Information on EC 4.99.1.9 - coproporphyrin ferrochelatase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.99.1.9
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RECOMMENDED NAME
GeneOntology No.
coproporphyrin ferrochelatase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Fe-coproporphyrin III + 2 H+ = coproporphyrin III + Fe2+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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heme b biosynthesis IV (Gram-positive bacteria)
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Metabolic pathways
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Porphyrin and chlorophyll metabolism
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SYSTEMATIC NAME
IUBMB Comments
protoheme ferro-lyase (protoporphyrin-forming)
The enzyme, present in Gram-positive bacteria, participates in heme biosynthesis. It can also catalyse the reaction of EC 4.99.1.1, protoporphyrin IX ferrochelatase, at a much lower level.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
coproporphyrin III + Co2+
Co-coproporphyrin III + 2 H+
show the reaction diagram
coproporphyrin III + Cu2+
Cu-coproporphyrin III + 2 H+
show the reaction diagram
coproporphyrin III + Fe2+
Fe-coproporphyrin III + 2 H+
show the reaction diagram
coproporphyrin III + Ni2+
Ni-coproporphyrin III + 2 H+
show the reaction diagram
protoporphyrin + Fe2+
protoheme + 2 H+
show the reaction diagram
protoporphyrin IX + Cu2+
Cu-protoporphyrin IX + 2 H+
show the reaction diagram
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-
-
-
?
protoporphyrin IX + Fe2+
Fe-protoporphyrin IX + 2 H+
show the reaction diagram
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the enzyme shows no detectable activity with Ca2+, Co2+, Fe3+, Mg2+, or Rb+
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-
?
protoporphyrin IX + Zn2+
Zn protoporphyrin IX
show the reaction diagram
protoporphyrin IX + Zn2+
Zn-protoporphyrin IX + 2 H+
show the reaction diagram
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?
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
coproporphyrin III + Fe2+
Fe-coproporphyrin III + 2 H+
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-ethylmaleimide
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2 mM, 99% inactivation after incubation for 2 h. Protoporphyrin IX or Zn2+ at concentrations of 0.8 mM and 20 mM, respectively, does not protect
p-Chloromercuriphenylsulfonate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0018 - 0.0105
coproporphyrin III
0.17
Cu2+
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pH 7.2, 30C
0.008
protoporphyrin IX
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pH 7.2, 30C. The Km-value for protoporphyrin IX is the same independent of whether Zn2+ or Fe2+ is used in the reaction
0.017
Zn2+
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pH 7.2, 30C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0078 - 0.03
coproporphyrin III
0.4
protoporphyrin IX
Bacillus subtilis
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pH 7.2, 30C. The Km-value for protoporphyrin IX is the same independent of whether Zn2+ or Fe2+ is used in the reaction
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.9 - 4.3
coproporphyrin III
92964
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
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pH 6.5: about 50% of maximal activity, pH 8.0: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35348
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1 * 35348, calculated from sequence
40000
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gel filtration
40500
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1 * 40500, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 35348, calculated from sequence; 1 * 40500, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structure in presence of iron. Only a single iron ion is found in the active site, coordinated in a square pyramidal fashion by two amino acid residues, His183 and Glu264, and three water molecules. This iron ion is not present in the structure of a His183Ala modified ferrochelatase. Insertion of a metal ion into protoporphyrin IX by ferrochelatase occurs from a metal binding site represented by His183 and Glu264
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the three-dimensional structure is determined at 1.9 A resolution by the method of multiple isomorphous replacement. The structural model contains 308 of the 310 amino acid residues of the protein and 198 solvent molecules
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, the purified enzyme is stable for at least five months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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gene cloned in pUC18, expression in Escherichia coli JM109/pLUGlSe2
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E264Q
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21% of wild-type activity
E264V
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less than 1% of wild-type activity
H183A
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less than 1% of wild-type activity
H183C
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less than 1% of wild-type activity
H88A
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5% of wild-type activity
K87A
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92% of wild-type activity
Y13F
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71% of wild-type activity