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Information on EC 4.99.1.9 - coproporphyrin ferrochelatase and Organism(s) Bacillus subtilis and UniProt Accession P32396

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IUBMB Comments
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.
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This record set is specific for:
Bacillus subtilis
UNIPROT: P32396
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The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
coproporphyrin ferrochelatase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
protoporphyrin + Fe2+
protoheme + 2 H+
show the reaction diagram
i.e. reaction of EC 4.99.1.1
-
-
?
protoporphyrin IX + Zn2+
Zn protoporphyrin IX
show the reaction diagram
-
-
-
?
coproporphyrin III + Co2+
Co-coproporphyrin III + 2 H+
show the reaction diagram
-
specific activity with Co2+ is 6fold higher than with Fe2+
-
-
?
coproporphyrin III + Cu2+
Cu-coproporphyrin III + 2 H+
show the reaction diagram
-
specific activity with Cu2+ is 4.15old higher than with Fe2+
-
-
?
coproporphyrin III + Fe2+
Fe-coproporphyrin III + 2 H+
show the reaction diagram
-
-
-
-
?
coproporphyrin III + Ni2+
Ni-coproporphyrin III + 2 H+
show the reaction diagram
-
specific activity with Ni2+ is 4fold lower than with Fe2+
-
-
?
protoporphyrin IX + Cu2+
Cu-protoporphyrin IX + 2 H+
show the reaction diagram
-
-
-
-
?
protoporphyrin IX + Fe2+
Fe-protoporphyrin IX + 2 H+
show the reaction diagram
-
the enzyme shows no detectable activity with Ca2+, Co2+, Fe3+, Mg2+, or Rb+
-
-
?
protoporphyrin IX + Zn2+
Zn-protoporphyrin IX + 2 H+
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
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
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-ethylmaleimide
-
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
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0018
coproporphyrin III
-
pH 7.5, 37°C
0.17
Cu2+
-
pH 7.2, 30°C
0.008
protoporphyrin IX
-
pH 7.2, 30°C. The Km-value for protoporphyrin IX is the same independent of whether Zn2+ or Fe2+ is used in the reaction
0.017
Zn2+
-
pH 7.2, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0078
coproporphyrin III
-
pH 7.5, 37°C
0.4
protoporphyrin IX
-
pH 7.2, 30°C. 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
4.3
coproporphyrin III
-
pH 7.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
-
pH 6.5: about 50% of maximal activity, pH 8.0: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
a hemH mutant primarily accumulates protoporphyrin IX
metabolism
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35348
-
1 * 35348, calculated from sequence
40000
-
gel filtration
40500
-
1 * 40500, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 40500, SDS-PAGE, x * 35348, calculated
monomer
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
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E264Q
21% of wild-type activity
E264V
less than 1% of wild-type activity
H183A
less than 1% of wild-type activity
H183C
less than 1% of wild-type activity
H88A
5% of wild-type activity
K87A
92% of wild-type activity
Y13F
71% of wild-type activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, the purified enzyme is stable for at least five months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene cloned in pUC18, expression in Escherichia coli JM109/pLUGlSe2
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hansson, M.; Hederstedt, L.
Purification and characterisation of a water-soluble ferrochelatase from Bacillus subtilis
Eur. J. Biochem.
220
201-208
1994
Bacillus subtilis
Manually annotated by BRENDA team
Hansson, M.D.; Karlberg, T.; Rahardja, M.A.; Al-Karadaghi, S.; Hansson, M.
Amino acid residues His183 and Glu264 in Bacillus subtilis ferrochelatase direct and facilitate the insertion of metal ion into protoporphyrin IX
Biochemistry
46
87-94
2007
Bacillus subtilis (P32396), Bacillus subtilis 168 (P32396)
Manually annotated by BRENDA team
Hansson, M.; Hederstedt, L.
Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes
J. Bacteriol.
174
8081-8093
1992
Bacillus subtilis (P32396), Bacillus subtilis 168 (P32396)
Manually annotated by BRENDA team
Dailey, H.A.; Gerdes, S.; Dailey, T.A.; Burch, J.S.; Phillips, J.D.
Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin
Proc. Natl. Acad. Sci. USA
112
2210-2215
2015
Bacillus subtilis, Cutibacterium acnes, Mycobacterium tuberculosis
Manually annotated by BRENDA team
Al-Karadaghi, S.; Hansson, M.; Nikonov, S.; Jonsson, B.; Hederstedt, L.
Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis
Structure
5
1501-1510
1997
Bacillus subtilis, Bacillus subtilis 168
Manually annotated by BRENDA team