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Enzyme Nomenclature
Information on EC 4.99.1.9 - coproporphyrin ferrochelatase
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4.99.1.9 coproporphyrin ferrochelataseIUBMB 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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The enzyme appears in viruses and cellular organisms
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
hemH
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Fe-coproporphyrin III + 2 H+ = coproporphyrin III + Fe2+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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.
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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
protoporphyrin IX + Fe2+
Fe-protoporphyrin IX + 2 H+
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the enzyme shows no detectable activity with Ca2+, Co2+, Fe3+, Mg2+, or Rb+
-
-
?
coproporphyrin III + Co2+
Co-coproporphyrin III + 2 H+
-
specific activity with Co2+ is 6fold higher than with Fe2+
-
-
?
coproporphyrin III + Co2+
Co-coproporphyrin III + 2 H+
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specific activity with Co2+ is 2.8fold higher than with Fe2+
-
-
?
coproporphyrin III + Cu2+
Cu-coproporphyrin III + 2 H+
-
specific activity with Cu2+ is 4.15old higher than with Fe2+
-
-
?
coproporphyrin III + Cu2+
Cu-coproporphyrin III + 2 H+
-
specific activity with Cu2+ is 5.35old higher than with Fe2+
-
-
?
coproporphyrin III + Ni2+
Ni-coproporphyrin III + 2 H+
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specific activity with Ni2+ is 4fold lower than with Fe2+
-
-
?
coproporphyrin III + Ni2+
Ni-coproporphyrin III + 2 H+
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specific activity with Ni2+ is 80% compared to activity with Fe2+
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
i.e. reaction of EC 4.99.1.1
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
i.e. reaction of EC 4.99.1.1
-
-
?
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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
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8
-
pH 6.5: about 50% of maximal activity, pH 8.0: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
physiological function
a hemH mutant primarily accumulates protoporphyrin IX
physiological function
-
hemH mutants accumulate all three tetrapyrroles: uroporphyrin, coproporphyrin, and protoporphyrin. Porphyrin accumulation does not occur in these mutants (in a hemA4 background) in the absence of 5-aminolevulinic acid
physiological function
-
a hemH mutant primarily accumulates protoporphyrin IX
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35348
40500
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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
brenda
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)
brenda
Xu, K.; Delling, J.; Elliott, T.
The genes required for heme synthesis in Salmonella typhimurium include those encoding alternative functions for aerobic and anaerobic coproporphyrinogen oxidation
J. Bacteriol.
174
3953-3963
1992
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
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)
brenda
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, Mycobacterium tuberculosis, Cutibacterium acnes
brenda
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
brenda
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