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Ligand coproporphyrinogen III

Basic Ligand Information

Molecular Structure

Related pathways

Pathway Source

Pathways

BRENDA

heme metabolism

KEGG

Biosynthesis of cofactors, Biosynthesis of secondary metabolites, Porphyrin metabolism

MetaCyc

3,8-divinyl-chlorophyllide a biosynthesis I (aerobic, light-dependent), 3,8-divinyl-chlorophyllide a biosynthesis II (anaerobic), 3,8-divinyl-chlorophyllide a biosynthesis III (aerobic, light independent), heme b biosynthesis I (aerobic), heme b biosynthesis II (oxygen-independent), heme b biosynthesis IV (Gram-positive bacteria), heme b biosynthesis V (aerobic) more

Show all BRENDA pathways known for coproporphyrinogen III

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (14 results)

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Show Natural Substrate (14 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.3.15

coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2

765676, 765480

-

1.3.3.15

coproporphyrinogen III + O2 = coproporphyrin III + H2O

737655, 737734, 738499, 738501, 739107, 739547, 391011, 712895

-

1.3.3.3

coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen IX + 2 CO2 + 2 H2O

713182, 712835, 713258, 697204

-

1.3.3.3

coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O

725779, 724548, 712835, 713182, 744139, 745239, 745755, 765393, 763898, 764514, 765391, 764113, 764783, 765045, 746121

-

1.3.3.3

coproporphyrinogen III + O2 + H+ = protoporphyrinogen IX + CO2 + H2O

726153

-

1.3.3.3

coproporphyrinogen III + O2 = coproporphyrin III + H2O

738987, 672533

-

1.3.3.3

coproporphyrinogen-III + 2 NADP+ = protoporphyrinogen-IX + 2 CO2 + 2 NADPH + 2 H+

390974, 390975

-

1.3.3.3

coproporphyrinogen-III + ? = protoporphyrinogen-IX + ?

390963, 390962, 390976, 390975

-

1.3.3.3

coproporphyrinogen-III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O

390944, 390950, 390958, 390973, 390954, 390952, 390953, 390947, 390945, 390948, 390951, 390979, 390949, 390965, 390966, 390962, 390975, 390976, 390946, 390978, 390963, 390959, 390968, 390969, 390971, 390980, 390961, 390955, 390960, 390970, 390974, 390964, 390977, 390967, 390956, 390957, 390943

-

1.3.3.3

coproporphyrinogen-III + O2 = protoporphyrinogen-IX + 2 CO2 + 2 H2O

656245

-

1.3.3.3

coproporphyrinogen-III + O2 = protoporphyrinogen-IX + CO2 + H2O

654966, 656175, 654975, 657084, 654965, 656432, 655119

-

1.3.98.3

coproporphyrinogen III + 2 S-adenosyl-L-methionine = protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine

713258, 711348, 712016, 726009, 765437, 763891

-

1.3.98.3

coproporphyrinogen III + S-adenosyl-L-methionine = protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine

739104

-

1.3.98.3

coproporphyrinogen-III + S-adenosyl-L-methionine = protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine

658501, 655340

-

1.3.3.15

2 entries

1.3.3.3

9 entries

1.3.98.3

3 entries

In Vivo Product in Enzyme-catalyzed Reactions (12 results)

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Show Natural Product (12 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

4.1.1.37

Uroporphyrinogen III = Coproporphyrinogen III + 4 CO2

650726, 651526, 650797, 649782, 650999, 650890, 651454, 649149, 390946, -

1R3T, 3D-view

4.1.1.37

Uroporphyrinogen III = Coproporphyrinogen III + 4 CO2

650726, 651526, 650797, 649782, 650999, 650890, 651454, 649149, 390946, -

1R3W, 3D-view

4.1.1.37

Uroporphyrinogen III = Coproporphyrinogen III + 4 CO2

650726, 651526, 650797, 649782, 650999, 650890, 651454, 649149, 390946, -

1R3Y, 3D-view

4.1.1.37

Uroporphyrinogen III = Coproporphyrinogen III + 4 CO2

650726, 651526, 650797, 649782, 650999, 650890, 651454, 649149, 390946, -

2Q71, 3D-view

4.1.1.37

uroporphyrinogen-III = coproporphyrinogen-III + 4 CO2

-

1R3T, 3D-view

4.1.1.37

uroporphyrinogen-III = coproporphyrinogen-III + 4 CO2

-

1R3W, 3D-view

4.1.1.37

uroporphyrinogen-III = coproporphyrinogen-III + 4 CO2

-

1R3Y, 3D-view

4.1.1.37

uroporphyrinogen-III = coproporphyrinogen-III + 4 CO2

-

2Q71, 3D-view

4.1.1.37

uroporphyrinogen-III = coproporphyrinogen-III + CO2

652198

1R3T, 3D-view

4.1.1.37

uroporphyrinogen-III = coproporphyrinogen-III + CO2

652198

1R3W, 3D-view

4.1.1.37

uroporphyrinogen-III = coproporphyrinogen-III + CO2

652198

1R3Y, 3D-view

4.1.1.37

uroporphyrinogen-III = coproporphyrinogen-III + CO2

652198

2Q71, 3D-view

4.1.1.37

12 entries

Substrate in Enzyme-catalyzed Reactions (21 results)

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Show Substrate (21 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.3.15

coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2

765676, 765480

-

1.3.3.15

coproporphyrinogen III + O2 = coproporphyrin III + H2O

737655, 737734, 738499, 738501, 739107, 739547, 391011, 712895

-

1.3.3.3

coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen IX + 2 CO2 + 2 H2O

713182, 712835, 713258, 697204

-

1.3.3.3

coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O

725779, 724548, 712835, 713182, 744139, 745239, 745755, 765393, 763898, 764514, 765391, 764113, 764783, 765045, 746121

-

1.3.3.3

coproporphyrinogen III + O2 + H+ = protoporphyrinogen IX + CO2 + H2O

726153

-

1.3.3.3

coproporphyrinogen III + O2 = coproporphyrin III + H2O

738987, 672533

-

1.3.3.3

coproporphyrinogen-III + 2 NADP+ = protoporphyrinogen-IX + 2 CO2 + 2 NADPH + 2 H+

390974, 390975

-

1.3.3.3

coproporphyrinogen-III + ? = protoporphyrinogen-IX + ?

390963, 390962, 390976, 390975, 684418

-

1.3.3.3

coproporphyrinogen-III + O2 + 2 H+ = harderoporphyrinogen + CO2 + 2 H2O

675777

-

1.3.3.3

coproporphyrinogen-III + O2 + 2 H+ = protoporphyrinogen IX + 2 CO2 + 2 H2O

685536

-

1.3.3.3

coproporphyrinogen-III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O

390944, 390950, 390958, 390973, 390954, 390952, 390953, 390947, 390945, 390948, 390951, 390979, 390949, 390965, 390966, 390962, 390975, 390976, 390946, 390978, 390963, 390959, 390968, 390969, 390971, 390980, 390961, 390955, 390960, 390970, 390974, 390964, 390977, 390967, 390956, 390957, 390943, 675776, 672473, 673936, 671195, 672827, 672533, 672822, 690136, 690137, 684418, 685536, 688811, 675777, 701321, 763670

-

1.3.3.3

coproporphyrinogen-III + O2 = protoporphyrinogen-IX + 2 CO2 + 2 H2O

656245

-

1.3.3.3

coproporphyrinogen-III + O2 = protoporphyrinogen-IX + CO2 + H2O

654966, 656175, 654975, 657084, 654965, 656432, 655119, 655624

-

1.3.3.15

2 entries

1.3.3.3

11 entries

1.3.3.4

coproporphyrinogen-III + 3 O2 = coproporphyrin-III + 3 H2O2

391011

-

1.3.98.3

coproporphyrinogen III + 2 S-adenosyl-L-methionine = protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine

713258, 711348, 712016, 726009, 765437, 763891

-

1.3.98.3

coproporphyrinogen III + S-adenosyl-L-methionine = protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine

739104

-

1.3.98.3

coproporphyrinogen-III + S-adenosyl-L-methionine = protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine

658501, 655340, 656073, 674567, 674462, 672473, 686237

-

4.1.1.37

5-COOH-porphyrinogen III = Coproporphyrinogen III + CO2

4420, 4425, 4430, 4440, 4422, 4427

1R3T, 3D-view

4.1.1.37

5-COOH-porphyrinogen III = Coproporphyrinogen III + CO2

4420, 4425, 4430, 4440, 4422, 4427

1R3W, 3D-view

4.1.1.37

5-COOH-porphyrinogen III = Coproporphyrinogen III + CO2

4420, 4425, 4430, 4440, 4422, 4427

1R3Y, 3D-view

4.1.1.37

5-COOH-porphyrinogen III = Coproporphyrinogen III + CO2

4420, 4425, 4430, 4440, 4422, 4427

2Q71, 3D-view

1.3.98.3

3 entries

4.1.1.37

4 entries

Product in Enzyme-catalyzed Reactions (28 results)

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Show Product (28 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

4.1.1.37

5-COOH-porphyrinogen III = Coproporphyrinogen III + CO2

-

1R3T, 3D-view

4.1.1.37

5-COOH-porphyrinogen III = Coproporphyrinogen III + CO2

-

1R3W, 3D-view

4.1.1.37

5-COOH-porphyrinogen III = Coproporphyrinogen III + CO2

-

1R3Y, 3D-view

4.1.1.37

5-COOH-porphyrinogen III = Coproporphyrinogen III + CO2

-

2Q71, 3D-view

4.1.1.37

6-COOH-porphyrinogen III = Coproporphyrinogen III + CO2

-

1R3T, 3D-view

4.1.1.37

6-COOH-porphyrinogen III = Coproporphyrinogen III + CO2

-

1R3W, 3D-view

4.1.1.37

6-COOH-porphyrinogen III = Coproporphyrinogen III + CO2

-

1R3Y, 3D-view

4.1.1.37

6-COOH-porphyrinogen III = Coproporphyrinogen III + CO2

-

2Q71, 3D-view

4.1.1.37

7-COOH-porphyrinogen III = Coproporphyrinogen III + CO2

-

1R3T, 3D-view

4.1.1.37

7-COOH-porphyrinogen III = Coproporphyrinogen III + CO2

-

1R3W, 3D-view

4.1.1.37

7-COOH-porphyrinogen III = Coproporphyrinogen III + CO2

-

1R3Y, 3D-view

4.1.1.37

7-COOH-porphyrinogen III = Coproporphyrinogen III + CO2

-

2Q71, 3D-view

4.1.1.37

8-COOH-porphyrinogen III = Coproporphyrinogen III + CO2

-

1R3T, 3D-view

4.1.1.37

8-COOH-porphyrinogen III = Coproporphyrinogen III + CO2

-

1R3W, 3D-view

4.1.1.37

8-COOH-porphyrinogen III = Coproporphyrinogen III + CO2

-

1R3Y, 3D-view

4.1.1.37

8-COOH-porphyrinogen III = Coproporphyrinogen III + CO2

-

2Q71, 3D-view

4.1.1.37

Uroporphyrinogen III = Coproporphyrinogen III + 4 CO2

4425, 650797, 650999, 649782, 4417, 4444, 4445, 650726, 651454, 651526, 650890, 390946, 649149, -

1R3T, 3D-view

4.1.1.37

Uroporphyrinogen III = Coproporphyrinogen III + 4 CO2

4425, 650797, 650999, 649782, 4417, 4444, 4445, 650726, 651454, 651526, 650890, 390946, 649149, -

1R3W, 3D-view

4.1.1.37

Uroporphyrinogen III = Coproporphyrinogen III + 4 CO2

4425, 650797, 650999, 649782, 4417, 4444, 4445, 650726, 651454, 651526, 650890, 390946, 649149, -

1R3Y, 3D-view

4.1.1.37

Uroporphyrinogen III = Coproporphyrinogen III + 4 CO2

4425, 650797, 650999, 649782, 4417, 4444, 4445, 650726, 651454, 651526, 650890, 390946, 649149, -

2Q71, 3D-view

4.1.1.37

uroporphyrinogen-III = coproporphyrinogen-III + 4 CO2

-

1R3T, 3D-view

4.1.1.37

uroporphyrinogen-III = coproporphyrinogen-III + 4 CO2

-

1R3W, 3D-view

4.1.1.37

uroporphyrinogen-III = coproporphyrinogen-III + 4 CO2

-

1R3Y, 3D-view

4.1.1.37

uroporphyrinogen-III = coproporphyrinogen-III + 4 CO2

-

2Q71, 3D-view

4.1.1.37

uroporphyrinogen-III = coproporphyrinogen-III + CO2

652198

1R3T, 3D-view

4.1.1.37

uroporphyrinogen-III = coproporphyrinogen-III + CO2

652198

1R3W, 3D-view

4.1.1.37

uroporphyrinogen-III = coproporphyrinogen-III + CO2

652198

1R3Y, 3D-view

4.1.1.37

uroporphyrinogen-III = coproporphyrinogen-III + CO2

652198

2Q71, 3D-view

4.1.1.37

28 entries

Inhibitor in Enzyme-catalyzed Reactions (1 result)

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Show Inhibitors (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

4.2.1.24

-

210697

-

3D Structure of Enzyme-Ligand-Complex (PDB) (12 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (12 entries)

EC NUMBER

ENZYME 3D STRUCTURE

4.1.1.37

1R3T, 3D-view

4.1.1.37

1R3W, 3D-view

4.1.1.37

1R3Y, 3D-view

4.1.1.37

2Q71, 3D-view

4.1.1.37

1R3T, 3D-view

4.1.1.37

1R3W, 3D-view

4.1.1.37

1R3Y, 3D-view

4.1.1.37

2Q71, 3D-view

4.1.1.37

1R3T, 3D-view

4.1.1.37

1R3W, 3D-view

4.1.1.37

1R3Y, 3D-view

4.1.1.37

2Q71, 3D-view

4.1.1.37

12 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (25 results)

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Show Turnover Number (25 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.3.3.15

0.46

-

at pH 8.0 and 37°C

737655

1.3.3.3

0.000002

-

mutant D400A, total product, 37°C, pH not specified in the publication

763670

1.3.3.3

0.000012

-

mutant R262A, divinyl product, 37°C, pH not specified in the publication

763670

1.3.3.3

0.00025

-

mutant H158A

675777

1.3.3.3

0.00042

-

mutant R262A, total product, 37°C, pH not specified in the publication

763670

1.3.3.3

0.00167

-

mutant R401A, divinyl product, 37°C, pH not specified in the publication

763670

1.3.3.3

0.003

-

recombinant O2-dependent enzyme form

656175

1.3.3.3

0.0033

-

monovinyl as product

672533

1.3.3.3

0.0033

-

with monovinyl product

675776

1.3.3.3

0.0125

-

divinyl as product

672533

1.3.3.3

0.01616

-

total product

672533

1.3.3.3

0.017

-

pH and temperature not specified in the publication

672533

1.3.3.3

0.02

-

mutant R401A, total product, 37°C, pH not specified in the publication

763670

1.3.3.3

0.02667

-

wild-type, divinyl product, 37°C, pH not specified in the publication

763670

1.3.3.3

0.045

-

wild-type, total product, 37°C, pH not specified in the publication

763670

1.3.3.3

0.055

-

with divinyl product

675776

1.3.3.3

0.06

-

at 37°C

688811

1.3.3.3

0.06

-

total product

675776

1.3.3.3

0.06

-

wild-type

675777

1.3.3.3

0.6

-

mutant N272H, pH 7.2, 37°C

701321

1.3.3.3

1.8

-

wild-type, pH 7.2, 37°C

701321

1.3.3.3

16

-

-

390951

1.3.3.3

21 entries

1.3.3.4

0.000833

-

-

391011

1.3.98.3

360

-

mutant enzyme Y74F, at pH 8.0 and 30°C

739104

1.3.98.3

900

-

wild type enzyme, at pH 8.0 and 30°C

739104

1.3.98.3

2 entries

K_M Value (66 results)

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Show KM Value (66 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.3.3.15

0.00529

-

at pH 8.7 and 37°C

391011

1.3.3.15

0.0067

-

at pH 8.0 and 37°C

737655

1.3.3.3

0.000066

-

in 250 mM Tris-HCl, 2.5 mM EDTA, pH 7.15, at 37°C

684418

1.3.3.3

0.000066

-

pH 7.2, 37°C

684418

1.3.3.3

0.00012

-

-

390971

1.3.3.3

0.00013

-

with monovinyl product

675776

1.3.3.3

0.00015

-

mutant enzyme H158A, at 37°C

675777

1.3.3.3

0.00016

-

-

390968

1.3.3.3

0.00025

-

recombinant enzyme

657084

1.3.3.3

0.00029

-

wild-type, pH 7.2, 37°C

701321

1.3.3.3

0.0003

-

-

390948

1.3.3.3

0.0003

-

wild type enzyme, at 37°C

675777

1.3.3.3

0.00034

-

wild-type, divinyl product, 37°C, pH not specified in the publication

763670

1.3.3.3

0.0005

-

mutant R231W

390948

1.3.3.3

0.00054

-

pH and temperature not specified in the publication

672533

1.3.3.3

0.00054

-

mutant N272H, pH 7.2, 37°C

701321

1.3.3.3

0.00054

-

total product

672533

1.3.3.3

0.00055

-

divinyl as product

672533

1.3.3.3

0.0006

-

-

390951

1.3.3.3

0.00068

-

at 37°C

688811

1.3.3.3

0.00068

-

total product

675776

1.3.3.3

0.0007

-

with divinyl product

675776

1.3.3.3

0.00078

-

mutant D400A, total product, 37°C, pH not specified in the publication

763670

1.3.3.3

0.00079

-

wild-type, total product, 37°C, pH not specified in the publication

763670

1.3.3.3

0.00096

-

mutant R401A, divinyl product, 37°C, pH not specified in the publication

763670

1.3.3.3

0.00097

-

monovinyl as product

672533

1.3.3.3

0.001

-

-

390959

1.3.3.3

0.0016

-

HemF mutant C167S

656175

1.3.3.3

0.002

-

HemF mutant Y240F

656175

1.3.3.3

0.0021

-

HemF mutant G127V

656175

1.3.3.3

0.0026

-

recombinant O2-dependent enzyme form HemF

656175

1.3.3.3

0.0029

-

mutant R401A, total product, 37°C, pH not specified in the publication

763670

1.3.3.3

0.003

-

HemF mutants Y213F, T132A, and W166L

656175

1.3.3.3

0.0031

-

recombinant wild-type enzyme, pH 7.0, 37°C

655624

1.3.3.3

0.0032

-

-

390944

1.3.3.3

0.0032

-

HemF mutant W298L

656175

1.3.3.3

0.0032

-

same value for aerobic and anaerobic oxidation

390974

1.3.3.3

0.0033

-

HemF mutant W123L

656175

1.3.3.3

0.0035

-

HemF mutants Y160F, W123L, and P133A

656175

1.3.3.3

0.0036

-

HemF mutant W124R

656175

1.3.3.3

0.0038

-

HemF mutant Y135F

656175

1.3.3.3

0.0041

-

HemF mutant Y170F

656175

1.3.3.3

0.0043

-

HemF mutants Y276F and W36L

656175

1.3.3.3

0.0051

-

mutant R262A, divinyl product, 37°C, pH not specified in the publication

763670

1.3.3.3

0.0087

-

mutant R262A, total product, 37°C, pH not specified in the publication

763670

1.3.3.3

0.00967

-

pH 7.5, 37°C, recombinant enzyme

713182

1.3.3.3

0.012

-

-

390979

1.3.3.3

0.0151

-

pH 7.5, 37°C, native enzyme

713182

1.3.3.3

0.018

0.025

presence of phospholipids

390964

1.3.3.3

0.025

-

crude extract

390964

1.3.3.3

0.03

-

-

390980

1.3.3.3

0.03

0.05

-

390976

1.3.3.3

0.035

-

-

390977

1.3.3.3

0.036

-

-

390978

1.3.3.3

0.047

-

-

390949, 390953

1.3.3.3

0.048

-

-

390949

1.3.3.3

0.048

-

purified enzyme

390964

1.3.3.3

0.05

-

-

390960

1.3.3.3

0.1

-

presence of activating lecithin

390956

1.3.3.3

0.32

-

-

390956

1.3.3.15

2 entries

1.3.3.3

58 entries

1.3.3.4

0.0053

-

-

391011

1.3.98.3

0.0052

-

wild type enzyme, at pH 8.0 and 30°C

739104

1.3.98.3

0.0067

-

mutant enzyme Y74F, at pH 8.0 and 30°C

739104

4.1.1.37

0.00005

-

-

4425, 4440

4.1.1.37

0.0004

-

-

4420

4.1.1.37

0.00043

-

-

4427

1.3.98.3

2 entries

4.1.1.37

3 entries

K_i Value (1 result)

top print hide

Show KI Value (1 entry)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.3.3.3

0.0076

-

competitive inhibition

390971

References & Links

Literature References (135)

top print hide

Show Reference (135 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

4417

13549492

Porphyrin biosynthesis in erythrocytes. III. Uroporphyrinogen and its decarboxylase

1958

Mauzerall, D.; Granick, S.

J. Biol. Chem.

232

1141-1162

4420

7350915

Some kinetic properties of human red cell uroporphyrinogen decarboxylase

1980

De Verneuil, H.; Grandchamp, B.; Nordmann, Y.

Biochim. Biophys. Acta

611

174-186

4422

534506

Decarboxylation of porphyrinogens by rat liver uroporphyrinogen decarboxylase

1979

Smith, A.G.; Francis, J.E.

Biochem. J.

183

455-458

4425

6822570

Purification and properties of uroporphyrinogen decarboxylase from human erythrocytes

1983

De Verneuil, H.; Sassa, Sh.; Kappas, A.

J. Biol. Chem.

258

2454-2460

4427

6626522

Purification and characterization of bovine hepatic uroporphyrinogen decarboxylase

1983

Straka, J.G.; Kushner, J.P.

Biochemistry

22

4664-4672

4430

-

Human uroporphyrinogen decarboxylase. Do tissue-specific isoenzymes exist?

1984

Elder, G.H.; Urquhart, A.J.

Biochem. Soc. Trans.

12

663-664

4440

9251000

Purification and properties of uroporphyrinogen decarboxylase from human erythrocytes

1997

Roberts, A.G.; Elder, G.H.

Methods Enzymol.

281

349-355

4444

2492941

Studies on uroporphyrinogen decarboxylase of etiolated Euglena gracilis Z

1989

Juknat, A.A.; Seubert, A.; Seubert, S.; Ippen, H.

Eur. J. Biochem.

179

423-428

4445

8352737

Purification and properties of the uroporphyrinogen decarboxylase from Rhodobacter sphaeroides

1993

Jones, R.M.; Jordan, P.M.

Biochem. J.

293

703-712

210697

6451221

Purification, properties and synthesis of delta-aminolaevulinate dehydratase from Neurospora crassa

1980

Chandrika, S.R.; Padmanaban, G.

Biochem. J.

191

29-36

390943

11079369

Function and structure of rat hepatic coproporphyrinogen oxidase

2000

Sorianello, E.M.; Mazzetti, M.B.

Comp. Biochem. Physiol. B

127

155-164

390944

11820932

Kinetic studies of novel di- and tri-propionate substrates for the chicken red blood cell enzyme coproporphyrinogen oxidase

2002

Jones, M.A.; He, J.; Lash, T.D.

J. Biochem.

131

201-205

390945

11929047

Molecular, immunological, enzymatic and biochemical studies of coproporphyrinogen oxidase deficiency in a family with hereditary coproporphyria

2002

Gross, U.; Puy, H.; Kuhnel, U.; Meissauer, U.; Deybach, J.C.; Jacob, K.; Martasek, P.; Nordmann, Y.; Doss, M.O.

Cell. Mol. Biol.

48

49-55

390946

9933622

Expression of uroporphyrinogen decarboxylase or coproporphyrinogen oxidase antisense RNA in tobacco induces pathogen defense responses conferring increased resistance to tobacco mosaic virus

1999

Mock, H.P; Heller, W.; Molina, A.; Neubohn, B.; Sandermann, H.; Grimm, B.

J. Biol. Chem.

274

4231-4238

390947

10485293

Oxidation of protoporphyrinogen IX in Escherichia coli is mediated by the aerobic coproporphyrinogen oxidase

1999

Narita, S.; Taketani, S.; Inokuchi, H.

Mol. Gen. Genet.

261

1012-1020

390948

9074788

Human coproporphyrinogen oxidase. Biochemical characterization of recombinant normal and R231W mutated enzymes expressed in E. coli as soluble, catalytically active homodimers

1997

Martasek, P.; Camadro, J.M.; Raman, R.S.; Lecomte, M.C.; Le Caer, J.P.; Demeler, B.; Grandchamp, B.; Labbe, P.

Cell. Mol. Biol.

43

47-58

390949

9251001

Purification and properties of coproporphyrinogen III oxidase from bovine liver

1997

Yoshinaga, T.

Methods Enzymol.

281

355-367

390950

9090723

Effect of covalent modification on coproporphyrinogen oxidase from chicken red blood cells

1997

Jones, M.A.; Hamilton, M.L.; Lash, T.D.

Prep. Biochem. Biotechnol.

27

47-57

390951

8955072

Human coproporphyrinogen oxidase is not a metalloprotein

1996

Medlock, A.E.; Dailey, H.A.

J. Biol. Chem.

271

32507-32510

390952

8407975

Coproporhyrinogen oxidase. Purification, molecular cloning, and induction of mRNA during erythroid differentiation

1993

Kohno, H.; Furukawa, T.; Yoshinaga, T.; Tokunaga, R.; Taketani, S.

J. Biol. Chem.

268

21359-21363

390953

8547339

Mouse coprophorphyrinogen oxidase is a copper-containing enzyme: expression in E. coli and site-directed mutagenesis

1996

Kohno, H.; Furukawa, T.; Tokunaga, R.; Taketani, S.; Yoshinaga, T.

Biochim. Biophys. Acta

1292

156-162

390954

7889936

Coordinate expression of coproporphyrinogen oxidase and cytochrome c6 in the green alga Chlamydomonas reinhardtii in response to changes in copper availability

1995

Hill, K.L.; Merchant, S.

EMBO J.

14

857-865

390955

7768836

Cloning and characterization of the Escherichia coli hemN gene encoding the oxygen-independent coproporphyrinogen III oxidase

1995

Troup, B.; Hungerer, C.; Jahn, D.

J. Bacteriol.

177

3326-3331

390956

2540974

Purification and properties of mouse liver coproporphyrinogen oxidase

1989

Bogard, M.; Camadro, J.M.; Labbe, P.

Eur. J. Biochem.

181

417-421

390957

2838478

Isolation, sequence, and regulation by oxygen of the yeast hem13 gene coding for coproporphyrinogen oxidase

1988

Zagorec, M.; Buhler, J.M.; Treich, I.; Keng, T.; Guarente, L.; Labbe-Bois, R.

J. Biol. Chem.

263

9718-9724

390958

-

Synthetic and biosynthetic studies of porphyrins. Part 7. The Action of coproporphyrinogen oxidase on coproporphyrinogen-IV: Syntheses of protoporphyrin-XII, mesoporphyrin XIII, and related tricarboxylic porphyrins

1987

Al-Hazimi, H.M.G.; Jackson, A.H.; Knight, D.W.; Lash, T.D.

J. Chem. Soc. Perkin Trans. I

1987

265-276

390959

3814086

A high-performance-liquid-chromatographic method for the assay of coproporphyrinogen oxidase activity in rat liver

1986

Li, F.; Lim, C.K.; Peters, T.J.

Biochem. J.

239

481-484

390960

3516695

Purification and properties of coproporphyrinogen oxidase from yeast Saccharomyces cerevisiae

1986

Camadro, J.M.; Chambon, H.; Jolles, J.; Labbe, P.

Eur. J. Biochem.

156

579-587

390961

-

Biosynthesis of porphyrins and related macrocycles. Part 25. Synthesis of analogues of coproporphyrinogen-III and studies of their interaction with coproporphyrinogen-III oxidase from Euglena gracilis

1985

Robinson, J.A.; McDonald, E.; Battersby, A.R.

J. Chem. Soc. Perkin Trans. I

1985

1699-1709

390962

6603215

Anaerobic and aerobic coproporphyrinogen III oxidases of Rhodopseudomonas spheroids. Mechanism and stereochemistry of vinyl group formation

1983

Seehra, J.S.; Jordan, P.M.; Akhtar, M.

Biochem. J.

209

709-718

390963

6841317

Protoporphyrin formation in Rhizobium japonicum

1983

Keithly, J.H.; Nadler, K.D.

J. Bacteriol.

154

838-845

390964

7372605

Coproporphyrinogen oxidase. I. Purification, properties, and activation by phospholipids

1980

Yoshinaga, T.; Sano, S.

J. Biol. Chem.

255

4722-4726

390965

7372606

Coproporphyrinogen oxidase. II. Reaction mechanism and role of tyrosine residues on the activity

1980

Yoshinaga, T.; Sano, S.

J. Biol. Chem.

255

4727-4731

390966

-

Biosynthesis of porphyrins and related macrocycles. Part 13. Structure of the protopophyrin isomer derived from coproporphyrinogen IV by the action of beef-liver coproporphyrinogenase: Synthesis of protoporphyrin XIII

1980

Battersby, A.R.; Hamilton, A.D.; McDonald, E.; Mombelli, L.; Wong, Q.H.

J. Chem. Soc. Perkin Trans. I

1980

1283-1289

390967

-

Measurement of heme biosynthetic enzymes in mammalian tissues. II. Coproporphyrinogen oxidase

1980

Kardish, R.M.; Woods, J.S.

J. Appl. Biochem.

2

168-174

390968

31872

The mitochondrial localization of coproporphyrinogen III oxidase

1978

Grandchamp, B.; Phung, N.; Nordmann, Y.

Biochem. J.

176

97-102

390969

666752

Evidence that the coproporphyrinogen oxidase activity of rat liver is situated in the intermembrane space of mitochondria

1978

Elder, G.H.; Evans, J.O.

Biochem. J.

172

345-347

390970

629747

Factors determining the sequence of oxidative decarboxylation of the 2- and 4-propionate substituents of coproporphyrinogen III by coproporphyrinogen oxidase in rat liver

1978

Elder, G.H.; Evans, J.O.; Jackson, J.R.; Jackson, A.H.

Biochem. J.

169

215-223

390971

629746

A radiochemical method for the measurement of coproporphyrinogen oxidase and the utilization of substrates other than coproporphyrinogen III by the enzyme from rat liver

1978

Elder, G.H.; Evans, J.O.

Biochem. J.

169

205-214

390973

-

Specificity of coproporphyrinogen oxidase: Conversion of coproporphyrinogen-IV into protoporphyrin-XIII

1976

Al-Hazimi, H.M.G.; Jackson, A.H.; Ryder, D.J.

J. Chem. Soc. Chem. Commun.

1976

188-189

390974

4153629

Aerobic and anaerobic coproporphyrinogenase activities in extracts from Saccharomyces cerevisiae. Purification and characterization

1974

Poulson, R.; Polglase, W.J.

J. Biol. Chem.

249

6367-6371

390975

4394949

Coproporphyrinogenase activities in extracts of Rhodopseudomonas spheroids

1976

Tait, G.H.

Biochem. J.

118

28P-29P

390976

4345352

Coproporphyrinogenase activities in extracts of Rhodopseudomonas spheroids and Chromatium strain D

1972

Tait, G.H.

Biochem. J.

128

1159-1169

390977

-

Studies on the formation of protoporphyrin IX by anaerobic bacteria

1972

Mori, M.; Sano, S.

Biochim. Biophys. Acta

264

252-262

390978

4986869

Coproporphyrinogenase in tobacco (Nicotiana tabacum L.)

1970

Hsu, W.P.; Miller, G.W.

Biochem. J.

117

215-220

390979

5724967

Coproporphyrinogenase in a respiration-deficient mutant of yeast lacking all cytochromes and accumulating coproporphyrin

1968

Miyake, S.; Sugimura, T.

J. Bacteriol.

96

1997-2003

390980

5881662

Purification and properties of coproporphyrinogenase

1965

Battle, A.M.del C.; Benson, A.; Rimington, C.

Biochem. J.

97

731-740

391011

9784236

Purification of and kinetic studies on a cloned protoporphyrinogen oxidase from the aerobic bacterium Bacillus subtilis

1998

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.

Arch. Biochem. Biophys.

358

251-256

649149

11679753

Tobacco uroporphyrinogen-III decarboxylase: characterization, crystallization and preliminary X-ray analysis

2001

Martins, B.M.; Grimm, B.; Mock, H.P.; Richter, G.; Huber, R.; Messerschmidt, A.

Acta Crystallogr. Sect. D

57

1709-1711

649782

10410240

Porphyria-induced hepatic porphyrinogen carboxy-lyase inhibitor and its interaction with the active site(s) of the enzyme

1999

Billi de Catabbi, S.; Wainstok de Calmanovici, R.; Minutolo, C.; Aldonatti, C.; San Martin de Viale, L.C.

Biochem. Mol. Biol. Int.

47

945-956

650726

11719352

Functional consequences of naturally occurring mutations in human uroporphyrinogen decarboxylase

2001

Phillips, J.D.; Parker, T.L.; Schubert, H.L.; Whitby, F.G.; Hill, C.P.; Kushner, J.P.

Blood

98

3179-3185

650797

11929044

Levels of uroporphyrinogen decarboxylase (URO-D) in erythrocytes of Italian porphyria cutanea tarda patients

2002

Tavazzi, D.; Di Montemuros, F.M.; Fargion, S.; Fracanzani, A.L.; Fiorelli, G.; Cappellini, M.D.

Cell. Mol. Biol.

48

27-32

650890

12381387

Comparison between crab hepatopancreas and rat liver uroporphyrinogen decarboxylase

2002

Chaufan, G.; Corvi, M.; Armesto, A.; San Martin de Viale, L.C.; Luquet, C.; Rios de Molina, M.

Comp. Biochem. Physiol. B

133

251-256

650999

14633982

Structural basis for tetrapyrrole coordination by uroporphyrinogen decarboxylase

2003

Phillips, J.D.; Whitby, F.G.; Kushner, J.P.; Hill, C.P.

EMBO J.

22

6225-6233

651454

10477430

Screening for mutations in the uroporphyrinogen decarboxylase gene using denaturing gradient gel electrophoresis. Identification and characterization of six novel mutations associated with familial PCT

1999

Christiansen, L.; Ged, C.; Hombrados, I.; Brons-Poulsen, J.; Fontanellas, A.; de Verneuil, H.; Horder, M.; Petersen, N.E.

Hum. Mutat.

14

222-232

651526

11378443

How does hexachlorobenzene treatment affect liver uroporphyrinogen decarboxylase?

2001

Chaufan, G.; Rios de Molina, M.C.; San Martin de Viale, L.C.

Int. J. Biochem. Cell Biol.

33

621-630

652198

11524417

Crystal structure and substrate binding modeling of the uroporphyrinogen-III decarboxylase from Nicotiana tabacum. Implications for the catalytic mechanism

2001

Martins, B.M.; Grimm, B.; Mock, H.P.; Huber, R.; Messerschmidt, A.

J. Biol. Chem.

276

44108-44116

654965

11909722

Unprecedented overmetabolism of a porphyrinogen substrate by coproporphyrinogen oxidase

2002

Lash, T.D.; Keck, A.S.; Mani, U.N.; Jones, M.A.

Bioorg. Med. Chem. Lett.

12

1079-1082

654966

11814818

Metabolism of analogues of coproporphyrinogen-III with modified side chains: implications for binding at the active site of coproporphyrinogen oxidase

2002

Lash, T.D.; Kaprak, T.A.; Shen, L.; Jones, M.A.

Bioorg. Med. Chem. Lett.

12

451-456

654975

15482924

An effective chromatographic separation of chicken red blood cell coproporphyrinogen oxidase and uroporphyrinogen decarboxylase, two enzymes in heme biosynthesis

2004

Jones, M.A.; Taneja, M.; Xu, Y.; Chung, W.; Stob, C.M.; Lash, T.D.

Bioorg. Med. Chem. Lett.

14

5559-5564

655119

12453883

Heme inhibits the mitochondrial import of coproporphyrinogen oxidase. Comments

2002

Susa, S.; Daimon, M.; Ono, H.; Li, S.; Yoshida, T.; Kato, T.

Blood

100

4678-4679

655340

14633981

Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of Radical SAM enzymes

2003

Layer, G.; Moser, J.; Heinz, D.W.; Jahn, D.; Schubert, W.D.

EMBO J.

22

6214-6224

655624

13129604

Oxygen-dependent coproporphyrinogen-III oxidase from Escherichia coli: one-step purification and biochemical characterisation

2003

Macieira, S.; Martins, B.M.; Huber, R.

FEMS Microbiol. Lett.

226

31-37

656073

12114526

Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli

2002

Layer, G.; Verfurth, K.; Mahlitz, E.; Jahn, D.

J. Biol. Chem.

277

34136-34142

656175

12975365

Oxygen-dependent coproporphyrinogen III oxidase (HemF) from Escherichia coli is stimulated by manganese

2003

Breckau, D.; Mahlitz, E.; Sauerwald, A.; Layer, G.; Jahn, D.

J. Biol. Chem.

278

46625-46631

656245

15194705

Crystal structure of the oxygen-dependant coproporphyrinogen oxidase (Hem13p) of Saccharomyces cerevisiae

2004

Phillips, J.D.; Whitby, F.G.; Warby, C.A.; Labbe, P.; Yang, C.; Pflugrath, J.W.; Ferrara, J.D.; Robinson, H.; Kushner, J.P.; Hill, C.P.

J. Biol. Chem.

279

38960-38968

656432

12181641

Two novel mutations and coexistence of the 991C>T and the 1339C>T mutation on a single allele in the coproporphyrinogen oxidase gene in Swedish patients with hereditary coproporphyria

2002

Wiman, A.; Floderus, Y.; Harper, P.

J. Hum. Genet.

47

407-412

657084

-

Molecular characterization of coproporphyrinogen oxidase from Glycine max and Arabidopsis thaliana

2002

Santana, M.A.; Tan, F.C.; Smith, A.G.

Plant Physiol. Biochem.

40

289-298

658501

15450488

Structure and function of radical SAM enzymes

2004

Layer, G.; Heinz, D.W.; Jahn, D.; Schubert, W.D.

Curr. Opin. Chem. Biol.

8

468-476

671195

-

Use of crosslinking to assess subunit interaction of recombinant human coproporphyrinogen oxidase

2005

Stephenson, J.R.; Thomas, N.E.; Friesen, J.A.; Jones, M.A.

Am. J. Biochem. Biotechnol.

1

103-106

672473

16218869

Structural and functional comparison of HemN to other radical SAM enzymes

2005

Layer, G.; Kervio, E.; Morlock, G.; Heinz, D.W.; Jahn, D.; Retey, J.; Schubert, W.D.

Biol. Chem.

386

971-980

672533

16084099

Metabolism of pentacarboxylate porphyrinogens by highly purified human coproporphyrinogen oxidase: further evidence for the existence of an abnormal pathway for heme biosynthesis

2005

Cooper, C.L.; Stob, C.M.; Jones, M.A.; Lash, T.D.

Bioorg. Med. Chem.

13

6244-6251

672822

16868543

Methotrexate used in combination with aminolaevulinic acid for photodynamic killing of prostate cancer cells

2006

Sinha, A.K.; Anand, S.; Ortel, B.J.; Chang, Y.; Mai, Z.; Hasan, T.; Maytin, E.V.

Br. J. Cancer

95

485-495

672827

16398658

Dual gene defects involving delta-aminolaevulinate dehydratase and coproporphyrinogen oxidase in a porphyria patient

2006

Akagi, R.; Inoue, R.; Muranaka, S.; Tahara, T.; Taketani, S.; Anderson, K.E.; Phillips, J.D.; Sassa, S.

Br. J. Haematol.

132

237-243

673936

16159891

Mutations in human CPO gene predict clinical expression of either hepatic hereditary coproporphyria or erythropoietic harderoporphyria

2005

Schmitt, C.; Gouya, L.; Malonova, E.; Lamoril, J.; Camadro, J.M.; Flamme, M.; Rose, C.; Lyoumi, S.; Da Silva, V.; Boileau, C.; Grandchamp, B.; Beaumont, C.; Deybach, J.C.; Puy, H.

Hum. Mol. Genet.

14

3089-3098

674462

15967800

Radical S-adenosylmethionine enzyme coproporphyrinogen III oxidase HemN: functional features of the [4Fe-4S] cluster and the two bound S-adenosyl-L-methionines

2005

Layer, G.; Grage, K.; Teschner, T.; Schuenemann, V.; Breckau, D.; Masoumi, A.; Jahn, M.; Heathcote, P.; Trautwein, A.X.; Jahn, D.

J. Biol. Chem.

280

29038-29046

674567

16606627

The substrate radical of Escherichia coli oxygen-independent coproporphyrinogen III oxidase HemN

2006

Layer, G.; Pierik, A.J.; Trost, M.; Rigby, S.E.; Leech, H.K.; Grage, K.; Breckau, D.; Astner, I.; Jaensch, L.; Heathcote, P.; Warren, M.J.; Heinz, D.W.; Jahn, D.

J. Biol. Chem.

281

15727-15734

675776

16258391

Kinetic evaluation of human cloned coproporphyrinogen oxidase using a ring isomer of the natural substrate

2005

Cooper, C.L.; Lash, T.D.; Jones, M.A.

Med. Sci. Monit.

11

BR420-BR425

675777

17179900

Investigation of the catalytic and structural roles of conserved histidines of human coproporphyrinogen oxidase using site-directed mutagenesis

2006

Gitter, S.J.; Cooper, C.L.; Friesen, J.A.; Jones, M.A.

Med. Sci. Monit.

13

BR1-BR10

684418

18294003

Direct assay of enzymes in heme biosynthesis for the detection of porphyrias by tandem mass spectrometry. Uroporphyrinogen decarboxylase and coproporphyrinogen III oxidase

2008

Wang, Y.; Gatti, P.; Sadilek, M.; Scott, C.R.; Turecek, F.; Gelb, M.H.

Anal. Chem.

80

2599-2605

685536

18226911

A comparative density-functional study of the reaction mechanism of the O2-dependent coproporphyrinogen III oxidase

2008

Silva, P.J.; Ramos, M.J.

Bioorg. Med. Chem.

16

2726-2733

686237

18307109

The radical SAM superfamily

2008

Frey, P.A.; Hegeman, A.D.; Ruzicka, F.J.

Crit. Rev. Biochem. Mol. Biol.

43

63-88

688811

18160932

Use of di- and tripropionate substrate analogs to probe the active site of human recombinant coproporphyrinogen oxidase

2008

Morgenthaler, J.B.; Barto, R.L.; Lash, T.D.; Jones, M.A.

Med. Sci. Monit.

14

BR1-BR7

690136

17215094

A cascade analysis of the interaction of mercury and coproporphyrinogen oxidase (CPOX) polymorphism on the heme biosynthetic pathway and porphyrin production by Heyer et al. [Toxicol. Lett. 161 (2006) 159-166]. Comment

2007

Bjoerkman, L.; Vahter, M.

Toxicol. Lett.

169

91-92

690137

17987105

A cascade analysis of the interaction of mercury and coproporphyrinogen oxidase (CPOX) polymorphism on the heme biosynthetic pathway and porphyrin production by Heyer et al. [Toxicol. Lett. 161 (2006) 159-166]. Reply

2007

Heyer, N.J.; Bittner, A.C.; Echeverria, D.; Woods, J.S.

Toxicol. Lett.

169

93-94

697204

19267996

Four novel mutations of the coproporphyrinogen III oxidase gene

2009

Aurizi, C.; Lupia Palmieri, G.; Barbieri, L.; Macri, A.; Sorge, F.; Usai, G.; Biolcati, G.

Cell. Mol. Biol.

55

15-18

701321

19339664

Cloning, expression, and biochemical properties of CPOX4, a genetic variant of coproporphyrinogen oxidase that affects susceptibility to mercury toxicity in humans

2009

Li, T.; Woods, J.S.

Toxicol. Sci.

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Functional differentiation of two analogous coproporphyrinogen III oxidases for heme and chlorophyll biosynthesis pathways in the cyanobacterium Synechocystis sp. PCC 6803

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Coproporphyrin III excretion identifies the anaerobic coproporphyrinogen III oxidase HemN as a copper target in the Cu+-ATPase mutant copA- of Rubrivivax gelatinosus

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A mutation in a coproporphyrinogen III oxidase gene confers growth inhibition, enhanced powdery mildew resistance and powdery mildew-induced cell death in Arabidopsis

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Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin

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Proc. Natl. Acad. Sci. USA

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The role of coproporphyrinogen III oxidase and ferrochelatase genes in heme biosynthesis and regulation in Aspergillus niger

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Franken, A.C.; Werner, E.R.; Haas, H.; Lokman, B.C.; van den Hondel, C.A.; Ram, A.F.; de Weert, S.; Punt, P.J.

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The role of coproporphyrinogen III oxidase and ferrochelatase genes in heme biosynthesis and regulation in Aspergillus niger

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The enzyme engineering of mutant homodimer and heterodimer of coproporphyinogen oxidase contributes to new insight into hereditary coproporphyria and harderoporphyria

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Fluorouracil enhances photodynamic therapy of squamous cell carcinoma via a p53-independent mechanism that increases protoporphyrin IX levels and tumor cell death

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Gametophyte development needs mitochondrial coproporphyrinogen III oxidase function

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Role of aspartate 400, arginine 262, and arginine 401 in the catalytic mechanism of human coproporphyrinogen oxidase

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A case of hereditary coproporphyria with posterior reversible encephalopathy and novel coproporphyrinogen oxidase gene mutation c.863T>G (p.Leu288Trp)

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A case of hereditary coproporphyria with posterior reversible encephalopathy and novel coproporphyrinogen oxidase gene mutation c.863T>G (p.Leu288Trp)

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Lambie, D.; Florkowski, C.; Sies, C.; Raizis, A.; Siu, W.K.; Towns, C.

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Cystathionine-gamma-lyase (CSE) deficiency increases erythropoiesis and promotes mitochondrial electron transport via the upregulation of coproporphyrinogen III oxidase and consequent stimulation of heme biosynthesis

2019

Modis, K.; Ramanujam, V.; Govar, A.; Lopez, E.; Anderson, K.; Wang, R.; Szabo, C.

Biochem. Pharmacol.

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Cystathionine-gamma-lyase (CSE) deficiency increases erythropoiesis and promotes mitochondrial electron transport via the upregulation of coproporphyrinogen III oxidase and consequent stimulation of heme biosynthesis

2019

Modis, K.; Ramanujam, V.; Govar, A.; Lopez, E.; Anderson, K.; Wang, R.; Szabo, C.

Biochem. Pharmacol.

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5-Fluorouracil enhances protoporphyrin IX accumulation and lesion clearance during photodynamic therapy of actinic keratoses A mechanism-based clinical trial

2018

Maytin, E.V.; Anand, S.; Riha, M.; Lohser, S.; Tellez, A.; Ishak, R.; Karpinski, L.; Sot, J.; Hu, B.; Denisyuk, A.; Davis, S.C.; Kyei, A.; Vidimos, A.

Clin. Cancer Res.

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Genetic mapping of a light-dependent lesion mimic mutant reveals the function of coproporphyrinogen III oxidase homolog in soybean

2020

Ma, J.; Yang, S.; Wang, D.; Tang, K.; Feng, X.X.; Feng, X.Z.

Front. Plant Sci.

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764783

32457787

Genetic mapping of a light-dependent lesion mimic mutant reveals the function of coproporphyrinogen III oxidase homolog in soybean

2020

Ma, J.; Yang, S.; Wang, D.; Tang, K.; Feng, X.X.; Feng, X.Z.

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557

765045

29925590

The cyanobacterial protoporphyrinogen oxidase HemJ is a new b-type heme protein functionally coupled with coproporphyrinogen III oxidase

2018

Skotnicova, P.; Sobotka, R.; Shepherd, M.; Hajek, J.; Hrouzek, P.; Tichy, M.

J. Biol. Chem.

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765045

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The cyanobacterial protoporphyrinogen oxidase HemJ is a new b-type heme protein functionally coupled with coproporphyrinogen III oxidase

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J. Biol. Chem.

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765391

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Acute hepatic porphyrias Identification of 46 hydroxymethylbilane synthase, 11 coproporphyrinogen oxidase, and 20 protoporphyrinogen oxidase novel mutations

2019

Loskove, Y.; Yasuda, M.; Chen, B.; Nazarenko, I.; Cody, N.; Desnick, R.J.

Mol. Genet. Metab.

128

352-357

765391

30385147

Acute hepatic porphyrias Identification of 46 hydroxymethylbilane synthase, 11 coproporphyrinogen oxidase, and 20 protoporphyrinogen oxidase novel mutations

2019

Loskove, Y.; Yasuda, M.; Chen, B.; Nazarenko, I.; Cody, N.; Desnick, R.J.

Mol. Genet. Metab.

128

352-357

765393

30828546

Harderoporphyria Case of lifelong photosensitivity associated with compound heterozygous coproporphyrinogen oxidase (CPOX) mutations

2019

Moghe, A.; Ramanujam, V.M.S.; Phillips, J.D.; Desnick, R.J.; Anderson, K.E.

Mol. Genet. Metab. Rep.

19

100457

765393

30828546

Harderoporphyria Case of lifelong photosensitivity associated with compound heterozygous coproporphyrinogen oxidase (CPOX) mutations

2019

Moghe, A.; Ramanujam, V.M.S.; Phillips, J.D.; Desnick, R.J.; Anderson, K.E.

Mol. Genet. Metab. Rep.

19

100457

765437

31292227

Staphylococcus aureus Coproporphyrinogen III Oxidase is required for aerobic and anaerobic heme synthesis

2019

Choby, J.E.; Skaar, E.P.

mSphere

4

e00235-19

765437

31292227

Staphylococcus aureus Coproporphyrinogen III Oxidase is required for aerobic and anaerobic heme synthesis

2019

Choby, J.E.; Skaar, E.P.

mSphere

4

e00235-19

765480

33462229

Epitope-specific immunity against Staphylococcus aureus coproporphyrinogen III oxidase

2021

Klimka, A.; Mertins, S.; Nicolai, A.K.; Rummler, L.M.; Higgins, P.G.; Guenther, S.D.; Tosetti, B.; Krut, O.; Kroenke, M.

NPJ Vaccines

6

11

765480

33462229

Epitope-specific immunity against Staphylococcus aureus coproporphyrinogen III oxidase

2021

Klimka, A.; Mertins, S.; Nicolai, A.K.; Rummler, L.M.; Higgins, P.G.; Guenther, S.D.; Tosetti, B.; Krut, O.; Kroenke, M.

NPJ Vaccines

6

11

765676

28739897

Antibacterial photosensitization through activation of coproporphyrinogen oxidase

2017

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.

Proc. Natl. Acad. Sci. USA

114

E6652-E6659

765676

28739897

Antibacterial photosensitization through activation of coproporphyrinogen oxidase

2017

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.

Proc. Natl. Acad. Sci. USA

114

E6652-E6659

764783

2 entries

765045

2 entries

765391

2 entries

765393

2 entries

765437

2 entries

765480

2 entries

765676

2 entries

Links to other databases for coproporphyrinogen III

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