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Fe-coproporphyrin III + 2 H2O2
heme b + 2 CO2 + 4 H2O
Fe-coproporphyrin III + 2 H2O2
protoheme + 2 CO2 + 4 H2O
Fe-coproporphyrin III + H2O2
harderoheme III + CO2 + 2 H2O
-
-
-
?
Fe-coproporphyrin III + H2O2
harderoheme III + CO2 + H2O
Fe-coproporphyrin III + H2O2
protoheme + CO2 + H2O
harderoheme III + H2O2
protoheme + CO2 + 2 H2O
-
-
-
?
harderoheme III + H2O2
protoheme + CO2 + H2O
harderoheme IV + H2O2
protoheme + CO2 + H2O
-
-
-
?
harderoheme IV + peracetic acid
? + CO2 + 2 acetate
-
-
-
?
Mn(III) coproporphyrinate III + H2O2
?
additional information
?
-
Fe-coproporphyrin III + 2 H2O2
heme b + 2 CO2 + 4 H2O
-
-
-
?
Fe-coproporphyrin III + 2 H2O2
heme b + 2 CO2 + 4 H2O
-
-
-
?
Fe-coproporphyrin III + 2 H2O2
protoheme + 2 CO2 + 4 H2O
-
-
-
?
Fe-coproporphyrin III + 2 H2O2
protoheme + 2 CO2 + 4 H2O
-
-
-
?
Fe-coproporphyrin III + 2 H2O2
protoheme + 2 CO2 + 4 H2O
-
-
-
?
Fe-coproporphyrin III + H2O2
harderoheme III + CO2 + H2O
-
-
-
-
?
Fe-coproporphyrin III + H2O2
harderoheme III + CO2 + H2O
-
-
-
-
?
Fe-coproporphyrin III + H2O2
harderoheme III + CO2 + H2O
-
-
-
?
Fe-coproporphyrin III + H2O2
harderoheme III + CO2 + H2O
-
-
-
?
Fe-coproporphyrin III + H2O2
harderoheme III + CO2 + H2O
-
-
-
?
Fe-coproporphyrin III + H2O2
harderoheme III + CO2 + H2O
-
-
-
?
Fe-coproporphyrin III + H2O2
harderoheme III + CO2 + H2O
-
-
-
-
?
Fe-coproporphyrin III + H2O2
harderoheme III + CO2 + H2O
-
-
-
?
Fe-coproporphyrin III + H2O2
harderoheme III + CO2 + H2O
-
-
-
-
?
Fe-coproporphyrin III + H2O2
protoheme + CO2 + H2O
-
overall reaction
-
-
?
Fe-coproporphyrin III + H2O2
protoheme + CO2 + H2O
-
overall reaction
-
-
?
Fe-coproporphyrin III + H2O2
protoheme + CO2 + H2O
overall reaction
-
-
?
Fe-coproporphyrin III + H2O2
protoheme + CO2 + H2O
overall reaction
-
-
?
Fe-coproporphyrin III + H2O2
protoheme + CO2 + H2O
overall reaction
-
-
?
Fe-coproporphyrin III + H2O2
protoheme + CO2 + H2O
overall reaction
-
-
?
Fe-coproporphyrin III + H2O2
protoheme + CO2 + H2O
-
overall reaction
-
-
?
Fe-coproporphyrin III + H2O2
protoheme + CO2 + H2O
overall reaction
-
-
?
Fe-coproporphyrin III + H2O2
protoheme + CO2 + H2O
-
overall reaction
-
-
?
harderoheme III + H2O2
protoheme + CO2 + H2O
-
-
-
-
?
harderoheme III + H2O2
protoheme + CO2 + H2O
-
-
-
-
?
harderoheme III + H2O2
protoheme + CO2 + H2O
-
-
-
?
harderoheme III + H2O2
protoheme + CO2 + H2O
-
-
-
?
harderoheme III + H2O2
protoheme + CO2 + H2O
-
-
-
?
harderoheme III + H2O2
protoheme + CO2 + H2O
-
-
-
?
harderoheme III + H2O2
protoheme + CO2 + H2O
-
-
-
-
?
harderoheme III + H2O2
protoheme + CO2 + H2O
-
-
-
?
harderoheme III + H2O2
protoheme + CO2 + H2O
-
-
-
-
?
Mn(III) coproporphyrinate III + H2O2
?
coproporphyrinate III = tetrakis-2,4,6,7-propionate-protoporphyrin
-
-
?
Mn(III) coproporphyrinate III + H2O2
?
coproporphyrinate III = tetrakis-2,4,6,7-propionate-protoporphyrin
-
-
?
additional information
?
-
-
HemQ additionally possesses minimal peroxidase activity, and as a catalase it has a turnover of over 10000 per min
-
-
?
additional information
?
-
heme binding is reversible with KD-values of 7.2 microM (by circular dichroism spectroscopy) and 16.8 microM (by isothermal titration calorimetry) at pH 7.0. Heme-binding is a cooperative process with Hill coefficients between 1.6 and 1.8
-
-
?
additional information
?
-
heme binding is reversible with KD-values of 7.2 microM (by circular dichroism spectroscopy) and 16.8 microM (by isothermal titration calorimetry) at pH 7.0. Heme-binding is a cooperative process with Hill coefficients between 1.6 and 1.8
-
-
?
additional information
?
-
-
HemQ additionally possesses minimal peroxidase activity, and as a catalase it has a turnover of over 10000 per min
-
-
?
additional information
?
-
-
no activity with meta-chloroperbenzoic acid or tert-butyl-peroxide
-
-
?
additional information
?
-
no activity with meta-chloroperbenzoic acid or tert-butyl-peroxide
-
-
?
additional information
?
-
in the absence of H2O2, HemQ converts only around 1% of Fe-coproporphyrin III into protoheme IX
-
-
?
additional information
?
-
-
HemQ additionally possesses minimal peroxidase activity, and as a catalase it has a turnover of over 10000 per min
-
-
?
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Fe-coproporphyrin III + 2 H2O2
protoheme + 2 CO2 + 4 H2O
-
-
-
?
Fe-coproporphyrin III + H2O2
harderoheme III + CO2 + H2O
Fe-coproporphyrin III + H2O2
protoheme + CO2 + H2O
harderoheme III + H2O2
protoheme + CO2 + H2O
harderoheme IV + H2O2
protoheme + CO2 + H2O
-
-
-
?
Fe-coproporphyrin III + H2O2
harderoheme III + CO2 + H2O
-
-
-
-
?
Fe-coproporphyrin III + H2O2
harderoheme III + CO2 + H2O
-
-
-
-
?
Fe-coproporphyrin III + H2O2
harderoheme III + CO2 + H2O
-
-
-
?
Fe-coproporphyrin III + H2O2
harderoheme III + CO2 + H2O
-
-
-
?
Fe-coproporphyrin III + H2O2
harderoheme III + CO2 + H2O
-
-
-
?
Fe-coproporphyrin III + H2O2
harderoheme III + CO2 + H2O
-
-
-
?
Fe-coproporphyrin III + H2O2
harderoheme III + CO2 + H2O
-
-
-
-
?
Fe-coproporphyrin III + H2O2
harderoheme III + CO2 + H2O
-
-
-
?
Fe-coproporphyrin III + H2O2
harderoheme III + CO2 + H2O
-
-
-
-
?
Fe-coproporphyrin III + H2O2
protoheme + CO2 + H2O
-
overall reaction
-
-
?
Fe-coproporphyrin III + H2O2
protoheme + CO2 + H2O
-
overall reaction
-
-
?
Fe-coproporphyrin III + H2O2
protoheme + CO2 + H2O
overall reaction
-
-
?
Fe-coproporphyrin III + H2O2
protoheme + CO2 + H2O
overall reaction
-
-
?
Fe-coproporphyrin III + H2O2
protoheme + CO2 + H2O
overall reaction
-
-
?
Fe-coproporphyrin III + H2O2
protoheme + CO2 + H2O
overall reaction
-
-
?
Fe-coproporphyrin III + H2O2
protoheme + CO2 + H2O
-
overall reaction
-
-
?
Fe-coproporphyrin III + H2O2
protoheme + CO2 + H2O
overall reaction
-
-
?
Fe-coproporphyrin III + H2O2
protoheme + CO2 + H2O
-
overall reaction
-
-
?
harderoheme III + H2O2
protoheme + CO2 + H2O
-
-
-
-
?
harderoheme III + H2O2
protoheme + CO2 + H2O
-
-
-
-
?
harderoheme III + H2O2
protoheme + CO2 + H2O
-
-
-
?
harderoheme III + H2O2
protoheme + CO2 + H2O
-
-
-
?
harderoheme III + H2O2
protoheme + CO2 + H2O
-
-
-
?
harderoheme III + H2O2
protoheme + CO2 + H2O
-
-
-
?
harderoheme III + H2O2
protoheme + CO2 + H2O
-
-
-
-
?
harderoheme III + H2O2
protoheme + CO2 + H2O
-
-
-
?
harderoheme III + H2O2
protoheme + CO2 + H2O
-
-
-
-
?
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metabolism
-
the enzyme, along with the terminal two pathway enzymes protoporphyrinogen oxidase HemY and ferrochelatase is required to synthesize heme in vivo and in vitro
metabolism
-
the enzyme, along with the terminal two pathway enzymes protoporphyrinogen oxidase HemY and ferrochelatase is required to synthesize heme in vivo and in vitro
metabolism
-
the enzyme, along with the terminal two pathway enzymes protoporphyrinogen oxidase HemY and ferrochelatase is required to synthesize heme in vivo and in vitro
metabolism
-
the enzyme, along with the terminal two pathway enzymes protoporphyrinogen oxidase HemY and ferrochelatase is required to synthesize heme in vivo and in vitro
physiological function
-
Actinobacteria and Firmicutes (high-GC and low-GC Gram-positive bacteria) are unable to synthesize protoporphyrin. Instead, they oxidize coproporphyrinogen to coproporphyrin, insert ferrous iron to make Fe-coproporphyrin (coproheme), and then decarboxylate coproheme to generate protoheme. This pathway is specified by three genes named hemY, hemH, and hemQ and is the most ancient heme synthesis pathway in the Eubacteria
physiological function
enzymes HemY, HemH and HemQ act as a coproporphyrinogen III oxidase, coproporphyrin III ferrochelatase and Fe-coproporphyrin III oxidase/dehydrogenase
physiological function
HemQ can stimulate the generation of protoporphyrin IX but not coproporphyrin III
physiological function
-
the presence of HemQ along with the terminal two pathway enzymes, protoporphyrinogen oxidase (HemY) and ferrochelatase, is required to synthesize heme in vivo and in vitro. To be fully functional in vitro, HemQ requires the presence of a bound heme
physiological function
-
the presence of HemQ along with the terminal two pathway enzymes, protoporphyrinogen oxidase (HemY) and ferrochelatase, is required to synthesize heme in vivo and in vitro. To be fully functional in vitro, HemQ requires the presence of a bound heme
physiological function
-
the presence of HemQ along with the terminal two pathway enzymes, protoporphyrinogen oxidase (HemY) and ferrochelatase, is required to synthesize heme in vivo and in vitro. To be fully functional in vitro, HemQ requires the presence of a bound heme
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CHDC_LISMF
Listeria monocytogenes serotype 4b (strain F2365)
251
0
28850
Swiss-Prot
-
CHDC_LISMH
Listeria monocytogenes serotype 4a (strain HCC23)
251
0
28866
Swiss-Prot
-
CHDC_LISMO
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
251
0
28852
Swiss-Prot
-
CHDC_LISW6
Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / CIP 8149 / NCTC 11857 / SLCC 5334 / V8)
251
0
28854
Swiss-Prot
-
CHDC_MYCS2
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
231
0
26305
Swiss-Prot
-
CHDC_MYCTO
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
231
0
26250
Swiss-Prot
-
CHDC_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
231
0
26250
Swiss-Prot
-
CHDC_OCEIH
Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831)
249
0
29154
Swiss-Prot
-
CHDC_STAA1
Staphylococcus aureus (strain Mu3 / ATCC 700698)
250
0
29390
Swiss-Prot
-
CHDC_STAA2
Staphylococcus aureus (strain JH1)
250
0
29390
Swiss-Prot
-
CHDC_STAA3
Staphylococcus aureus (strain USA300)
250
0
29390
Swiss-Prot
-
CHDC_STAA8
Staphylococcus aureus (strain NCTC 8325 / PS 47)
250
0
29390
Swiss-Prot
-
CHDC_STAA9
Staphylococcus aureus (strain JH9)
250
0
29390
Swiss-Prot
-
CHDC_STAAB
Staphylococcus aureus (strain bovine RF122 / ET3-1)
250
0
29328
Swiss-Prot
-
CHDC_STAAC
Staphylococcus aureus (strain COL)
250
0
29390
Swiss-Prot
-
CHDC_STAAE
Staphylococcus aureus (strain Newman)
250
0
29390
Swiss-Prot
-
CHDC_STAAM
250
0
29390
Swiss-Prot
-
CHDC_STAAN
250
0
29390
Swiss-Prot
-
CHDC_STAAR
Staphylococcus aureus (strain MRSA252)
250
0
29389
Swiss-Prot
-
CHDC_STAAS
Staphylococcus aureus (strain MSSA476)
250
0
29390
Swiss-Prot
-
CPFCB_CUTAK
Cutibacterium acnes (strain DSM 16379 / KPA171202)
683
0
74065
Swiss-Prot
-
CHDC_STAAT
Staphylococcus aureus (strain USA300 / TCH1516)
250
0
29390
Swiss-Prot
-
CHDC_STAAW
250
0
29390
Swiss-Prot
-
CHDC_STACT
Staphylococcus carnosus (strain TM300)
249
0
29406
Swiss-Prot
-
CHDC_STAEQ
Staphylococcus epidermidis (strain ATCC 35984 / RP62A)
249
0
29541
Swiss-Prot
-
CHDC_STAES
Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200)
249
0
29585
Swiss-Prot
-
CHDC_STAHJ
Staphylococcus haemolyticus (strain JCSC1435)
249
0
29631
Swiss-Prot
-
CHDC_STAS1
Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41)
249
0
29282
Swiss-Prot
-
CHDC_STRCO
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
243
0
28132
Swiss-Prot
-
CHDC_THET2
Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)
249
0
28906
Swiss-Prot
-
CHDC_THET8
Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
249
0
28906
Swiss-Prot
-
CHDC_BACC1
Bacillus cereus (strain ATCC 10987 / NRS 248)
247
0
28682
Swiss-Prot
-
CHDC_BACC2
Bacillus cereus (strain G9842)
247
0
28696
Swiss-Prot
-
CHDC_BACC3
Bacillus cereus (strain 03BB102)
247
0
28652
Swiss-Prot
-
CHDC_BACC4
Bacillus cereus (strain B4264)
247
0
28696
Swiss-Prot
-
CHDC_BACC7
Bacillus cereus (strain AH187)
247
0
28652
Swiss-Prot
-
CHDC_BACCN
Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98)
247
0
28795
Swiss-Prot
-
CHDC_BACCQ
Bacillus cereus (strain Q1)
247
0
28652
Swiss-Prot
-
CHDC_BACCR
Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711)
247
0
28696
Swiss-Prot
-
CHDC_BACCZ
Bacillus cereus (strain ZK / E33L)
247
0
28652
Swiss-Prot
-
CHDC_BACHK
Bacillus thuringiensis subsp. konkukian (strain 97-27)
247
0
28652
Swiss-Prot
-
CHDC_BACLD
Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46)
254
0
29395
Swiss-Prot
-
CHDC_BACMK
Bacillus mycoides (strain KBAB4)
247
0
28678
Swiss-Prot
-
CHDC_BACSU
Bacillus subtilis (strain 168)
254
0
29505
Swiss-Prot
-
CHDC_BACVZ
Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
254
0
29485
Swiss-Prot
-
CHDC_GEOKA
Geobacillus kaustophilus (strain HTA426)
248
0
28769
Swiss-Prot
-
CHDC_GEOS3
Geobacillus stearothermophilus (strain DSM 13240 / CIP 106956 / 10)
248
0
28787
Swiss-Prot
-
CHDC_GEOSW
Geobacillus sp. (strain WCH70)
248
0
28870
Swiss-Prot
-
CHDC_GEOTN
Geobacillus thermodenitrificans (strain NG80-2)
248
0
28865
Swiss-Prot
-
CHDC_LISIN
Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262)
251
0
28836
Swiss-Prot
-
CHDC_LISMC
Listeria monocytogenes serotype 4b (strain CLIP80459)
251
0
28850
Swiss-Prot
-
CHDC_ALKCK
Alkalihalobacillus clausii (strain KSM-K16)
249
0
29065
Swiss-Prot
-
CHDC_ALKHC
Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
249
0
28942
Swiss-Prot
-
CHDC_BACAA
Bacillus anthracis (strain A0248)
247
0
28652
Swiss-Prot
-
CHDC_BACAC
Bacillus anthracis (strain CDC 684 / NRRL 3495)
247
0
28652
Swiss-Prot
-
CHDC_BACAH
Bacillus thuringiensis (strain Al Hakam)
247
0
28652
Swiss-Prot
-
CHDC_BACAN
247
0
28652
Swiss-Prot
-
CHDC_BACC0
Bacillus cereus (strain AH820)
247
0
28666
Swiss-Prot
-
A0A0S3DY11_STAAU
250
0
29390
TrEMBL
-
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K151A
disruption of the H-bond interactions with p2 and p4, impairs the structural rearrangement upon binding of coproheme. Decarboxylation activity is highly impaired
M149A
mutation alters the heme coordination, which becomes a 6-coordinate low spin species with the amide nitrogen atom of the Q187 residue bound to the heme iron. In the mutant, two CO conformers are present corresponding to open (A0) and closed (A1) conformations. Residue M149 is involved in the formation of a covalent bond with a vinyl substituent of heme b at excess of hydrogen peroxide
M149A/Q187A
binding of coproheme is significantly decreased. In the absence of the Q187, only the A0 conformer is found
R133A
catalytic activity similar to wild-type
R179A
catalytic activity similar to wild-type
Y113A
catalytic activity similar to wild-type
Y113A/K151A
disruption of the H-bond interactions with p2 and p4, impairs the structural rearrangement upon binding of coproheme
Y147A
mutant is completely inactive
Y147A/R220A/S225A
mutations affect the extended H-bond network spanning from p2 to p4
K151A
-
disruption of the H-bond interactions with p2 and p4, impairs the structural rearrangement upon binding of coproheme. Decarboxylation activity is highly impaired
-
M149A
-
mutation alters the heme coordination, which becomes a 6-coordinate low spin species with the amide nitrogen atom of the Q187 residue bound to the heme iron. In the mutant, two CO conformers are present corresponding to open (A0) and closed (A1) conformations. Residue M149 is involved in the formation of a covalent bond with a vinyl substituent of heme b at excess of hydrogen peroxide
-
M149A/Q187A
-
binding of coproheme is significantly decreased. In the absence of the Q187, only the A0 conformer is found
-
Q187A
-
in the absence of the Q187, only the A0 conformer is found compared to two CO conformers are present corresponding to open (A0) and closed (A1) conformations in mutant M149A
-
R133A
-
catalytic activity similar to wild-type
-
R179A
-
catalytic activity similar to wild-type
-
Y113A
-
catalytic activity similar to wild-type
-
Y147A
-
mutant is completely inactive
-
H156A
-
the mutant shows less than 10% of wild type activity
H156C
-
the mutant shows less than 10% of wild type activity
Q187A
catalytic activity similar to wild-type
Q187A
in the absence of the Q187, only the A0 conformer is found compared to two CO conformers are present corresponding to open (A0) and closed (A1) conformations in mutant M149A
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Celis, A.I.; Streit, B.R.; Moraski, G.C.; Kant, R.; Lash, T.D.; Lukat-Rodgers, G.S.; Rodgers, K.R.; DuBois, J.L.
Unusual peroxide-dependent, heme-transforming reaction catalyzed by HemQ
Biochemistry
54
4022-4032
2015
Staphylococcus aureus, Staphylococcus aureus (A0A0S3DY11)
brenda
Hofbauer, S.; Mlynek, G.; Milazzo, L.; Puehringer, D.; Maresch, D.; Schaffner, I.; Furtmueller, P.G.; Smulevich, G.; Djinovic-Carugo, K.; Obinger, C.
Hydrogen peroxide-mediated conversion of coproheme to heme b by HemQ-lessons from the first crystal structure and kinetic studies
FEBS J.
283
4386-4401
2016
Listeria monocytogenes (Q8Y5F1), Listeria monocytogenes serotype 1/2a (Q8Y5F1), Listeria monocytogenes ATCC BAA-679 (Q8Y5F1), Listeria monocytogenes serotype 1/2a ATCC BAA-679 (Q8Y5F1)
brenda
Celis, A.I.; Gauss, G.H.; Streit, B.R.; Shisler, K.; Moraski, G.C.; Rodgers, K.R.; Lukat-Rodgers, G.S.; Peters, J.W.; DuBois, J.L.
A structure-based mechanism for oxidative decarboxylation reactions mediated by amino acids and heme propionates in coproheme decarboxylase (HemQ)
J. Am. Chem. Soc.
139
1900-1911
2017
Geobacillus stearothermophilus (A0A0K2H9D8), Geobacillus stearothermophilus 10 (A0A0K2H9D8)
brenda
Dailey, T.A.; Boynton, T.O.; Albetel, A.N.; Gerdes, S.; Johnson, M.K.; Dailey, H.A.
Discovery and characterization of HemQ an essential heme biosynthetic pathway component
J. Biol. Chem.
285
25978-25986
2010
Bacillus subtilis, Mycobacterium tuberculosis, Cutibacterium acnes, Streptomyces coelicolor
brenda
Hofbauer, S.; Hagmueller, A.; Schaffner, I.; Mlynek, G.; Krutzler, M.; Stadlmayr, G.; Pirker, K.; Obinger, C.; Daims, H.; Djinovic-Carugo, K.; Furtmueller, P.
Structure and heme-binding properties of HemQ (chlorite dismutase-like protein) from Listeria monocytogenes
Arch. Biochem. Biophys.
574
36-48
2015
Listeria monocytogenes serotype 1/2a (Q8Y5F1), Listeria monocytogenes serotype 1/2a ATCC BAA-679 (Q8Y5F1)
brenda
Hobbs, C.; Dailey, H.; 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 (A0A0S3DY11)
brenda
Milazzo, L.; Hofbauer, S.; Howes, B.D.; Gabler, T.; Furtmueller, P.G.; Obinger, C.; Smulevich, G.
Insights into the active site of coproheme decarboxylase from Listeria monocytogenes
Biochemistry
57
2044-2057
2018
Listeria monocytogenes serotype 1/2a (Q8Y5F1), Listeria monocytogenes serotype 1/2a ATCC BAA-679 (Q8Y5F1)
brenda
Milazzo, L.; Gabler, T.; Pfanzagl, V.; Michlits, H.; Furtmueller, P.G.; Obinger, C.; Hofbauer, S.; Smulevich, G.
The hydrogen bonding network of coproheme in coproheme decarboxylase from Listeria monocytogenes Effect on structure and catalysis
J. Inorg. Biochem.
195
61-70
2019
Listeria monocytogenes serotype 1/2a (Q8Y5F1), Listeria monocytogenes serotype 1/2a ATCC BAA-679 (Q8Y5F1)
brenda
Lobo, S.; Scott, A.; Videira, M.; Winpenny, D.; Gardner, M.; Palmer, M.; Schroeder, S.; Lawrence, A.; Parkinson, T.; Warren, M.; Saraiva, L.
Staphylococcus aureus haem biosynthesis Characterisation of the enzymes involved in final steps of the pathway
Mol. Microbiol.
97
472-487
2015
Staphylococcus aureus (A0A0S3DY11)
brenda
Dailey, H.; Gerdes, S.; Dailey, T.; Burch, J.; Phillips, J.
Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin
Proc. Natl. Acad. Sci. USA
112
2210-2215
2015
Firmicutes
brenda