Information on EC 4.99.1.4 - sirohydrochlorin ferrochelatase

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

EC NUMBER
COMMENTARY hide
4.99.1.4
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RECOMMENDED NAME
GeneOntology No.
sirohydrochlorin ferrochelatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
siroheme + 2 H+ = sirohydrochlorin + Fe2+
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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Metabolic pathways
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Porphyrin and chlorophyll metabolism
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siroheme biosynthesis
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heme metabolism
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SYSTEMATIC NAME
IUBMB Comments
siroheme ferro-lyase (sirohydrochlorin-forming)
This enzyme catalyses the third of three steps leading to the formation of siroheme from uroporphyrinogen III. The first step involves the donation of two S-adenosyl-L-methionine-derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107, uroporphyrin-III C-methyltransferase) and the second step involves an NAD+-dependent dehydrogenation to form sirohydrochlorin from precorrin-2 (EC 1.3.1.76, precorrin-2 dehydrogenase). In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. In some bacteria, steps 1-3 are catalysed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirB being responsible for the above reaction.
CAS REGISTRY NUMBER
COMMENTARY hide
9012-93-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain DSM509
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Manually annotated by BRENDA team
no activity in Desulfovibrio vulgaris
gene cysG
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
precorrin-2 + Co2+
cobalt-precorrin-2 + 2 H+
show the reaction diagram
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + 2 H+
show the reaction diagram
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
show the reaction diagram
-
pH 8.0
-
-
?
sirohydrochlorin + Fe2+
siroheme + 2 H+
show the reaction diagram
sirohydrochlorin + Fe2+
siroheme + H+
show the reaction diagram
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
sirohydrochlorin + Fe2+
siroheme + 2 H+
show the reaction diagram
sirohydrochlorin + Fe2+
siroheme + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4Fe-4S-center
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
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inactivates the enzyme at high concentrations
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Co2+
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inactivates the enzyme at high concentrations
Fe2+
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inactivates the enzyme at high concentrations
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0034
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pH 8, cobaltochelation of precorrin-2
0.0054
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isolated recombinant enzyme, with ferrous iron as substrate
0.0138
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S128D mutant CysG, cobalt chelation of sirohydrochlorin
0.0311
wild-type Met8p
0.0485
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isolated recombinant enzyme, with cobalt as substrate
0.0656
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wild-type CysG, cobalt chelation of sirohydrochlorin
0.243
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S128A mutant CysG, cobalt chelation of sirohydrochlorin
0.337
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pH 8, cobaltochelation of sirohydrochlorin
33.25
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mutant enzyme C199A, in 20 mM Tris/HCl (pH 8.0) and 10 mM NaCl, at 23C
36.08
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mutant enzyme C213A, in 20 mM Tris/HCl (pH 8.0) and 10 mM NaCl, at 23C
38.5
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wild type enzyme, in 20 mM Tris/HCl (pH 8.0) and 10 mM NaCl, at 23C
43
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mutant enzyme C219A, in 20 mM Tris/HCl (pH 8.0) and 10 mM NaCl, at 23C
44.67
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mutant enzyme C135A, in 20 mM Tris/HCl (pH 8.0) and 10 mM NaCl, at 23C
55.17
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mutant enzyme C210A, in 20 mM Tris/HCl (pH 8.0) and 10 mM NaCl, at 23C
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18600
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2 * 18600, estimated from SDS-PAGE
20000
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x * 20000, SDS-PAGE
33000
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1 * 33000, SDS-PAGE
36010
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calculated from gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 20000, SDS-PAGE
homodimer
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
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CysG, phosphorylation of Ser-128, plays a regulatory role
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using in 0.2 M imidazole malate pH 5.5, 24% (w/v) PEG 600 at a ratio of 50:50 ratio of protein : mother liquor and 10% ethylene glycol
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X-ray crystal structure of Met8p
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X-ray crystal structure of Met8p, hanging drop method
X-ray crystal structure of CysG
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
chelating Sepharose column chromatography
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Ni-NTA column chromatography
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recombinant protein
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recombinant SirB
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 codonplus (RIPL) cells
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expressed in Escherichia coli BL21(DE3) cells
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expression in Escherichia coli
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sirB, expression in Escherichia coli BL21(DE3)pLysS, sirA,B,C operon, amino acid sequence
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C135A
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the mutant shows increased specific activity compared to the wild type enzyme
C199A
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the mutant shows reduced specific activity compared to the wild type enzyme
C210A
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the mutant shows increased specific activity compared to the wild type enzyme
C213A
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the mutant shows reduced specific activity compared to the wild type enzyme
C219A
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the mutant shows increased specific activity compared to the wild type enzyme
H237A
mutant of bifunctional Met8p is active as both dehydrogenase and ferrochelatase
S128A
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mutant has higher cobalt chelatase activity than wild-type CysG with sirohydrochlorin as substrate
S128D
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mutant has lower cobalt chelatase activity than wild-type CysG with sirohydrochlorin as substrate
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