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Ligand coproporphyrin III

Basic Ligand Information

Molecular Structure

Related pathways

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (5 results)

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Show Natural Substrate (5 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

4.99.1.9

coproporphyrin III + Fe2+ = Fe-coproporphyrin III + 2 H+

739547, 775669, 771056, 771075

8AW7, 3D-view

4.99.1.9

coproporphyrin III + Fe2+ = Fe-coproporphyrin III + 2 H+

739547, 775669, 771056, 771075

8BBV, 3D-view

4.99.1.9

coproporphyrin III + Fe2+ = Fe-coproporphyrin III + 2 H+

739547, 775669, 771056, 771075

8OFL, 3D-view

4.99.1.9

coproporphyrin III + Fe2+ = Fe-coproporphyrin III + 2 H+

739547, 775669, 771056, 771075

8OMM, 3D-view

4.99.1.9

coproporphyrin III + Fe2+ = Fe-coproporphyrin III + 2 H+

739547, 775669, 771056, 771075

9F0F, 3D-view

4.99.1.9

5 entries

In Vivo Product in Enzyme-catalyzed Reactions (3 results)

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Show Natural Product (3 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

-

-

1.3.3.15

coproporphyrinogen III + O2 = coproporphyrin III + H2O

-

-

1.3.3.15

2 entries

1.3.3.3

coproporphyrinogen III + O2 = coproporphyrin III + H2O

-

-

Substrate in Enzyme-catalyzed Reactions (21 results)

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Show Substrate (21 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.98.6

coproporphyrin III + 2 S-adenosyl-L-methionine = ? + 2 CO2 + 2 5'-deoxyadenosine + 2 L-methionine

753257

-

4.99.1.9

coproporphyrin III + Co2+ = Co-coproporphyrin III + 2 H+

739547

8AW7, 3D-view

4.99.1.9

coproporphyrin III + Co2+ = Co-coproporphyrin III + 2 H+

739547

8BBV, 3D-view

4.99.1.9

coproporphyrin III + Co2+ = Co-coproporphyrin III + 2 H+

739547

8OFL, 3D-view

4.99.1.9

coproporphyrin III + Co2+ = Co-coproporphyrin III + 2 H+

739547

8OMM, 3D-view

4.99.1.9

coproporphyrin III + Co2+ = Co-coproporphyrin III + 2 H+

739547

9F0F, 3D-view

4.99.1.9

coproporphyrin III + Cu2+ = Cu-coproporphyrin III + 2 H+

739547

8AW7, 3D-view

4.99.1.9

coproporphyrin III + Cu2+ = Cu-coproporphyrin III + 2 H+

739547

8BBV, 3D-view

4.99.1.9

coproporphyrin III + Cu2+ = Cu-coproporphyrin III + 2 H+

739547

8OFL, 3D-view

4.99.1.9

coproporphyrin III + Cu2+ = Cu-coproporphyrin III + 2 H+

739547

8OMM, 3D-view

4.99.1.9

coproporphyrin III + Cu2+ = Cu-coproporphyrin III + 2 H+

739547

9F0F, 3D-view

4.99.1.9

coproporphyrin III + Fe2+ = Fe-coproporphyrin III + 2 H+

739547, 775669, 771056, 771075

8AW7, 3D-view

4.99.1.9

coproporphyrin III + Fe2+ = Fe-coproporphyrin III + 2 H+

739547, 775669, 771056, 771075

8BBV, 3D-view

4.99.1.9

coproporphyrin III + Fe2+ = Fe-coproporphyrin III + 2 H+

739547, 775669, 771056, 771075

8OFL, 3D-view

4.99.1.9

coproporphyrin III + Fe2+ = Fe-coproporphyrin III + 2 H+

739547, 775669, 771056, 771075

8OMM, 3D-view

4.99.1.9

coproporphyrin III + Fe2+ = Fe-coproporphyrin III + 2 H+

739547, 775669, 771056, 771075

9F0F, 3D-view

4.99.1.9

coproporphyrin III + Ni2+ = Ni-coproporphyrin III + 2 H+

739547

8AW7, 3D-view

4.99.1.9

coproporphyrin III + Ni2+ = Ni-coproporphyrin III + 2 H+

739547

8BBV, 3D-view

4.99.1.9

coproporphyrin III + Ni2+ = Ni-coproporphyrin III + 2 H+

739547

8OFL, 3D-view

4.99.1.9

coproporphyrin III + Ni2+ = Ni-coproporphyrin III + 2 H+

739547

8OMM, 3D-view

4.99.1.9

coproporphyrin III + Ni2+ = Ni-coproporphyrin III + 2 H+

739547

9F0F, 3D-view

4.99.1.9

20 entries

Product in Enzyme-catalyzed Reactions (4 results)

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Show Product (4 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.3.15

coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2

-

-

1.3.3.15

coproporphyrinogen III + O2 = coproporphyrin III + H2O

-

-

1.3.3.15

2 entries

1.3.3.3

coproporphyrinogen III + O2 = coproporphyrin III + H2O

-

-

1.3.3.4

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

-

-

Inhibitor in Enzyme-catalyzed Reactions (3 results)

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Show Inhibitors (3 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.3.3.3

52% inhibition at 0.0194 mM

390971

-

1.3.3.3

competitive inhibitor

738987

-

1.3.3.3

2 entries

4.1.1.37

-

4445

-

3D Structure of Enzyme-Ligand-Complex (PDB) (11 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (11 entries)

EC NUMBER

ENZYME 3D STRUCTURE

4.99.1.1

8AT8, 3D-view

4.99.1.9

8AW7, 3D-view

4.99.1.9

8BBV, 3D-view

4.99.1.9

8OFL, 3D-view

4.99.1.9

8OMM, 3D-view

4.99.1.9

9F0F, 3D-view

4.99.1.9

8AW7, 3D-view

4.99.1.9

8BBV, 3D-view

4.99.1.9

8OFL, 3D-view

4.99.1.9

8OMM, 3D-view

4.99.1.9

9F0F, 3D-view

4.99.1.9

10 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (2 results)

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Show Turnover Number (2 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

4.99.1.9

0.0078

-

pH 7.5, 37°C

739547

4.99.1.9

0.03

-

pH 7.5, 37°C

739547

4.99.1.9

2 entries

K_M Value (2 results)

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Show KM Value (2 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

4.99.1.9

0.0018

-

pH 7.5, 37°C

739547

4.99.1.9

0.0105

-

pH 7.5, 37°C

739547

4.99.1.9

2 entries

References & Links

Literature References (9)

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Show Reference (9 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

4445

8352737

Purification and properties of the uroporphyrinogen decarboxylase from Rhodobacter sphaeroides

1993

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

Biochem. J.

293

703-712

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

738987

9251002

Purification and properties of coproporphyrinogen III oxidase from yeast

1997

Labbe, P.

Methods Enzymol.

281

367-378

739547

25646457

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

2015

Dailey, H.A.; Gerdes, S.; Dailey, T.A.; Burch, J.S.; Phillips, J.D.

Proc. Natl. Acad. Sci. USA

112

2210-2215

753257

30155111

The auxiliary [4Fe-4S] cluster of the radical SAM heme synthase from Methanosarcina barkeri is involved in electron transfer

2016

Kuehner, M.; Schweyen, P.; Hoffmann, M.; Ramos, J.; Reijerse, E.; Lubitz, W.; Broering, M.; Layer, G.

Chem. Sci.

7

4633-4643

753257

30155111

The auxiliary [4Fe-4S] cluster of the radical SAM heme synthase from Methanosarcina barkeri is involved in electron transfer

2016

Kuehner, M.; Schweyen, P.; Hoffmann, M.; Ramos, J.; Reijerse, E.; Lubitz, W.; Broering, M.; Layer, G.

Chem. Sci.

7

4633-4643

753257

2 entries

771056

31794133

Crystal structures and calorimetry reveal catalytically relevant binding mode of coproporphyrin and coproheme in coproporphyrin ferrochelatase

2020

Hofbauer, S.; Helm, J.; Obinger, C.; Djinovic-Carugo, K.; Furtmueller, P.G.

FEBS J.

287

2779-2796

771075

34719106

Substrate specificity and complex stability of coproporphyrin ferrochelatase is governed by hydrogen-bonding interactions of the four propionate groups

2022

Gabler, T.; Sebastiani, F.; Helm, J.; Dali, A.; Obinger, C.; Furtmueller, P.G.; Smulevich, G.; Hofbauer, S.

FEBS J.

289

1680-1699

775669

36479958

Active site architecture of coproporphyrin ferrochelatase with its physiological substrate coproporphyrin III propionate interactions and porphyrin core deformation

2023

Dali, A.; Gabler, T.; Sebastiani, F.; Destinger, A.; Furtmueller, P.G.; Pfanzagl, V.; Becucci, M.; Smulevich, G.; Hofbauer, S.

Protein Sci.

32

e4534

Links to other databases for coproporphyrin III

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Show Links (1 entry)