudomonas aeruginosa in place of the naturally occuring cysteine-rich sequence of the human enzyme. The chimeric enzymes are substantially activated by both magnesium and potassium, but not by zinc.
Zinc
Zn2+
Zinc
-
4 Zn at metal binding site A and 4 Zn at metal binding site B are required for full activity per homooctamer
Zinc
-
binds 8 mol of zinc per mol of octamer, zinc may interact with one or more of the highly reactive enzyme thiol groups
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7-(3-aminopentan-3-yl)-5-chloroquinolin-8-ol
using in silico screening two hexamer-stabilizing inhibitors of PBGS are identified: N-(3-methoxyphenyl)-1-methyl-6-oxo-2-[(pyridin-2-ylmethyl)sulfanyl]-1,6-dihydropyrimidine-5-carboxamide and 7-(3-aminopentan-3-yl)-5-chloroquinolin-8-ol
N-(3-methoxyphenyl)-1-methyl-6-oxo-2-[(pyridin-2-ylmethyl)sulfanyl]-1,6-dihydropyrimidine-5-carboxamide
using in silico screening two hexamer-stabilizing inhibitors of PBGS are identified: N-(3-methoxyphenyl)-1-methyl-6-oxo-2-[(pyridin-2-ylmethyl)sulfanyl]-1,6-dihydropyrimidine-5-carboxamide and 7-(3-aminopentan-3-yl)-5-chloroquinolin-8-ol
1,1',1''-[(3-ethoxyprop-1-ene-1,1,2-triyl)triselanyl]tribenzene ethyl 2,3,3-tris(phenylselanyl)prop-2-en-1-yl ether
-
0.6 mM, 65% inhibition
1,1',1''-[(3-ethoxyprop-1-ene-1,1,2-triyl)triselanyl]tris(2,4,6-trimethylbenzene) ethyl 2,3,3-tris[(2,4,6-trimethylphenyl)selanyl]prop-2-en-1-yl ether
-
0.6 mM, 44% inhibition
1,1',1''-[(3-ethoxyprop-1-ene-1,1,2-triyl)triselanyl]tris(4-chlorobenzene) ethyl 2,3,3-tris[(4-chlorophenyl)selanyl]prop-2-en-1-yl ether
-
modest inhibition
2,3-Dimercaptopropanol
-
cysteine and ZnCl2 protects. Dithiothreitol protects inhibition by 1 mM 2,3-dimercaptopropanol in a concentration dependent manner
Carbonate
-
using a carbonate buffer rather than phosphate causes nearly a 90% drop in activity in the developed assay method
D-fructose
-
formation of a Schiff base with the critical lysine residue of the enzyme is involved in inhibition of the enzyme by hexoses and pentoses
D-ribose
-
formation of a Schiff base with the critical lysine residue of the enzyme is involved in inhibition of the enzyme by hexoses and pentoses
Hg2+
-
inhibitory effect is increased by meso-2,3-dimercaptosuccinic acid, inhibition is prevented by dithiothreitol
additional information
-
the enzyme from human erythrocytes is a potential target for organochalcogens
-
2,3-dimercaptopropane-1-sulfonic acid
-
1 mM, 0.5 mM ZnCl2 protects but does not reverse inhibition. Dithiothreitol protects inhibition by 1 mM 2,3-dimercaptopropane-1-sulfonic acid in a concentration dependent manner
2,3-dimercaptopropane-1-sulfonic acid
-
in presence of Hg2+ or Cd2+ the inhibitory potency increases, no change in inhibitory potency by inclusion of Pb2+, Zn2+ does not modify the inhibitory effect
D-glucose
-
formation of a Schiff base with the critical lysine residue of the enzyme is involved in inhibition of the enzyme by hexoses and pentoses
D-glucose
-
incubations of erythrocytes for 24 h with glucose results in an increase of delta-ALA-D activity. Incubations of erythrocytes with 100 to 200 mM glucose for 48 h inhibit delta-ALA-D activity
meso-2,3-dimercaptosuccinic acid
-
4 mM, 1 mM ZnCl2 protects but does not reverse inhibition. Dithiothreitol protects inhibition by 1 mM meso-2,3-dimercaptosuccinic acid in a concentration dependent manner
meso-2,3-dimercaptosuccinic acid
-
in presence of Hg2+ or Cd2+ the inhibitory potency increases, Zn2+ does not modify the inhibitory effect
Zn2+
-
exocenous addition of zinc results in a decrease by up to 35% in enzyme activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glucose
-
incubations of erythrocytes for 24 h with glucose result in an increase of delta-ALA-D activity. Incubations of erythrocytes with 100 to 200 mM glucose for 48 h inhibit delta-ALA-D activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.5
5-aminolevulinic acid
wild type, pH 9, predominantly hexamer and/or dimer
additional information
additional information
the kinetic data do not follow a simple Michaelis-Menten relationship, but can be attributed to catalysis by two different forms of the enzyme that have different Km-values
-
additional information
additional information
-
the kinetic data do not follow a simple Michaelis-Menten relationship, but can be attributed to catalysis by two different forms of the enzyme that have different Km-values
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.9 - 8
pH 5.9: about 50% of maximal activity, pH 8.0: about 70% of maximal activity, wild-type enzyme
6.8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
delta-ALA-D activity in patients with chronic renal failure with hemodialysis treatment and in patients not undergoing hemodialysis is lower when compared to the control group. delta-ALA-D activity correlates positively with hemoglobin content
-
delta-ALA-D activity is decreased in situations associated to hyperglycemia maintained for long periods. Hypofunction of the thyroid gland, when non-compensated, increase the activity of delta-ALA-D
-
-
-
delta-aminolevulinate dehydratase activity is lower in hemodialysis patients compared to control
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
-
delta-aminolevulinic acid dehydratase is involved in the heme biosynthetic pathway
physiological function
-
it is shown that autologous and allogeneic bone marrow transplantation are associated with oxidative stress and that delta-ALA-D activity is a reliable marker for oxidative stress in bone marrow transplantation patients
malfunction
-
delta-ALA-D activity is inhibited in diabetes mellitus, which can result in aminolevulinic acid accumulation that, under physiological relevant conditions, can have pro-oxidant effects. delta-ALA-D activity shows to be correlated with lipid profile indicating that disturbances in lipoproteins metabolism may affect the enzymatic activity
malfunction
-
delta-aminolevulinic acid dehydratase-deficient porphyria is a rare enzymatic deficiency of the heme biosynthetic pathway
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HEM2_HUMAN
330
0
36295
Swiss-Prot
Secretory Pathway (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
244000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
octamer
octamer
additional information
dimer
pro-hexamer dimer and pro-octamer dimer, analyzed by gel filtration
hexamer
wild type, pH 8.8, catalytic turnover favors octamer, analyzed by gel filtration and anion exchange chromatography
hexamer
hexameric structure of the enzyme only shows low activity. Using in silico screening two hexamer-stabilizing inhibitors of PBGS are identified: N-(3-methoxyphenyl)-1-methyl-6-oxo-2-[(pyridin-2-ylmethyl)sulfanyl]-1,6-dihydropyrimidine-5-carboxamide and 7-(3-aminopentan-3-yl)-5-chloroquinolin-8-ol
octamer
the enzyme is an obligate oligomer that can exist in functionally distinct quaternary states of different stoichiometries, which are called morpheeins, human PBGS assembles into long-lived morpheeins and is capable of forming either a high activity octamer or a low activity hexamer
octamer
wild type, pH 6.9 and pH 8.8, analyzed by gel filtration and anion exchange chromatography
additional information
wild-type enzyme and variant F12L exist in different oligomeric states. The wild-type enzyme exists as an octamer and the F12L variant exists as a hexamer. It appears that any equilibrium between octamer and hexamer most probably proceeds through the interconversion of hugging dimer and the detached dimer
additional information
-
wild-type enzyme and variant F12L exist in different oligomeric states. The wild-type enzyme exists as an octamer and the F12L variant exists as a hexamer. It appears that any equilibrium between octamer and hexamer most probably proceeds through the interconversion of hugging dimer and the detached dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
two monomers per asymmetric unit. In native human ALAD, the A monomer has a ligand resembling the substrate 5-aminolaevulinic acid which is covalently bound by a Schiff base to active-site Lys252 and is held in place by an ordered active-site loop. These features of the active-site structure are disordered or absent in the B subunit. Comparison of substrate and product complexes from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A274K
naturally occurring ALAD porphyria-associated human PBGS mutants are shown to have an increased susceptibility to inhibition by both N-(3-methoxyphenyl)-1-methyl-6-oxo-2-[(pyridin-2-ylmethyl)sulfanyl]-1,6-dihydropyrimidine-5-carboxamide and 7-(3-aminopentan-3-yl)-5-chloroquinolin-8-ol
E89K
naturally occurring ALAD porphyria-associated human PBGS mutants are shown to have an increased susceptibility to inhibition by both N-(3-methoxyphenyl)-1-methyl-6-oxo-2-[(pyridin-2-ylmethyl)sulfanyl]-1,6-dihydropyrimidine-5-carboxamide and 7-(3-aminopentan-3-yl)-5-chloroquinolin-8-ol
F12L
R240A
mutant enzyme assembles into a metastable hexamer, which can undergo a reversible conversion to the octamer in the presence of substrate
additional information
F12L
the catalytic activity is very low under conditions at which the wild-type human enzyme is most active
F12L
low activity mutant F12L shows a hexameric structure, mutant F12L is used for in silico screening of 111000 structures for hexamer-stabilizing inhibitors
additional information
chimeric proteins that contain the aspartate-rich sequences of the pea enzyme or the enzyme from Pseudomonas aeruginosa in place of the naturally occuring cysteine-rich sequence of the human enzyme. The chimeric enzymes are substantially activated by both magnesium and potassium, but not by zinc. The specific activities of the chimeras are significantly lower than the specific activity of the wild-type enzyme
additional information
-
chimeric proteins that contain the aspartate-rich sequences of the pea enzyme or the enzyme from Pseudomonas aeruginosa in place of the naturally occuring cysteine-rich sequence of the human enzyme. The chimeric enzymes are substantially activated by both magnesium and potassium, but not by zinc. The specific activities of the chimeras are significantly lower than the specific activity of the wild-type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
sensitive to oxygen, t1/2: 135 min, the oxygen-inactivated enzyme is restored to full activity by incubation with thiols
-
210688
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, protein concentration above 2 mg/ml, 20 mM phosphate, 5 mM dithiothreitol, pH 6.8, stable for 6 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
diagnostics
medicine
diagnostics
-
the DELTA-aminolevulinic acid dehydratase test of blood is valid and representative for low-level as well as long-term exposure to lead. The test might be applicable to diagnostic purposes and screening of the population having been exposed to low-level lead over a long-term period
diagnostics
-
the enzyme activity is a diagnostic marker for the clinical diagnosis of delta-aminolevulinic acid dehydratase-deficient porphyria, a rare enzymatic deficiency of the heme biosynthetic pathway
medicine
-
delta-ALA-D activity is a reliable marker for oxidative stress in bone marrow transplantation patients
medicine
-
in blood samples from patients previously treated for lung cancer with chemotherapy, ALAD activity shows a 37% decrease compared with control. Reactive species and thiobarbituric acid reactive substances are 8% and 99% higher in the patient group, respectively. The activity of superoxide dismutase and catalase as well as the vitamin C content are 41%, 35% and 127% lower in patients when compared with controls, respectively. Total thiols and vitamin E levels are 27% and 44% higher in lung cancer patients, respectively
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wetmur, J.G.; Bishop, D.F.; Ostasiewicz, L.; Desnick, R.J.
Molecular cloning of cDNA for human delta-aminolevulinate dehydratase
Gene
43
123-130
1986
Homo sapiens
Bishop, D.F.; Desnick, R.J.
Porphobilinogen synthase: a specific and sensitive coupled-enzyme assay
Methods Enzymol.
123
339-345
1986
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus
Gibbs, P.N.B.; Chaudhry, A.G.; Jordan, P.M.
Purification and properties of 5-aminolevulinate dehydratase from human erythrocytes
Biochem. J.
230
25-34
1985
Homo sapiens
Gibbs, P.N.B.; Gore, M.G.; Jordan, P.M.
Investigation of the effect of metal ions on the reactivity of thiol groups in human 5-aminolaevulinate dehydratase
Biochem. J.
225
573-580
1985
Homo sapiens
Schaller, K.H.; Berlin, A.
delta-Aminolevulinate dehydratase
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
4
363-368
1984
Homo sapiens
-
Gibbs, P.N.B.; Jordan, P.M.
5-Aminolaevulinate dehydratase: Zinc-65 binding and exchange with the enzyme from human erythrocytes
Biochem. Soc. Trans.
9
232-233
1981
Homo sapiens
-
Hueckel, D.; Beyersmann, D.
Rapid purification and direct spectrophotometric assay for 5-aminolevulinic acid dehydratase
Anal. Biochem.
97
277-281
1979
Homo sapiens
Anderson, P.M.; Desnick, R.J.
Purification and properties of delta-aminolevulinate dehydrase from human erythrocytes
J. Biol. Chem.
254
6924-6930
1979
Homo sapiens
Shemin, D.
delta-Aminolevulinic acid dehydratase
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
7
323-337
1972
Bos taurus, Saccharomyces cerevisiae, Gallus gallus, Oryctolagus cuniculus, Homo sapiens, Mus musculus, Nicotiana tabacum, Rattus norvegicus, Rhodobacter capsulatus, Cereibacter sphaeroides, Triticum aestivum
-
Guo, G.G.; Gu, M.; Etlinger, J.D.
240-kDa proteasome inhibitor (CF-2) is identical to delta-aminolevulinic acid dehydratase
J. Biol. Chem.
269
12399-12402
1994
Homo sapiens
Jaffe, E.K.
The porphobilinogen synthase family of metalloenzymes
Acta Crystallogr. Sect. D
56
115-128
2000
Actinobacillus sp., Synechocystis sp., Aquifex sp., Archaeoglobus sp., Bordetella sp., Bradyrhizobium sp., Campylobacter sp., Candida sp. (in: Saccharomycetales), Caulobacter sp., Streptomyces sp., Chlamydia sp., Chlamydomonas sp., Clostridium sp., Deinococcus sp., Escherichia coli, Helicobacter sp., Homo sapiens, Methanobacterium sp., Methanococcus sp., Methanothermus sp., Mycobacterium sp., Neisseria sp., Physcomitrella sp., Pisum sativum, Propionibacterium sp., Rattus norvegicus, Rhodobacter sp., Rickettsia sp., Salmonella sp., Schizosaccharomyces sp., Shewanella sp., Vibrio sp., Yersinia sp., Saccharomyces cerevisiae (P05373), Pseudomonas aeruginosa (Q59643)
Nogueira, C.W.; Santos, F.W.; Soares, F.A.; Rocha, J.B.
2,3-Dimercaptopropanol, 2,3-dimercaptopropane-1-sulfonic acid, and meso-2,3-dimercaptosuccinic acid inhibit delta-aminolevulinate dehydratase from human erythrocytes in vitro
Environ. Res.
94
254-261
2004
Homo sapiens
Jaffe, E.K.
Investigations on the metal switch region of human porphobilinogen synthase
J. Biol. Inorg. Chem.
8
176-184
2003
Homo sapiens (P13716), Homo sapiens
Breinig, S.; Kervinen, J.; Stith, L.; Wasson, A.S.; Fairman, R.; Wlodawer, A.; Zdanov, A.; Jaffe, E.K.
Control of tetrapyrrole biosynthesis by alternate quaternary forms of porphobilinogen synthase
Nat. Struct. Biol.
10
757-763
2003
Homo sapiens (P13716), Homo sapiens
Nogueira, C.W.; Soares, F.A.; Nascimento, P.C.; Muller, D.; Rocha, J.B.
2,3-Dimercaptopropane-1-sulfonic acid and meso-2,3-dimercaptosuccinic acid increase mercury- and cadmium-induced inhibition of delta-aminolevulinate dehydratase
Toxicology
184
85-95
2003
Homo sapiens
Nogueira, C.W.; Borges, V.C.; Zeni, G.; Rocha, J.B.T.
Organochalcogens effects on D-aminolevulinate dehydratase activity from human erythrocytic cells in vitro
Toxicology
191
169-178
2003
Homo sapiens
Gabriel, D.; Pivetta, L.; Folmer, V.; Soares, J.C.; Augusti, G.R.; Nogueira, C.W.; Zeni, G.; Rocha, J.B.
Human erythrocyte delta-aminolevulinate dehydratase inhibition by monosaccharides is not mediated by oxidation of enzyme sulfhydryl groups
Cell Biol. Int.
29
669-674
2005
Homo sapiens
Baranauskiene, D.; Naginiene, R.; Kregzdyte, R.; Ryselis, S.; Abdrakhmanovas, O.
Application of D-aminolevulinic acid dehydratase test for the assessment of occupational long-term lead exposure
Trace Elem. Electrolytes
21
232-235
2004
Homo sapiens
-
Soares, J.C.; Gabriel, D.; Folmer, V.; Augusti, G.R.; Rocha, J.B.
High concentrations of glucose can activate or inhibit human erythrocyte aminolevulinate dehydratase in vitro depending exposure time
Am. J. Biochem. Biotechnol.
2
180-185
2006
Homo sapiens
-
da Silva, A.C.; Rocha, J.B.; Morsch, A.L.; Zanin, R.F.; Kaizer, R.; Maldonado, P.A.; Arantes, L.C.; Silva, L.A.; Morsch, V.M.; Schetinger, M.R.
Oxidative stress and delta-ALA-D activity in chronic renal failure patients
Biomed. Pharmacother.
61
180-185
2007
Homo sapiens
Souza, J.B.; Rocha, J.B.; Nogueira, C.W.; Borges, V.C.; Kaizer, R.R.; Morsch, V.M.; Dressler, V.L.; Martins, A.F.; Flores, E.M.; Schetinger, M.R.
delta-Aminolevulinate dehydratase (delta-ALA-D) activity in diabetes and hypothyroidism
Clin. Biochem.
40
321-325
2007
Homo sapiens
Valentini, J.; Schmitt, G.C.; Grotto, D.; Santa Maria, L.D.; Boeira, S.P.; Piva, S.J.; Brucker, N.; Bohrer, D.; Pomblum, V.J.; Emanuelli, T.; Garcia, S.C.
Human erythrocyte delta-aminolevulinate dehydratase activity and oxidative stress in hemodialysis patients
Clin. Biochem.
40
591-594
2007
Homo sapiens
Tang, L.; Breinig, S.; Stith, L.; Mischel, A.; Tannir, J.; Kokona, B.; Fairman, R.; Jaffe, E.K.
Single amino acid mutations alter the distribution of human porphobilinogen synthase quaternary structure isoforms (morpheeins)
J. Biol. Chem.
281
6682-6690
2006
Homo sapiens (P13716), Homo sapiens
Borges, V.C.; Dadalt, G.; Savegnago, L.; Moro, A.V.; Rocha, J.B.; Nogueira, C.W.
1,1,2-Tris-organoselenide alkene derivatives, but not 1,2-bis-organoselenide alkene derivatives, inhibited delta-aminolevulinate dehydratase activity from human erythrocytic cells in vitro
Toxicol. In Vitro
21
387-391
2007
Homo sapiens
Selwood, T.; Tang, L.; Lawrence, S.H.; Anokhina, Y.; Jaffe, E.K.
Kinetics and thermodynamics of the interchange of the morpheein forms of human porphobilinogen synthase
Biochemistry
47
3245-3257
2008
Homo sapiens (P13716), Homo sapiens
Inoue, R.; Akagi, R.
Co-synthesis of human delta-aminolevulinate dehydratase (ALAD) mutants with the wild-type enzyme in cell-free system-critical importance of conformation on enzyme activity-
J. Clin. Biochem. Nutr.
43
143-153
2008
Homo sapiens
Goncalves, T.L.; Benvegnu, D.M.; Bonfanti, G.; Frediani, A.V.; Rocha, J.B.
delta-Aminolevulinate dehydratase activity and oxidative stress during melphalan and cyclophosphamide-BCNU-etoposide (CBV) conditioning regimens in autologous bone marrow transplantation patients
Pharmacol. Res.
59
279-284
2008
Homo sapiens
Goncalves, T.L.; Benvegnu, D.M.; Bonfanti, G.; Frediani, A.V.; Rocha, J.B.
Delta-ALA-D activity is a reliable marker for oxidative stress in bone marrow transplant patients
BMC Cancer
9
138
2009
Homo sapiens
Lawrence, S.H.; Ramirez, U.D.; Selwood, T.; Stith, L.; Jaffe, E.K.
Allosteric inhibition of human porphobilinogen synthase
J. Biol. Chem.
284
35807-35817
2009
Homo sapiens (P13716), Homo sapiens
Choiniere, J.R.; Scott, C.R.; Gelb, M.H.; Turecek, F.
Direct assay of delta-aminolevulinic acid dehydratase in heme biosynthesis for the detection of porphyrias by tandem mass spectrometry
Anal. Chem.
82
6730-6736
2010
Homo sapiens
Bonfanti, G.; Ceolin, R.B.; Valcorte, T.; De Bona, K.S.; de Lucca, L.; Goncalves, T.L.; Moretto, M.B.
delta-Aminolevulinate dehydratase activity in type 2 diabetic patients and its association with lipid profile and oxidative stress
Clin. Biochem.
44
1105-1109
2011
Homo sapiens
Saraiva, R.A.; Bueno, D.C.; Nogara, P.A.; Rocha, J.B.
Molecular docking studies of disubstituted diaryl diselenides as mammalian delta-aminolevulinic acid dehydratase enzyme inhibitors
J. Toxicol. Environ. Health A
75
1012-1022
2012
Homo sapiens
Mills-Davies, N.; Butler, D.; Norton, E.; Thompson, D.; Sarwar, M.; Guo, J.; Gill, R.; Azim, N.; Coker, A.; Wood, S.; Erskine, P.; Coates, L.; Cooper, J.; Rashid, N.; Akhtar, M.; Shoolingin-Jordan, P.
Structural studies of substrate and product complexes of 5-aminolaevulinic acid dehydratase from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis
Acta Crystallogr. Sect. D
73
9-21
2017
Pyrobaculum calidifontis (A3MWV9), Pyrobaculum calidifontis, Escherichia coli (P0ACB2), Escherichia coli, Homo sapiens (P13716), Homo sapiens, Pyrobaculum calidifontis JCM 11548 (A3MWV9)
Zanini, D.; Pelinson, L.; Schmatz, R.; Belmonte Pereira, L.; Curry Martins, C.; Baldissareli, J.; Pires Amaral, G.; Antunes Soares, F.; Brenner Reetz, L.; Araujo, M.; Chiesa, J.; Morsch, V.; Bitencourt Rosa Leal, D.; Schetinger, M.
delta-Aminolevulinate dehydratase activity in lung cancer patients and its relationship with oxidative stress
Biomed. Pharmacother.
68
603-609
2014
Homo sapiens
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