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Information on EC 1.3.3.15 - coproporphyrinogen III oxidase (coproporphyrin-forming) and Organism(s) Bacillus subtilis and UniProt Accession P32397
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1.3.3.15 coproporphyrinogen III oxidase (coproporphyrin-forming)IUBMB Comments
Contains FAD. The enzyme, present in Gram-positive bacteria, participates in heme biosynthesis. It can also catalyse the reaction of EC 1.3.3.4, protoporphyrinogen oxidase, at a lower level.
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The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
CgoX, coproporphyrinogen III oxidase, coproporphyrinogen oxidase, hemY, PPO, proto'gen oxidase, protoporphyrinogen IX oxidase, protoporphyrinogen oxidase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
hemY
hemY
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
coproporphyrinogen-III:oxygen oxidoreductase (coproporphyrin-forming)
Contains FAD. The enzyme, present in Gram-positive bacteria, participates in heme biosynthesis. It can also catalyse the reaction of EC 1.3.3.4, protoporphyrinogen oxidase, at a lower level.
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
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
-
-
-
-
?
additional information
?
-
-
the enzyme does not oxidize uroporphyrinogen III
-
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
20fold lower activity with protoporphyrinogen IX compared to coproporphyrinogen III
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
-
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
12fold higher catalytic efficiency with coproporphyrinogen III compared to protoporphyrinogen as substrate
-
-
?
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
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
-
-
-
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
20fold lower activity with protoporphyrinogen IX compared to coproporphyrinogen III
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
-
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
12fold higher catalytic efficiency with coproporphyrinogen III compared to protoporphyrinogen as substrate
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
protoporphyrinogen IX
-
acts as a competitive inhibitor of the coproporphyrinogen III to coproporphyrin oxidase activity of HemY
additional information
-
the enzyme is not inhibited by the diphenyl ether herbicide acifluorfen at 0.1 mM
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03774
acifluorfen
wild type enzyme at pH 7.5, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
-
the enzyme is required for a late step in protoheme IX synthesis
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with acifluorfen, sitting drop vapor diffusion method, using 2.4 M ammonium phosphate dibasic, 0.1 M Tris-HCl pH 7.5
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F227R
the mutant exhibits slight decrease in catalysis compared to the wild type enzyme
I176A
the mutation leads to about 30fold decrease in catalytic efficiency compared to the wild type enzyme
K71A
the mutation leads to about 50fold decrease in catalytic efficiency compared to the wild type enzyme
P64A
the mutant exhibits a 14fold decrease in catalysis compared to the wild type enzyme
Y366N
the mutation leads to about 100fold decrease in catalytic efficiency compared to the wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the enzyme gene is fused in its 3'-end to a polynucleotide encoding six histidine residues and expressed in both Escherichia coli BL21(DE3) cells and Bacillus subtilis 168A cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Corrigall, A.V.; Siziba, K.B.; Maneli, M.H.; Shephard, E.G.; Ziman, M.; Dailey, T.A.; Dailey, H.A.; Kirsch, R.E.; Meissner, P.N.
Purification of and kinetic studies on a cloned protoporphyrinogen oxidase from the aerobic bacterium Bacillus subtilis
Arch. Biochem. Biophys.
358
251-256
1998
Bacillus subtilis
Qin, X.; Sun, L.; Wen, X.; Yang, X.; Tan, Y.; Jin, H.; Cao, Q.; Zhou, W.; Xi, Z.; Shen, Y.
Structural insight into unique properties of protoporphyrinogen oxidase from Bacillus subtilis
J. Struct. Biol.
170
76-82
2010
Bacillus subtilis (P32397), Bacillus subtilis 168 (P32397)
Hansson, M.; Gustafsson, M.C.; Kannangara, C.G.; Hederstedt, L.
Isolated Bacillus subtilis HemY has coproporphyrinogen III to coproporphyrin III oxidase activity
Biochim. Biophys. Acta
1340
97-104
1997
Bacillus subtilis (P32397), Bacillus subtilis 168 (P32397)
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, Bacillus subtilis 3G18
Hansson, M.; Hederstedt, L.
Bacillus subtilis HemY is a peripheral membrane protein essential for protoheme IX synthesis which can oxidize coproporphyrinogen III and protoporphyrinogen IX
J. Bacteriol.
176
5962-5970
1994
Bacillus subtilis, Bacillus subtilis 3G18
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
Surdel, M.C.; Horvath, D.J.; Lojek, L.J.; Fullen, A.R.; Simpson, J.; Dutter, B.F.; Salleng, K.J.; Ford, J.B.; Jenkins, J.L.; Nagarajan, R.; Teixeira, P.L.; Albertolle, M.; Georgiev, I.S.; Jansen, E.D.; Sulikowski, G.A.; Lacy, D.B.; Dailey, H.A.; Skaar, E.P.
Antibacterial photosensitization through activation of coproporphyrinogen oxidase
Proc. Natl. Acad. Sci. USA
114
E6652-E6659
2017
Bacillus anthracis, Bacillus subtilis, Cutibacterium acnes, Staphylococcus aureus, Staphylococcus aureus USA300, Staphylococcus epidermidis, Staphylococcus haemolyticus, Staphylococcus lugdunensis
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