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EC Tree
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.
The enzyme appears in viruses and cellular organisms
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hemH
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hemH
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gene name. HemH and HemQ exist as a fusion protein
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Fe-coproporphyrin III + 2 H+ = coproporphyrin III + Fe2+
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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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coproporphyrin III + Co2+
Co-coproporphyrin III + 2 H+
coproporphyrin III + Cu2+
Cu-coproporphyrin III + 2 H+
coproporphyrin III + Fe2+
Fe-coproporphyrin III + 2 H+
coproporphyrin III + Ni2+
Ni-coproporphyrin III + 2 H+
protoporphyrin + Fe2+
protoheme + 2 H+
protoporphyrin IX + Cu2+
Cu-protoporphyrin IX + 2 H+
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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+
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protoporphyrin IX + Zn2+
Zn protoporphyrin IX
protoporphyrin IX + Zn2+
Zn-protoporphyrin IX + 2 H+
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coproporphyrin III + Co2+
Co-coproporphyrin III + 2 H+
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specific activity with Co2+ is 6fold higher than with Fe2+
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coproporphyrin III + Co2+
Co-coproporphyrin III + 2 H+
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specific activity with Co2+ is 2.8fold higher than with Fe2+
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coproporphyrin III + Cu2+
Cu-coproporphyrin III + 2 H+
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specific activity with Cu2+ is 4.15old higher than with Fe2+
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coproporphyrin III + Cu2+
Cu-coproporphyrin III + 2 H+
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specific activity with Cu2+ is 5.35old higher than with Fe2+
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coproporphyrin III + Fe2+
Fe-coproporphyrin III + 2 H+
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coproporphyrin III + Fe2+
Fe-coproporphyrin III + 2 H+
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coproporphyrin III + Fe2+
Fe-coproporphyrin III + 2 H+
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coproporphyrin III + Ni2+
Ni-coproporphyrin III + 2 H+
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specific activity with Ni2+ is 4fold lower than with Fe2+
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coproporphyrin III + Ni2+
Ni-coproporphyrin III + 2 H+
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specific activity with Ni2+ is 80% compared to activity with Fe2+
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protoporphyrin + Fe2+
protoheme + 2 H+
i.e. reaction of EC 4.99.1.1
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protoporphyrin + Fe2+
protoheme + 2 H+
i.e. reaction of EC 4.99.1.1
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protoporphyrin IX + Zn2+
Zn protoporphyrin IX
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protoporphyrin IX + Zn2+
Zn protoporphyrin IX
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coproporphyrin III + Fe2+
Fe-coproporphyrin III + 2 H+
coproporphyrin III + Fe2+
Fe-coproporphyrin III + 2 H+
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coproporphyrin III + Fe2+
Fe-coproporphyrin III + 2 H+
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coproporphyrin III + Fe2+
Fe-coproporphyrin III + 2 H+
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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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0.0018 - 0.0105
coproporphyrin III
0.008
protoporphyrin IX
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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+
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pH 7.2, 30°C
0.0018
coproporphyrin III
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pH 7.5, 37°C
0.0105
coproporphyrin III
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pH 7.5, 37°C
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0.0078 - 0.03
coproporphyrin III
0.4
protoporphyrin IX
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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
0.0078
coproporphyrin III
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pH 7.5, 37°C
0.03
coproporphyrin III
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pH 7.5, 37°C
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2.9 - 4.3
coproporphyrin III
2.9
coproporphyrin III
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pH 7.5, 37°C
4.3
coproporphyrin III
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pH 7.5, 37°C
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6.5 - 8
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pH 6.5: about 50% of maximal activity, pH 8.0: about 50% of maximal activity
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brenda
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SwissProt
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SwissProt
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metabolism
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the enzyme participates in heme biosynthesis
metabolism
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the enzyme catalyzes the terminal step in heme biosynthesis
metabolism
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the enzyme catalyzes the terminal step in heme biosynthesis
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physiological function
a hemH mutant primarily accumulates protoporphyrin IX
physiological function
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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
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a hemH mutant primarily accumulates protoporphyrin IX
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35348
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35348
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1 * 35348, calculated from sequence
40500
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40500
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1 * 40500, SDS-PAGE
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x * 40500, SDS-PAGE, x * 35348, calculated
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x * 40500, SDS-PAGE, x * 35348, calculated
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monomer
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1 * 40500, SDS-PAGE
monomer
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1 * 35348, calculated from sequence
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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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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
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-20°C, the purified enzyme is stable for at least five months
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expression in Escherichia coli
gene cloned in pUC18, expression in Escherichia coli JM109/pLUGlSe2
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Hansson, M.; Hederstedt, L.
Purification and characterisation of a water-soluble ferrochelatase from Bacillus subtilis
Eur. J. Biochem.
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201-208
1994
Bacillus subtilis
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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)
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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
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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)
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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
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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
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Enzyme Nomenclature
4.99.1.9 coproporphyrin ferrochelatase
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