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Information on EC 4.2.1.24 - porphobilinogen synthase and Organism(s) Pyrobaculum calidifontis and UniProt Accession A3MWV9

for references in articles please use BRENDA:EC4.2.1.24
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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.24 porphobilinogen synthase
IUBMB 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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Pyrobaculum calidifontis
UNIPROT: A3MWV9
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Word Map
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The taxonomic range for the selected organisms is: Pyrobaculum calidifontis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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2
5-aminolevulinate
=
porphobilinogen
+
2
H2O
2
=
+
2
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Pcal_1709
locus name
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
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-
-
-
ALAD
-
-
-
-
ALADH
-
-
-
-
aminolevulinate dehydrase
-
-
-
-
aminolevulinate dehydratase
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-
-
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aminolevulinic dehydratase
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-
-
-
delta-ALAD
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-
-
-
delta-aminolevulinate dehydrase
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-
-
-
delta-aminolevulinate dehydratase
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-
-
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delta-aminolevulinic acid dehydrase
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-
-
-
delta-aminolevulinic acid dehydratase
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-
-
-
delta-aminolevulinic dehydratase
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-
-
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gamma-aminolevulinic acid dehydratase
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-
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Porphobilinogen synthase
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-
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porphobilinogen synthetase
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-
-
-
synthase, porphobilinogen
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-
-
-
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 hide
9036-37-7
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
requires exogenous thiols and zinc ions for optimal activity. 0.7 zinc ions per mol of subunit
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 37676, mass spectroscopy
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 3.5 A resolution. Comparison of substrate and product complexes from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team