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Ligand protoporphyrinogen

Basic Ligand Information

Molecular Structure

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 V (aerobic) more

Show all BRENDA pathways known for protoporphyrinogen

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (13 results)

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Show Natural Substrate (13 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.3.15

protoporphyrinogen IX + 3 O2 = protoporphyrin IX + 3 H2O2

765480

-

1.3.3.15

protoporphyrinogen IX + O2 = protoporphyrin IX + H2O

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

-

1.3.3.3

protoporphyrinogen IX + O2 = protoporphyrin IX + H2O

672533

-

1.3.3.3

protoporphyrinogen-IX + O2 = protoporphyrin-IX + CO2

390947

-

1.3.3.4

protoporphyrinogen IX + 3 O2 = protoporphyrin + 3 H2O2

695546, 698422, 698439, 695527, 699636, 700047

-

1.3.3.4

protoporphyrinogen IX + 3 O2 = protoporphyrin IX + 3 H2O2

725290, 764518, 765503, 724554, 725177, 726346, 764083, 764914, 765697, 724557, 764284, 764954, 764962, 744459, 764394, 765508, 712895, 744202, 745451, 746243, 711307, 713418, 744734, 745787, 765577, 744529

-

1.3.3.4

protoporphyrinogen IX + O2 = protoporphyrin IX + H2O

737734

-

1.3.3.4

protoporphyrinogen-IX + 3 O2 = protoporphyrin-IX + 3 H2O2

655194, 655018, 654950, 390988, 391010, 391011, 391016, 34955, 390990, 390994, 390995, 390997, 390999, 391003, 391017, 390981, 390986, 391002, 391004, 391007, 391012, 390985, 390987, 390993, 390982, 390983, 391001, 391006, 391008, 391013, 390992, 390984, 391000, 390991, 390998, 391014, 391015, 391009, 391005, 390996, 655341, 654874, 656991, 655497

-

1.3.5.3

protoporphyrinogen IX + 3 menadione = protoporphyrin IX + 3 menadiol

696347

-

1.3.5.3

protoporphyrinogen IX + 3 menaquinone = protoporphyrin IX + 3 menaquinol

726366

-

1.3.5.3

protoporphyrinogen IX + 3 plastoquinone = protoporphyrin IX + 3 plastoquinol

764518

-

1.3.5.3

protoporphyrinogen IX + 3 ubiquinone = protoporphyrin IX + 3 ubiquinol

726366

-

1.3.3.15

2 entries

1.3.3.3

2 entries

1.3.3.4

4 entries

1.3.5.3

4 entries

2.5.1.18

protoporphyrinogen + glutathione = protoporphyrinogen-S-glutathione + H2O

723365

-

In Vivo Product in Enzyme-catalyzed Reactions (13 results)

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Show Natural Product (13 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.3.3

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

0

-

1.3.3.3

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

0

-

1.3.3.3

harderoporphyrinogen + O2 = protoporphyrinogen IX + CO2 + H2O2

390971, 390965, 390970

-

1.3.3.3

isoharderoporphyrinogen + O2 = protoporphyrinogen IX + CO2 + H2O2

390970, 390965

-

1.3.3.3

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

0

-

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, 0, 390976

-

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, 390963, 390946, 390978, 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

0

-

1.3.3.3

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

0

-

1.3.98.3

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

0

-

1.3.98.3

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

0

-

1.3.98.3

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

0

-

1.3.3.3

10 entries

1.3.98.3

3 entries

Substrate in Enzyme-catalyzed Reactions (16 results)

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Show Substrate (16 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.3.15

protoporphyrinogen IX + 3 O2 = protoporphyrin IX + 3 H2O2

765577, 765480

-

1.3.3.15

protoporphyrinogen IX + O2 = protoporphyrin IX + H2O

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

-

1.3.3.3

protoporphyrinogen IX + O2 = protoporphyrin IX + H2O

672533

-

1.3.3.3

protoporphyrinogen-IX + O2 = protoporphyrin IX + CO2

390947

-

1.3.3.3

protoporphyrinogen-IX + O2 = protoporphyrin-IX + CO2

390947

-

1.3.3.4

protoporphyrinogen IX + 3 O2 = protoporphyrin + 3 H2O2

695546, 698422, 698439, 695527, 700047, 699636

-

1.3.3.4

protoporphyrinogen IX + 3 O2 = protoporphyrin IX + 3 H2O2

725290, 764518, 725862, 765503, 724554, 725177, 726346, 764083, 764914, 765697, 724557, 764284, 764954, 764962, 744459, 764394, 765508, 712895, 744202, 745451, 746243, 711307, 713418, 744734, 745787, 765577, 744529

-

1.3.3.4

protoporphyrinogen IX + O2 = protoporphyrin IX + H2O

737734

-

1.3.3.4

protoporphyrinogen-IX + 3 2,6-dichlorophenolindophenol = protoporphyrin-IX + 3 reduced 2,6-dichlorophenolindophenol

390988

-

1.3.3.4

protoporphyrinogen-IX + 3 O2 = protoporphyrin-IX + 3 H2O2

391010, 391011, 391016, 656991, 34955, 390990, 390994, 390995, 390997, 390999, 391003, 391017, 671294, 390981, 390986, 391002, 391004, 391007, 391012, 655194, 689568, 390985, 390987, 390993, 390982, 390983, 391001, 391006, 391008, 391013, 390992, 390984, 391000, 390991, 390998, 391014, 391015, 391009, 655018, 671892, 391005, 676308, 689348, 689352, 390996, 687248, 654950, 676521, 676307, 655497, 655341, 390988, 654874

-

1.3.5.3

protoporphyrinogen IX + 3 menadione = protoporphyrin IX + 3 menadiol

696347

-

1.3.5.3

protoporphyrinogen IX + 3 menaquinone = protoporphyrin IX + 3 menaquinol

726366

-

1.3.5.3

protoporphyrinogen IX + 3 plastoquinone = protoporphyrin IX + 3 plastoquinol

764518

-

1.3.5.3

protoporphyrinogen IX + 3 triphenyltetrazolium chloride = protoporphyrin IX + ?

726366

-

1.3.5.3

protoporphyrinogen IX + 3 ubiquinone = protoporphyrin IX + 3 ubiquinol

726366

-

1.3.3.15

2 entries

1.3.3.3

3 entries

1.3.3.4

5 entries

1.3.5.3

5 entries

2.5.1.18

protoporphyrinogen + glutathione = protoporphyrinogen-S-glutathione + H2O

723365

-

Product in Enzyme-catalyzed Reactions (22 results)

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Show Product (22 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.3.3

harderoporphyrinogen + O2 + 2 H+ = protoporphyrinogen + CO2 + H2O

0

-

1.3.3.3

2,4-bis-(beta-hydroxypropionic acid) deuteroporphyrinogen IX + O2 = protoporphyrinogen IX + CO2

390965

-

1.3.3.3

2-beta-hydroxypropionic acid-4-propionic acid deuteroporphyrinogen IX + O2 = protoporphyrinogen IX + CO2

390965

-

1.3.3.3

2-propionic acid-4-beta-hydroxypropionic acid deuteroporphyrinogen IX + O2 = protoporphyrinogen IX + CO2

390965

-

1.3.3.3

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

0

-

1.3.3.3

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

0

-

1.3.3.3

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

0

-

1.3.3.3

harderoporphyrinogen + O2 + H+ = protoporphyrinogen IX + CO2 + H2O2

0

-

1.3.3.3

harderoporphyrinogen + O2 = protoporphyrinogen IX + CO2 + H2O2

0, 390971, 390965, 390970

-

1.3.3.3

isoharderoporphyrinogen + O2 = protoporphyrinogen IX + CO2 + H2O2

390970, 390965

-

1.3.3.3

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

0

-

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 + ?

0, 390963, 390962, 390976

-

1.3.3.3

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

390944, 390950, 390958, 390973, 390954, 390952, 390953, 390947, 0, 390945, 390948, 390951, 390979, 390949, 390965, 390966, 390962, 390975, 390976, 390963, 390946, 390978, 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

0

-

1.3.3.3

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

0

-

1.3.3.3

harderoporphyrinogen + O2 + 2 H+ = protoporphyrinogen-IX + CO2 + 2 H2O

0

-

1.3.98.3

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

0

-

1.3.98.3

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

0

-

1.3.98.3

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

0

-

1.3.98.3

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

0

-

1.3.98.3

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

0

-

1.3.3.3

17 entries

1.3.98.3

5 entries

Inhibitor in Enzyme-catalyzed Reactions (4 results)

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Show Inhibitors (4 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.3.3.15

acts as a competitive inhibitor of the coproporphyrinogen III to coproporphyrin oxidase activity of HemY

738501

-

1.3.3.4

substrate inhibition above 0.05 mM

390992

-

2.5.1.61

inhibits both erythroid and lymphoblast forms of the enzyme

489948

-

4.2.1.24

feedback inhibition by downstream intermediate

749311

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (94 results)

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Show Turnover Number (94 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.3.3.15

0.252

-

pH and temperature not specified in the publication

765577

1.3.3.15

0.256

-

pH and temperature not specified in the publication

765577

1.3.3.15

0.44

-

at pH 8.0 and 37°C

737655

1.3.3.4

0.00000783

-

-

391016

1.3.3.4

0.00015

-

pH 7.5, 22°C, recombinant mutant Y366E

695527

1.3.3.4

0.0004

-

mutant K71A, pH 7.5, temperature not specified in the publication

712895

1.3.3.4

0.00042

-

pH 7.5, 22°C, recombinant mutant Y366A

695527

1.3.3.4

0.001

-

mutant I176A, pH 7.5, temperature not specified in the publication

712895

1.3.3.4

0.0016

-

pH 7.5, 22°C, recombinant mutant Y366H

695527

1.3.3.4

0.0027

-

mutant P64A, pH 7.5, temperature not specified in the publication

712895

1.3.3.4

0.00317

-

-

391011

1.3.3.4

0.00333

-

below 0.2/min, R59W mutant enzyme

391002

1.3.3.4

0.0034

-

pH 7.5, 22°C, recombinant wild-type enzyme

695527

1.3.3.4

0.0062

-

pH 7.4, temperature not specified in the publication, mutant G169A

726346, 746243

1.3.3.4

0.012

-

mutant enzyme D349R, at pH 7.4 and 25°C

764083

1.3.3.4

0.0131

-

wild-type enzyme, pH 7.5, temperature not specified in the publication

712895

1.3.3.4

0.0181

-

mutant F227R, pH 7.5, temperature not specified in the publication

712895

1.3.3.4

0.023

-

mutant enzyme D349A, at pH 7.4 and 25°C

764083

1.3.3.4

0.0303

-

pH 7.4, temperature not specified in the publication, mutant L166N

726346, 746243

1.3.3.4

0.04

-

recombinant mutant R59W, pH 8.2

654874

1.3.3.4

0.0495

-

pH 7.4, temperature not specified in the publication, wild-type enzyme

746243

1.3.3.4

0.05

-

pH 7.4, temperature not specified in the publication, wild-type enzyme

726346

1.3.3.4

0.055

-

pH 7.4, temperature not specified in the publication, mutant R168S

726346

1.3.3.4

0.0553

-

pH 7.4, temperature not specified in the publication, mutant R168S

746243

1.3.3.4

0.07

-

mutant enzyme R59A, at pH 7.4 and 25°C

764083

1.3.3.4

0.0727

-

pH 7.4, temperature not specified in the publication, mutant F331A

746243

1.3.3.4

0.073

-

pH 7.4, temperature not specified in the publication, mutant F331A

726346

1.3.3.4

0.08

-

pH 8.1, 37°C, recombinant mutant N44I

744202

1.3.3.4

0.0867

-

-

391005

1.3.3.4

0.092

-

mutant enzyme R59E, at pH 7.4 and 25°C

764083

1.3.3.4

0.117

-

pH and temperature not specified in the publication

765577

1.3.3.4

0.124

-

-

390994

1.3.3.4

0.128

-

pH 7.4, temperature not specified in the publication, mutant V170T

726346

1.3.3.4

0.1283

-

pH 7.4, temperature not specified in the publication, mutant V170T

746243

1.3.3.4

0.14

-

pH 8.1, 37°C, recombinant mutant W408L

744202

1.3.3.4

0.145

-

mutant enzyme D349E, at pH 7.4 and 25°C

764083

1.3.3.4

0.15

-

recombinant mutant R59I, pH 8.2

654874

1.3.3.4

0.151

-

pH 7.4, temperature not specified in the publication, mutant F331T

726346

1.3.3.4

0.1513

-

pH 7.4, temperature not specified in the publication, mutant F331T

746243

1.3.3.4

0.1548

-

pH 7.4, temperature not specified in the publication, mutant M368Q

746243

1.3.3.4

0.155

-

mutant enzyme T366A, at pH 7.4 and 25°C

764083

1.3.3.4

0.155

-

pH 7.4, temperature not specified in the publication, mutant M368Q

726346

1.3.3.4

0.17

-

recombinant mutant R59S, pH 8.2

654874

1.3.3.4

0.175

-

-

391004, 391007

1.3.3.4

0.175

-

wild type enzyme

391002

1.3.3.4

0.192

-

wild type enzyme, at pH 7.4 and 25°C

764083

1.3.3.4

0.21

-

mutant enzyme R59K, at pH 7.4 and 25°C

764083

1.3.3.4

0.236

-

pH 7.4, temperature not specified in the publication, mutant M368K

726346

1.3.3.4

0.2362

-

pH 7.4, temperature not specified in the publication, mutant M368K

746243

1.3.3.4

0.295

-

-

390988

1.3.3.4

0.32

-

pH 8.1, 37°C, recombinant mutant N44Q

744202

1.3.3.4

0.32

-

pH 8.1, 37°C, recombinant mutant W408Y

744202

1.3.3.4

0.42

-

pH 8.1, 37°C, recombinant mutant S20A

744202

1.3.3.4

0.53

-

recombinant mutant Y348, pH 7.8

654874

1.3.3.4

0.72

-

pH 8.1, 37°C, recombinant wild-type enzyme

744202

1.3.3.4

0.78

-

pH 8.1, 37°C, recombinant mutant S20T

744202

1.3.3.4

0.853

-

pH 7.4, temperature not specified in the publication, mutant L334V

726346

1.3.3.4

0.8532

-

pH 7.4, temperature not specified in the publication, mutant L334V

746243

1.3.3.4

1.02

-

recombinant mutant R168C, pH 8.2

654874

1.3.3.4

1.273

-

pH 7.4, temperature not specified in the publication, mutant R97G

726346, 746243

1.3.3.4

1.52

-

pH 8.1, 37°C, recombinant mutant E39D

744202

1.3.3.4

2.57

-

recombinant mutant R59K, pH 8.2

654874

1.3.3.4

3.9

-

recombinant mutant G14A, pH 8.2

654874

1.3.3.4

5.95

-

recombinant wild-type enzyme, pH 8.2

654874

1.3.3.4

6

-

pH 7.4, temperature not specified in the publication, wild-type enzyme

726346

1.3.3.4

6

-

wild type enzyme PPO2, at 20°C

671892

1.3.3.4

6

-

wild-type

671892

1.3.3.4

7

-

L372N

671892

1.3.3.4

7

-

mutant enzyme L372N, at 20°C

671892

1.3.3.4

11

-

F392E

671892

1.3.3.4

11

-

mutant enzyme F392E, at 20°C

671892

1.3.3.4

12

-

mutant enzyme N67W/S374D, at 20°C

671892

1.3.3.4

12

-

N67W/S374D

671892

1.3.3.4

12.9

-

recombinant mutant V311M, pH 7.4, 25°C

654950

1.3.3.4

14.1

-

recombinant wild-type enzyme, pH 7.4, 25°C

654950

1.3.3.4

34

-

mutant enzyme R98E, at 20°C

671892

1.3.3.4

34

-

R98E

671892

1.3.3.4

37

-

mutant enzyme R98K, at 20°C

671892

1.3.3.4

37

-

R98K

671892

1.3.3.4

38

-

L356N

671892

1.3.3.4

38

-

mutant enzyme L356N, at 20°C

671892

1.3.3.4

97

-

mutant enzyme N67R, at 20°C

671892

1.3.3.4

97

-

N67R

671892

1.3.3.4

111

-

mutant enzyme N67R/S374D, at 20°C

671892

1.3.3.4

111

-

N67R/S374D

671892

1.3.3.4

208

-

mutant enzyme S374D, at 20°C

671892

1.3.3.4

300

-

L356V

671892

1.3.3.4

300

-

mutant enzyme L356V, at 20°C

671892

1.3.3.4

365

-

pH 7.4, temperature not specified in the publication, mutant R98A

726346

1.3.3.4

365

-

mutant enzyme R98A, at 20°C

671892

1.3.3.4

365

-

R98A

671892

1.3.3.4

597

-

L372V

671892

1.3.3.4

597

-

mutant enzyme L372V, at 20°C

671892

1.3.3.15

3 entries

1.3.3.4

90 entries

1.3.5.3

0.292

-

pH 8.0, 37°C

696347

K_M Value (112 results)

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Show KM Value (112 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.3.3.15

0.001

-

at pH 8.7 and 37°C

391011

1.3.3.15

0.0077

-

pH and temperature not specified in the publication

765577

1.3.3.15

0.0091

-

pH and temperature not specified in the publication

765577

1.3.3.4

0.00002

-

-

391006

1.3.3.4

0.0001

-

-

391001

1.3.3.4

0.00016

-

pH 7.2

390986

1.3.3.4

0.00033

-

pH 8.0

390986

1.3.3.4

0.00038

-

pH 8.1, 37°C, recombinant wild-type enzyme

744202

1.3.3.4

0.0005

-

-

390991

1.3.3.4

0.00051

-

pH 8.1, 37°C, recombinant mutant N44I

744202

1.3.3.4

0.00051

-

pH 8.1, 37°C, recombinant mutant W408L

744202

1.3.3.4

0.00055

-

pH 8.5

390986

1.3.3.4

0.00059

-

pH 8.1, 37°C, recombinant mutant E39D

744202

1.3.3.4

0.00067

-

pH 7.5, 22°C, recombinant wild-type enzyme

695527

1.3.3.4

0.00074

-

pH 8.1, 37°C, recombinant mutant N44Q

744202

1.3.3.4

0.00078

-

in phospholipid vesicles

34955

1.3.3.4

0.00083

-

recombinant mutant R59K, pH 8.2

654874

1.3.3.4

0.00085

-

recombinant wild-type enzyme and mutant G14A, pH 8.2

654874

1.3.3.4

0.00092

-

pH 8.1, 37°C, recombinant mutant S20A

744202

1.3.3.4

0.001

-

about, pH 7.4, temperature not specified in the publication

711307

1.3.3.4

0.001

-

mutant F227R, pH 7.5, temperature not specified in the publication

712895

1.3.3.4

0.001

-

mutant I176A, pH 7.5, temperature not specified in the publication

712895

1.3.3.4

0.001

-

mutant K71A, pH 7.5, temperature not specified in the publication

712895

1.3.3.4

0.001

-

mutant P64A, pH 7.5, temperature not specified in the publication

712895

1.3.3.4

0.001

-

wild-type enzyme, pH 7.5, temperature not specified in the publication

712895

1.3.3.4

0.001

-

-

391011, 671294

1.3.3.4

0.001

-

recombinant mutant R168C, pH 8.2

654874

1.3.3.4

0.00107

-

pH 7.5, 22°C, recombinant mutant Y366A

695527

1.3.3.4

0.00107

-

recombinant mutant Y348, pH 7.8

654874

1.3.3.4

0.001162

-

mutant enzyme R59A, at pH 7.4 and 25°C

764083

1.3.3.4

0.00117

-

pH 7.4, temperature not specified in the publication, wild-type enzyme

726346

1.3.3.4

0.00117

-

pH 8.1, 37°C, recombinant mutant S20T

744202

1.3.3.4

0.00117

-

wild type enzyme PPO2, at 20°C

671892

1.3.3.4

0.00117

-

wild-type

671892

1.3.3.4

0.001253

-

mutant enzyme D349E, at pH 7.4 and 25°C

764083

1.3.3.4

0.00126

-

recombinant mutant R59W, pH 8.2

654874

1.3.3.4

0.0014

-

mutant enzyme N67R/S374D, at 20°C

671892

1.3.3.4

0.0014

-

N67R/S374D

671892

1.3.3.4

0.001405

-

wild type enzyme, at pH 7.4 and 25°C

764083

1.3.3.4

0.00149

-

pH 8.1, 37°C, recombinant mutant W408Y

744202

1.3.3.4

0.0016

-

-

391005

1.3.3.4

0.0017

-

-

391004, 391007

1.3.3.4

0.0017

-

recombinant mutant R59S, pH 8.2

654874

1.3.3.4

0.0017

-

wild type and R59W mutant enzyme

391002

1.3.3.4

0.001768

-

mutant enzyme T366A, at pH 7.4 and 25°C

764083

1.3.3.4

0.001865

-

mutant enzyme R59K, at pH 7.4 and 25°C

764083

1.3.3.4

0.002

-

in detergent solution in presence of cardiolipin

34955

1.3.3.4

0.00208

-

mutant enzyme D349A, at pH 7.4 and 25°C

764083

1.3.3.4

0.00208

-

pH 7.4, temperature not specified in the publication, wild-type enzyme

746243

1.3.3.4

0.00209

-

recombinant mutant R59I, pH 8.2

654874

1.3.3.4

0.0021

-

pH 7.4, temperature not specified in the publication, wild-type enzyme

726346

1.3.3.4

0.0021

-

-

390988

1.3.3.4

0.00217

-

pH 7.4, temperature not specified in the publication, mutant G169A

746243

1.3.3.4

0.0022

-

pH 7.4, temperature not specified in the publication, mutant G169A

726346

1.3.3.4

0.00234

-

pH 7.5, 22°C, recombinant mutant Y366E

695527

1.3.3.4

0.0026

-

mutant enzyme R98K, at 20°C

671892

1.3.3.4

0.0026

-

R98K

671892

1.3.3.4

0.00298

-

mutant enzyme R59E, at pH 7.4 and 25°C

764083

1.3.3.4

0.00298

-

pH 7.4, temperature not specified in the publication, mutant V170T

746243

1.3.3.4

0.003

-

pH 7.4, temperature not specified in the publication, mutant V170T

726346

1.3.3.4

0.00302

-

pH 7.4, temperature not specified in the publication, mutant F331T

726346

1.3.3.4

0.00303

-

pH 7.4, temperature not specified in the publication, mutant F331T

746243

1.3.3.4

0.0032

-

recombinant wild-type enzyme and recombinant mutant V311M, pH 7.4, 25°C

654950

1.3.3.4

0.00354

-

pH 7.5, 22°C, recombinant mutant Y366H

695527

1.3.3.4

0.00358

-

mutant enzyme D349R, at pH 7.4 and 25°C

764083

1.3.3.4

0.0036

-

-

671294

1.3.3.4

0.0038

-

-

671294

1.3.3.4

0.0048

-

-

390982

1.3.3.4

0.0051

-

pH 7.4, temperature not specified in the publication, mutant L166N

726346

1.3.3.4

0.00514

-

pH 7.4, temperature not specified in the publication, mutant L166N

746243

1.3.3.4

0.0056

-

pH 7.4, temperature not specified in the publication, mutant M368K

726346

1.3.3.4

0.0056

-

-

390990

1.3.3.4

0.0056

-

in detergent solution

34955

1.3.3.4

0.00564

-

pH 7.4, temperature not specified in the publication, mutant M368K

746243

1.3.3.4

0.0063

-

-

391016

1.3.3.4

0.0066

-

pH 7.4, temperature not specified in the publication, mutant F331A

726346

1.3.3.4

0.0066

-

-

390994

1.3.3.4

0.00661

-

pH 7.4, temperature not specified in the publication, mutant F331A

746243

1.3.3.4

0.007

-

pH 7.5, 25°C

695546

1.3.3.4

0.00709

-

pH 7.4, temperature not specified in the publication, mutant L334V

746243

1.3.3.4

0.0071

-

pH 7.4, temperature not specified in the publication, mutant L334V

726346

1.3.3.4

0.0073

-

L356V

671892

1.3.3.4

0.0073

-

mutant enzyme L356V, at 20°C

671892

1.3.3.4

0.0083

-

pH 7.4, temperature not specified in the publication, mutant R98A

726346

1.3.3.4

0.0083

-

mutant enzyme R98A, at 20°C

671892

1.3.3.4

0.0083

-

R98A

671892

1.3.3.4

0.0096

-

pH and temperature not specified in the publication

765577

1.3.3.4

0.0109

-

mutant enzyme S374D, at 20°C

671892

1.3.3.4

0.0109

-

S374D

671892

1.3.3.4

0.011

-

-

390981

1.3.3.4

0.011

-

L356N

671892

1.3.3.4

0.011

-

mutant enzyme L356N, at 20°C

671892

1.3.3.4

0.0112

-

F392E

671892

1.3.3.4

0.0112

-

mutant enzyme F392E, at 20°C

671892

1.3.3.4

0.0113

-

pH 7.4, temperature not specified in the publication, mutant R168S

726346

1.3.3.4

0.01134

-

pH 7.4, temperature not specified in the publication, mutant R168S

746243

1.3.3.4

0.0125

-

mutant enzyme R98E, at 20°C

671892

1.3.3.4

0.0125

-

R98E

671892

1.3.3.4

0.0139

-

pH 7.4, temperature not specified in the publication, mutant M368Q

746243

1.3.3.4

0.014

-

pH 7.4, temperature not specified in the publication, mutant M368Q

726346

1.3.3.4

0.0164

-

L372N

671892

1.3.3.4

0.0164

-

mutant enzyme L372N, at 20°C

671892

1.3.3.4

0.0166

-

-

390992

1.3.3.4

0.0196

-

pH 7.4, temperature not specified in the publication, mutant R97G

726346

1.3.3.4

0.01965

-

pH 7.4, temperature not specified in the publication, mutant R97G

746243

1.3.3.4

0.021

-

mutant enzyme N67W/S374D, at 20°C

671892

1.3.3.4

0.021

-

N67W/S374D

671892

1.3.3.4

0.097

-

mutant enzyme N67R, at 20°C

671892

1.3.3.4

0.097

-

N67R

671892

1.3.3.4

0.103

-

L372V

671892

1.3.3.4

0.103

-

mutant enzyme L372V, at 20°C

671892

1.3.3.15

3 entries

1.3.3.4

108 entries

1.3.5.3

0.007

-

pH 8.0, 37°C

696347

K_i Value (1 result)

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Show KI Value (1 entry)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.3.3.15

0.0003

-

at pH 7.2 and 30°C

738501

References & Links

Literature References (136)

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Show Reference (136 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

34955

3558411

Reconstitution of the two terminal enzymes of the heme biosynthetic pathway into phospholipid vesicles

1987

Ferreira, G.C.; Dailey, H.A.

J. Biol. Chem.

262

4407-4412

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

390981

6461

The enzymic conversion of protoporphyrinogen IX to protoporphyrin IX in mammalian mitochondria

1976

Poulson, R.

J. Biol. Chem.

251

3730-3733

390982

234450

The enzymic conversion of protoporphyrinogen IX to protoporphyrin IX. Protoporphyrinogen oxidase activity in mitochondrial extracts of Saccharomyces cerevisiae

1975

Poulson, R.; Polglase, W.J.

J. Biol. Chem.

250

1269-1274

390983

7052077

A new assay for protoporphyrinogen oxidase - evidence for a total deficiency in that activity in a heme-less mutant of Saccharomyces cerevisiae

1982

Camadro, J.M.; Urban-Grimal, D.; Labbe, P.

Biochem. Biophys. Res. Commun.

106

724-730

390984

-

Mechanism and stereochemistry of the porphobilinogen deaminase and protoporphyrinogen IX oxidase reactions: Stereospecific manipulation of hydrogen atoms at the for methylene bridges

1984

Jones, C.; Jordan, P.M.; Akhtar, M.

J. Chem. Soc. Perkin Trans. I

1984

2625-2633

390985

3996415

The mitochondrial location of protoporphyrinogen oxidase

1985

Deybach, J.C.; Da Silva, V.; Grandchamp, B.; Nordmann, Y.

Eur. J. Biochem.

149

431-435

390986

4051500

Kinetic properties of the membrane-bound human liver mitochondrial protoporphyrinogen oxidase

1985

Camadro, J.M.; Abraham, N.G.; Levere, R.D.

Arch. Biochem. Biophys.

242

206-212

390987

2451512

Haem biosynthesis in the Gunn rat

1986

McColl, K.E.L.; Bond, F.M.; Thompson, G.G.; Moore, M.R.

Biochem. Soc. Trans.

14

921-922

390988

3667528

Purification and properties of protoporphyrinogen oxidase from an anaerobic bacterium, Desulfovibrio gigas

1987

Klemm, D.J.; Barton, L.L.

J. Bacteriol.

169

5209-5215

390990

3606986

Purification and characterization of murine protoporphyrinogen oxidase

1987

Dailey, H.A.; Karr, S.W.

Biochemistry

26

2697-2701

390991

3663113

Oxidation of protoporphyrinogen to protoporphyrin, a step in chlorophyll and haem biosynthesis. Purification and partial characterization of the enzyme from barley organelles

1987

Jacobs, J.M.; Jacobs, N.J.

Biochem. J.

244

219-224

390992

2439126

Purification of bovine protoporphyrinogen oxidase: immunological cross-reactivity and structural relationship to ferrochelatase

1987

Siepker, L.J.; Ford, M.; de Kock, R.; Kramer, S.

Biochim. Biophys. Acta

913

349-358

390993

3663105

An HPLC assay for protoporphyrinogen oxidase activity in rat liver

1987

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

Biochem. J.

243

863-866

390994

2451512

Mouse protoporphyrinogen oxidase. Kinetic parameters and demonstration of inhibition by bilirubin

1988

Ferreira, G.C.; Dailey, H.A.

Biochem. J.

250

597-603

390995

3346226

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Processes

9

1-16

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