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coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
coproporphyrinogen III + O2
coproporphyrin III + H2O
mesoporphyrinogen IX + O2
mesoporphyrin IX + H2O
-
-
-
-
?
protoporphyrinogen IX + 3 O2
protoporphyrin IX + 3 H2O2
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
additional information
?
-
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
-
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
12fold higher catalytic efficiency with coproporphyrinogen III compared to protoporphyrinogen as substrate
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
-
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
12fold higher catalytic efficiency with coproporphyrinogen III compared to protoporphyrinogen as substrate
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
-
-
-
?
protoporphyrinogen IX + 3 O2
protoporphyrin IX + 3 H2O2
-
-
-
?
protoporphyrinogen IX + 3 O2
protoporphyrin IX + 3 H2O2
-
-
-
?
protoporphyrinogen IX + 3 O2
protoporphyrin IX + 3 H2O2
-
-
-
?
protoporphyrinogen IX + 3 O2
protoporphyrin IX + 3 H2O2
-
-
-
?
protoporphyrinogen IX + 3 O2
protoporphyrin IX + 3 H2O2
-
-
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
-
-
-
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
-
-
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
20fold lower activity with protoporphyrinogen IX compared to coproporphyrinogen III
-
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
20fold lower activity with protoporphyrinogen IX compared to coproporphyrinogen III
-
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
-
-
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
-
-
-
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
-
-
-
-
?
additional information
?
-
-
the enzyme does not oxidize uroporphyrinogen III
-
-
?
additional information
?
-
-
the enzyme does not oxidize uroporphyrinogen III
-
-
?
additional information
?
-
-
the enzyme cannot oxidize protoporphyrinogen IX
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
coproporphyrinogen III + O2
coproporphyrin III + H2O
mesoporphyrinogen IX + O2
mesoporphyrin IX + H2O
-
-
-
-
?
protoporphyrinogen IX + 3 O2
protoporphyrin IX + 3 H2O2
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
-
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
12fold higher catalytic efficiency with coproporphyrinogen III compared to protoporphyrinogen as substrate
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
-
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
12fold higher catalytic efficiency with coproporphyrinogen III compared to protoporphyrinogen as substrate
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
-
-
-
?
protoporphyrinogen IX + 3 O2
protoporphyrin IX + 3 H2O2
-
-
-
?
protoporphyrinogen IX + 3 O2
protoporphyrin IX + 3 H2O2
-
-
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
-
-
-
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
-
-
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
20fold lower activity with protoporphyrinogen IX compared to coproporphyrinogen III
-
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
20fold lower activity with protoporphyrinogen IX compared to coproporphyrinogen III
-
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
-
-
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
-
-
-
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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
K71A
-
the mutation leads to about 50fold decrease in catalytic efficiency compared to the wild type enzyme
-
F187W
-
the mutation inhibits the activation of the enzyme by VU0038882
M167F
-
the mutation inhibits the activation of the enzyme by VU0038882
N186F
-
the mutant exhibits increased baseline activity relative to the wild type enzyme
N186Y
-
the mutant exhibits increased baseline activity relative to the wild type enzyme
T183K
-
the mutation does not restrict enzyme function. The mutant does not respond to VU0038882 at concentrations up to 0.01 mM
F187W
-
the mutation inhibits the activation of the enzyme by VU0038882
-
M167F
-
the mutation inhibits the activation of the enzyme by VU0038882
-
N186F
-
the mutant exhibits increased baseline activity relative to the wild type enzyme
-
N186Y
-
the mutant exhibits increased baseline activity relative to the wild type enzyme
-
T183K
-
the mutation does not restrict enzyme function. The mutant does not respond to VU0038882 at concentrations up to 0.01 mM
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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
brenda
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)
brenda
Hobbs, C.; Dailey, H.A.; Shepherd, M.
The HemQ coprohaem decarboxylase generates reactive oxygen species: implications for the evolution of classical haem biosynthesis
Biochem. J.
473
3997-4009
2016
Staphylococcus aureus
brenda
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)
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, Bacillus subtilis 3G18
brenda
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
brenda
Lobo, S.A.; Scott, A.; Videira, M.A.; Winpenny, D.; Gardner, M.; Palmer, M.J.; Schroeder, S.; Lawrence, A.D.; Parkinson, T.; Warren, M.J.; Saraiva, L.M.
Staphylococcus aureus haem biosynthesis: characterisation of the enzymes involved in final steps of the pathway
Mol. Microbiol.
97
472-487
2015
Staphylococcus aureus
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
brenda
Klimka, A.; Mertins, S.; Nicolai, A.K.; Rummler, L.M.; Higgins, P.G.; Guenther, S.D.; Tosetti, B.; Krut, O.; Kroenke, M.
Epitope-specific immunity against Staphylococcus aureus coproporphyrinogen III oxidase
NPJ Vaccines
6
11
2021
Staphylococcus aureus (A0A3M8V9D3), Staphylococcus aureus USA300 (A0A3M8V9D3)
brenda
Yoon, J.; Han, Y.; Ahn, Y.O.; Hong, M.K.; Sung, S.K.
Characterization of HemY-type protoporphyrinogen IX oxidase genes from cyanobacteria and their functioning in transgenic Arabidopsis
Plant Mol. Biol.
101
561-574
2019
Oscillatoria nigro-viridis (K9VK16), Halothece sp. PCC7418 (K9Y873), Oscillatoria nigro-viridis PCC7112 (K9VK16)
brenda
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, Staphylococcus aureus, Cutibacterium acnes, Staphylococcus epidermidis, Staphylococcus haemolyticus, Staphylococcus lugdunensis, Staphylococcus aureus USA300
brenda