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Ligand protochlorophyllide

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for protochlorophyllide

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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

1.3.1.33

monovinyl protochlorophyllide a + NADPH = monovinyl chlorophyllide a + NADP+

671845

-

1.3.1.33

protochlorophyllide + NADH + H+ = chlorophyllide a + NAD+

740022

7jk9, 3D-view

1.3.1.33

protochlorophyllide + NADPH + H+ = chlorophyllide + NADP+

700814, 700943, 700758, 697892, 697680, 696149, 696150, 695583, 696223, 698913, 698961, 699004, 700718

7jk9, 3D-view

1.3.1.33

protochlorophyllide + NADPH + H+ = chlorophyllide a + NADP+

740086, 741187, 740022, 740071, 741157, 741184, 741337, 741108, 737615, 740446, 741396, 741255, 726255, 763100, 741099, 740894, 762601, 741021, 763334, 763678, 763023

7jk9, 3D-view

1.3.1.33

protochlorophyllide + NADPH = chlorophyllide + NADP+

393836, 393838, 393842, 393857, 393849, 393850, 393840, 393858, 393862, 393863, 393865, 393856, 393843, 393844, 393846, 393847, 393848, 393851, 393853, 393855, 393833, 393839, 393841, 393852, 393859, 393860, 393854, 393864, 393866, 393861, 393835, 393837, 393845, 654419, 699004, 656908, 393834, 393832, 657112, 657010, 654705, 656982, 657001, 656904, 656905

7jk9, 3D-view

1.3.1.33

protochlorophyllide + reduced ferredoxin = chlorophyllide + oxidized ferredoxin

687688

7jk9, 3D-view

1.3.1.33

protochlorophyllide a + NADPH + H+ = chlorophyllide a + NADP+

654842

-

1.3.1.33

7 entries

1.3.1.75

protochlorophyllide a + NADP+ = 3,8-divinyl protochlorophyllide a + NADPH + H+

765263

-

1.3.7.13

protochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster = 8-vinyl protochlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+

762912

-

1.3.7.13

protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster = 3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+

738520, 736444, 738542, 728467, 737646

-

1.3.7.13

2 entries

1.3.7.15

protochlorophyllide + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+ = chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate

737615

-

1.3.7.7

protochlorophyllide + oxidized ferredoxin + ADP + phosphate = chlorophyllide a + reduced ferredoxin + ATP

713251, 713252, 712268

2ynm, 3D-view

1.3.7.7

protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O = chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate

726526, 726255, 725412, 725877, 726394, 726104

-

1.3.7.7

2 entries

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

1.14.13.81

magnesium-protoporphyrin IX 13-monomethyl ester + NADPH + H+ + O2 = magnesium-protochlorophyllide + NADP+ + H2O

0

-

1.14.13.81

Mg-protoporphyrin IX monomethyl ester + O2 + NADPH + H+ = Mg-protochlorophyllide + NADP+ + H2O

0

-

1.14.13.81

magnesium-protoporphyrin IX monomethyl ester + NADPH + H+ + O2 = protochlorophyllide a + NADP+ + H2O

0

-

1.14.13.81

3 entries

1.3.1.33

chlorophyllide a + NADP+ = protochlorophyllide + NADPH + H+

0

7jk9, 3D-view

1.3.1.75

3,8-divinyl protochlorophyllide a + NADPH + H+ = protochlorophyllide a + NADP+

0

-

1.3.1.75

3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+ = protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster

0

-

1.3.1.75

8-vinyl protochlorophyllide a + NADPH + H+ = protochlorophyllide a + NADP+

0

-

1.3.7.13

3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+ + NADPH + H+ = protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+

0

-

1.3.7.13

3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+ = protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster

0

-

1.3.7.13

3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+ = protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+

0

-

1.3.7.13

8-vinyl protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster = protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+

0

-

1.3.7.7

chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O = protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+

0

2ynm, 3D-view

1.3.7.7

chlorophyllide a + reduced ferredoxin + ATP = protochlorophyllide + oxidized ferredoxin + ADP + phosphate

0

2ynm, 3D-view

1.3.1.75

3 entries

1.3.7.13

4 entries

1.3.7.7

2 entries

Substrate in Enzyme-catalyzed Reactions (19 results)

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Show Substrate (19 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.122

protochlorophyllide a + O2 + NADPH = 7-hydroxychlorophyllide a + H2O + NADP+

663257

-

1.3.1.33

C8-ethyl-C13(2)-(r)-protochlorophyllide + NADPH = ? + NADP+

393864

-

1.3.1.33

monovinyl protochlorophyllide a + NADPH = monovinyl chlorophyllide a + NADP+

671845

-

1.3.1.33

protochlorophyllide + dithionite = chlorophyllide + SO2

687688

7jk9, 3D-view

1.3.1.33

protochlorophyllide + dithiothreitol = chlorophyllide + oxidized dithiothreitol

687688

7jk9, 3D-view

1.3.1.33

protochlorophyllide + NADH + H+ = chlorophyllide a + NAD+

740022

7jk9, 3D-view

1.3.1.33

protochlorophyllide + NADPH + H+ = chlorophyllide + NADP+

689394, 689396, 700814, 700943, 689772, 689784, 686758, 700758, 697892, 697680, 696149, 696150, 695583, 696223, 698913, 698961, 699004, 700718

7jk9, 3D-view

1.3.1.33

protochlorophyllide + NADPH + H+ = chlorophyllide a + NADP+

393849, 740086, 741187, 740022, 740071, 741157, 741184, 741337, 741108, 737615, 740446, 741396, 741255, 726255, 763100, 741099, 740894, 762601, 741021, 763334, 763678, 763023

7jk9, 3D-view

1.3.1.33

protochlorophyllide + NADPH = chlorophyllide + NADP+

393836, 393838, 393842, 393857, 393849, 393850, 393840, 393858, 393862, 393863, 393865, 393856, 393843, 393844, 393846, 393847, 393848, 393851, 393853, 393855, 656911, 393832, 393833, 393834, 393839, 393841, 393852, 393859, 393860, 657112, 393854, 393864, 393866, 656904, 656908, 656905, 393861, 657010, 393835, 393837, 393845, 672324, 654419, 676324, 699004, 654705, 656982, 657001, 654842, 656854

7jk9, 3D-view

1.3.1.33

protochlorophyllide + reduced ferredoxin = chlorophyllide + oxidized ferredoxin

687688

7jk9, 3D-view

1.3.1.33

protochlorophyllide a + NADPH + H+ = chlorophyllide a + NADP+

689393, 656908, 654842, 687767, 687626

-

1.3.1.33

10 entries

1.3.1.75

protochlorophyllide a + NADP+ = 3,8-divinyl protochlorophyllide a + NADPH + H+

765263

-

1.3.7.13

protochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster = 8-vinyl protochlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+

762912

-

1.3.7.13

protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster = 3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+

738520, 736444, 738542, 728467, 737646

-

1.3.7.15

protochlorophyllide + reduced dithionite + ATP + H2O + H+ = chlorophyllide a + oxidized dithionite + ADP + phosphate

737615

-

1.3.7.15

protochlorophyllide + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+ = chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate

737615

-

1.3.7.7

protochlorophyllide + oxidized ferredoxin + ADP + phosphate = chlorophyllide a + reduced ferredoxin + ATP

393862, 672324, 686758, 713251, 713252, 712268, 700718, 711198, 712026

2ynm, 3D-view

1.3.7.7

protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O = chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate

726526, 726255, 725412, 725877, 726394, 726104

-

1.3.7.7

protochlorophyllide a + reduced ferredoxin + 4 ATP + 4 H2O = chlorophyllide a + oxidized ferredoxin + 4 ADP + 4 phosphate

741827

-

1.3.7.13

2 entries

1.3.7.15

2 entries

1.3.7.7

3 entries

Product in Enzyme-catalyzed Reactions (13 results)

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Show Product (13 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.81

magnesium-protoporphyrin IX 13-monomethyl ester + NADPH + H+ + O2 = magnesium-protochlorophyllide + NADP+ + H2O

0

-

1.14.13.81

Mg-protoporphyrin IX monomethyl ester + O2 + NADPH + H+ = Mg-protochlorophyllide + NADP+ + H2O

0

-

1.14.13.81

magnesium-protoporphyrin IX monomethyl ester + NADPH + H+ + O2 = protochlorophyllide a + NADP+ + H2O

0

-

1.14.13.81

3 entries

1.3.1.33

chlorophyllide a + NADP+ = protochlorophyllide + NADPH + H+

0

7jk9, 3D-view

1.3.1.75

3,8-divinyl protochlorophyllide a + NADPH + H+ = protochlorophyllide a + NADP+

0

-

1.3.1.75

3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+ = protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster

0

-

1.3.1.75

8-vinyl protochlorophyllide a + NADPH + H+ = protochlorophyllide a + NADP+

0

-

1.3.7.13

3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+ + NADPH + H+ = protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+

0

-

1.3.7.13

3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+ = protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster

0

-

1.3.7.13

3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+ = protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+

0

-

1.3.7.13

8-vinyl protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster = protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+

0

-

1.3.7.7

chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O = protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+

0

2ynm, 3D-view

1.3.7.7

chlorophyllide a + reduced ferredoxin + ATP = protochlorophyllide + oxidized ferredoxin + ADP + phosphate

0

2ynm, 3D-view

1.3.1.75

3 entries

1.3.7.13

4 entries

1.3.7.7

2 entries

Activator in Enzyme-catalyzed Reactions (1 result)

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Show Activating Compound (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.3.1.33

stringent requirement

393840

7jk9, 3D-view

Inhibitor in Enzyme-catalyzed Reactions (2 results)

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Show Inhibitors (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.3.1.33

-

740086

7jk9, 3D-view

2.1.1.11

-

485107

-

3D Structure of Enzyme-Ligand-Complex (PDB) (2 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (2 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.3.1.33

7jk9, 3D-view

1.3.7.7

2ynm, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (48 results)

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Show Turnover Number (48 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.3.1.33

0.003

-

mutant K197Q

698913

1.3.1.33

0.004

-

mutant K197A

698913

1.3.1.33

0.004

-

mutant K197R

698913

1.3.1.33

0.004

-

mutant Y193S

698913

1.3.1.33

0.007

-

pH 7.5, 40°C, mutant enzyme F233L

763023

1.3.1.33

0.009

-

mutant Y193A

698913

1.3.1.33

0.01

-

mutant enzyme N149V, at 25°C, pH not specified in the publication

740894

1.3.1.33

0.01

-

mutant enzyme T145A, at 25°C, pH not specified in the publication

740894

1.3.1.33

0.01

-

mutant enzyme T147F, at 25°C, pH not specified in the publication

740894

1.3.1.33

0.01

-

mutant enzyme T230F, at 25°C, pH not specified in the publication

740894

1.3.1.33

0.011

-

mutant C199/C226S

699004

1.3.1.33

0.011

-

pH 7.5, 25°C, mutant C199S/C226S, co-substrate: NADPH

699004

1.3.1.33

0.0113

-

mutant C37S/C226S

699004

1.3.1.33

0.0113

-

pH 7.5, 25°C, mutant C37S/C226S, co-substrate: NADPH

699004

1.3.1.33

0.0117

-

mutant C37S/C199S/C226S

699004

1.3.1.33

0.0117

-

pH 7.5, 25°C, mutant C37S/C199S/C226S, co-substrate: NADPH

699004

1.3.1.33

0.0118

-

mutant C226S

699004

1.3.1.33

0.0118

-

pH 7.5, 25°C, mutant C226S, co-substrate: NADPH

699004

1.3.1.33

0.013

-

pH 7.5, 40°C, mutant enzyme F233Y

763023

1.3.1.33

0.013

-

pH 7.5, 40°C, mutant enzyme P158F

763023

1.3.1.33

0.02

-

mutant enzyme N39V, at 25°C, pH not specified in the publication

740894

1.3.1.33

0.02

-

mutant enzyme T147S, at 25°C, pH not specified in the publication

740894

1.3.1.33

0.022

-

pH 7.5, 40°C, mutant enzyme K156N/I157V

763023

1.3.1.33

0.027

-

pH 7.5, 40°C, wild-type enzyme

763023

1.3.1.33

0.03

-

pH 7.5, 40°C, mutant enzyme F237Y

763023

1.3.1.33

0.032

-

mutant Y193F

698913

1.3.1.33

0.035

-

pH 7.5, 40°C, mutant enzyme K156N

763023

1.3.1.33

0.037

-

pH 7.5, 40°C, mutant enzyme I157V

763023

1.3.1.33

0.037

-

pH 7.5, 40°C, mutant enzyme P158A

763023

1.3.1.33

0.07

-

mutant enzyme N90A, at 25°C, pH not specified in the publication

740894

1.3.1.33

0.1

-

mutant enzyme H236A, at 25°C, pH not specified in the publication

740894

1.3.1.33

0.16

-

mutant enzyme G19A, at 25°C, pH not specified in the publication

740894

1.3.1.33

0.16

-

mutant enzyme K42A, at 25°C, pH not specified in the publication

740894

1.3.1.33

0.16

-

mutant enzyme R38V, at 25°C, pH not specified in the publication

740894

1.3.1.33

0.16

-

mutant enzyme S16C, at 25°C, pH not specified in the publication

740894

1.3.1.33

0.16

-

mutant enzyme S189A, at 25°C, pH not specified in the publication

740894

1.3.1.33

0.16

-

mutant enzyme T230A, at 25°C, pH not specified in the publication

740894

1.3.1.33

0.16

-

mutant enzyme T230S, at 25°C, pH not specified in the publication

740894

1.3.1.33

0.162

-

mutant C199S

699004

1.3.1.33

0.162

-

pH 7.5, 25°C, mutant C199S, co-substrate: NADPH

699004

1.3.1.33

0.163

-

mutant C37S/C199S

699004

1.3.1.33

0.164

-

mutant C37S

699004

1.3.1.33

0.164

-

pH 7.5, 25°C, mutant C37S, co-substrate: NADPH

699004

1.3.1.33

0.164

-

wild type enzyme

698913

1.3.1.33

0.165

-

pH 7.5, 25°C, wild-type, co-substrate: NADPH

699004

1.3.1.33

0.165

-

wild type enzyme

699004

1.3.1.33

0.17

-

mutant enzyme Y94F, at 25°C, pH not specified in the publication

740894

1.3.1.33

0.17

-

wild type enzyme, at 25°C, pH not specified in the publication

740894

1.3.1.33

48 entries

K_M Value (50 results)

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Show KM Value (50 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.3.1.33

-999

-

mutant C199/C226S, relative activity 6.6%

699004

1.3.1.33

-999

-

mutant C199S, relative activity 98.2%

699004

1.3.1.33

-999

-

mutant C226S, relative activity 7.2%

699004

1.3.1.33

-999

-

mutant C37S, relative activity 99.4%

699004

1.3.1.33

-999

-

mutant C37S/C199S, relative activity 98.8%

699004

1.3.1.33

-999

-

mutant C37S/C199S/C226S, relative activity 7.1%

699004

1.3.1.33

-999

-

mutant C37S/C226S, relative activity 6.8%

699004

1.3.1.33

-999

-

mutant K197A, relative activity 2.7%

698913

1.3.1.33

-999

-

mutant K197Q, relative activity 2.0%

698913

1.3.1.33

-999

-

mutant K197R, relative activity 2.3%

698913

1.3.1.33

-999

-

mutant Y193A, relative activity 5.5%

698913

1.3.1.33

-999

-

mutant Y193F, relative activity 19.5%

698913

1.3.1.33

-999

-

mutant Y193S, relative activity 2.4%

698913

1.3.1.33

-999

-

wild type enzyme, relative activity 100%

698913, 699004

1.3.1.33

0.00015

-

-

700758

1.3.1.33

0.00018

-

-

393864

1.3.1.33

0.00019

-

-

393856

1.3.1.33

0.00027

-

-

393856

1.3.1.33

0.00027

-

fusion protein with maltose-binding protein

656908

1.3.1.33

0.00039

-

-

700758

1.3.1.33

0.00046

-

-

393856

1.3.1.33

0.00047

-

-

656908

1.3.1.33

0.0005

-

-

700758

1.3.1.33

0.0012

-

pH and temperature not specified in the publication

740086

1.3.1.33

0.00136

-

pH 7.5

671845

1.3.1.33

0.0017

-

pH and temperature not specified in the publication

740086

1.3.1.33

0.0018

-

50°C, pH 7.5

676324

1.3.1.33

0.002

-

pH and temperature not specified in the publication

740086

1.3.1.33

0.0023

-

pH and temperature not specified in the publication

740086

1.3.1.33

0.0024

-

pH and temperature not specified in the publication

740086

1.3.1.33

0.0043

-

pH and temperature not specified in the publication

740086

1.3.1.33

0.0055

-

pH and temperature not specified in the publication

740086

1.3.1.33

0.0061

-

in 100 mM HEPES-NaOH (pH 7.5), 2 mM ATP, 5 mM MgCl2

687688

1.3.1.33

0.0069

-

pH 7.5, 40°C, mutant enzyme F237Y

763023

1.3.1.33

0.0075

-

pH 7.5, 40°C, mutant enzyme F233L

763023

1.3.1.33

0.0077

-

pH and temperature not specified in the publication

740086

1.3.1.33

0.0078

-

pH 7.5, 30°C

763334

1.3.1.33

0.0078

-

pH 7.5, 40°C, wild-type enzyme

763023

1.3.1.33

0.0078

-

pH and temperature not specified in the publication

740086

1.3.1.33

0.0081

-

pH 7.5, 40°C, mutant enzyme F233Y

763023

1.3.1.33

0.0086

-

-

656908

1.3.1.33

0.0106

-

pH 7.4, 34°C

672324

1.3.1.33

0.0107

-

pH 7.5, 40°C, mutant enzyme I157V

763023

1.3.1.33

0.01083

-

-

700758

1.3.1.33

0.0135

-

pH 7.5, 40°C, mutant enzyme P158A

763023

1.3.1.33

0.0151

-

pH 7.5, 40°C, mutant enzyme K156N

763023

1.3.1.33

0.0166

-

pH 7.5, 40°C, mutant enzyme K156N/I157V

763023

1.3.1.33

0.0181

-

pH 7.5, 40°C, mutant enzyme P158F

763023

1.3.1.33

0.035

-

-

393832

1.3.1.33

49 entries

1.3.7.7

0.0106

-

in 100 mM HEPES-KOH (pH 7.4), 5 mM MgCl2, 5 mM dithiothreitol, at 34°C

672324

K_i Value (3 results)

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Show KI Value (3 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.3.1.33

0.00215

-

pH and temperature not specified in the publication

740086

1.3.1.33

0.00322

-

pH and temperature not specified in the publication

740086

1.3.1.33

0.0073

-

pH and temperature not specified in the publication

740086

1.3.1.33

3 entries

References & Links

Literature References (113)

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Show Reference (113 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

393832

31865

Reconstitution of chlorophyllide formation by isolated etioplast membranes

1978

Griffiths, W.T.

Biochem. J.

174

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393833

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The protochlorophyllide holochrome of barley (Hordeum vulgare L.). Isolation and characterization of the NADPH: protochlorophyllide oxidoreductase

1980

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Eur. J. Biochem.

111

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393834

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Substrate-specificity studies on protochlorophyllide reductase in barley (Hordeum vulgare) etioplast membranes

1980

Griffiths, W.T.

Biochem. J.

186

267-278

393835

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Identification of the polypeptides of NADPH--protochlorophyllide oxidoreductase

1980

Oliver, R.P.; Griffiths, W.T.

Biochem. J.

191

277-280

393836

7306062

Purification of the enzyme NADPH: protochlorophyllide oxidoreductase

1981

Beer, N.S.; Griffiths, W.T.

Biochem. J.

195

83-92

393837

6456902

Sub-etioplast localization of the enzyme NADPH: protochlorophyllide oxidoreductase

1981

Luetz, C.; Roeper, U.; Beer, N.S.; Griffiths, T.

Eur. J. Biochem.

118

347-353

393838

7306063

Covalent labelling of the NADPH: protochlorophyllide oxidoreductase from etioplast membranes with [3H]N-phenylmaleimide

1981

Oliver, R.P.; Griffiths, W.T.

Biochem. J.

195

93-101

393839

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Site of synthesis of NADPH protochlorophyllide oxidoreductase in rye (Secale cereale)

1982

Griffiths, W.T.; Beer, N.S.

Plant Physiol.

70

1014-1018

393840

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Characterization of NADPH: Protochlorophyllide oxidoreductase in the y-7 and pc-1 y-7 mutants of Chlamydomonas reinhardtii

1983

Ford, C.; Mitchell, S.; Wang, W.

Mol. Gen. Genet.

192

290-292

393841

6696447

The proteolytic degradation in vitro of the NADPH-protochlorophyllide oxidoreductase of barley (Hordeum vulgare L.)

1984

Haeuser, I.; Dehesh, K.; Apel, K.

Arch. Biochem. Biophys.

228

577-586

393842

24249610

The NADPH-protochlorophyllide oxidoreductase is the major protein constituent of prolamellar bodies in wheat (Triticum aestivum L.)

1985

Dehesh, K.; Ryberg, M.

Planta

164

396-399

393843

24232546

Light-induced changes in the distribution of the 36000-Mr polypeptide of NADPH-protochlorophyllide oxidoreductase within different cellular compartments of barley (Hordeum vulgare L.) I. Localization by immunoblotting in isolated plastids and total leaf extracts

1986

Dehesh, K.; Klaas, M.; Haeuser, I.; Apel, K.

Planta

169

162-171

393844

24232547

Light-induced changes in the distribution of the 36000-Mr polypeptide of NADPH-protochlorophyllide oxidoreductase within different cellular compartments of barley (Hordeum vulgare L.) II. Lacalization by immunogold labelling in ultrathin sections

1986

Dehesh, K.; Van Cleve, B.; Ryberg, H.; Apel, K.

Planta

169

172-183

393845

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Amino acid composition of the enzyme NADPH: protochlorophyllide oxidoreductase

1987

Roeper, U.; Prinz, H.; Luetz, C.

Plant Sci.

52

15-19

393846

3314870

Synthesis of 4R- and 4S-tritium labeled NADPH for the determination of the coenzyme stereospecificity of NADPH: protochlorophyllide oxidoreductase

1987

Valera, V.; Fung, M.; Wessler, A.N.; Richards, W.R.

Biochem. Biophys. Res. Commun.

148

515-520

393847

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Protochlorophyllide reductase: a flavoprotein?

1988

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FEBS Lett.

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393848

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Protochlorophyllide reductase. 1. Determination of the regiochemistry and the stereochemistry of the reduction of protochlorophyllide to chlorophyllide

1989

Begley, T.P.; Young, H.

J. Am. Chem. Soc.

111

3095-3096

393849

2502114

Light-independent NADPH-protochlorophyllide oxidoreductase activity in purified plasma membrane from the cyanobacterium Anacystis nidulans

1989

Peschek, G.A.; Hinterstoisser, B.; Pineau, B.; Missbichler, A.

Biochem. Biophys. Res. Commun.

162

71-78

393850

2501298

Chlorophyll precursors in the plasma membrane of a cyanobacterium, Anacystis nidulans. Characterization of protochlorophyllide and chlorophyllide by spectrophotometry, spectrofluorimetry, solvent partition, and high performance liquid chromatography

1989

Peschek, G.A.; Hinterstoisser, B.; Wastyn, M.; Kuntner, O.; Pineau, B.; Missbichler, A.; Lang, J.

J. Biol. Chem.

264

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393851

2671659

Nucleotide sequence of a cDNA coding for the NADPH-protochlorophyllide oxidoreductase (PCR) of barley (Hordeum vulgare L.) and its expression in Escherichia coli

1989

Schulz, R.; Steinmueller, K.; Klaas, M.; Forreiter, C.; Rasmussen, S.; Hiller, C.; Apel, K.

Mol. Gen. Genet.

217

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393852

1689568

Cloning and sequencing of protochlorophyllide reductase

1990

Darrah, P.M.; Kay, S.A.; Teakle, G.R.; Griffiths, W.T.

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393853

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Identification of NADPH:protochlorophyllide oxidoreductases A and B: a branched pathway for light-dependent chlorophyll biosynthesis in Arabidopsis thaliana

1995

Armstrong, G.A.; Runge, S.; Frick, G.; Sperling, U.; Apel, K.

Plant Physiol.

108

1505-1517

393854

7846042

A light-dependent complementation system for analysis of NADPH:protochlorophyllide oxidoreductase: identification and mutagenesis of two conserved residues that are essential for enzyme activity

1995

Wilks, H.M.; Timko, M.P.

Proc. Natl. Acad. Sci. USA

92

724-728

393855

-

Absolute configuration of protochlorophyllide a and substrate specificity of NADPH-protochlorophyllide oxidoreductase

1996

Helfrich, M.; Schoch, S.; Schaefer, W.; Ryberg, M.; Ruediger, W.

J. Am. Chem. Soc.

118

2606-2611

393856

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Purification and kinetic analysis of pea (Pisum sativum L.) NADPH:protochlorophyllide oxidoreductase expressed as a fusion with maltose-binding protein in Escherichia coli

1997

Martin, G.E.M.; Timko, M.P.; Wilks, H.M.

Biochem. J.

325

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393857

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Isolation and characterization of photoactive complexes of NADPH:protochlorophyllide oxidoreductase from wheat

1998

Chahdi, M.A.O.; Schoefs, B.; Franck, F.

Planta

206

673-680

393858

10080697

The role of protein surface charge in catalytic activity and chloroplast membrane association of the pea NADPH: protochlorophyllide oxidoreductase (POR) as revealed by alanine scanning mutagenesis

1999

Dahlin, C.; Aronsson, H.; Wilks, H.M.; Lebedev, N.; Sundqvist, C.; Timko, M.P.

Plant Mol. Biol.

39

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393859

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Pigment-free NADPH:protochlorophyllide oxidoreductase from Avena sativa L: purification and substrate specificity

1999

Klement, H.; Helfrich, M.; Oster, U.; Schoch, S.; Rudiger, W.

Eur. J. Biochem.

265

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393860

10449801

Protochlorophyllide oxidoreductase B-catalyzed protochlorophyllide photoreduction in vitro: insight into the mechanism of chlorophyll formation in light-adapted plants

1999

Lebedev, N.; Timko, M.P.

Proc. Natl. Acad. Sci. USA

96

9954-9959

393861

11115885

Regulation of etioplast pigment-protein complexes, inner membrane architecture, and protochlorophyllide a chemical heterogeneity by light-dependent NADPH:protochlorophyllide oxidoreductases A and B

2000

Franck, F.; Sperling, U.; Frick, G.; Pochert, B.; Van Cleve, B.; Apel, K.; Armstrong, G.A.

Plant Physiol.

124

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393862

10811655

Reconstitution of light-independent protochlorophyllide reductase from purified bchl and BchN-BchB subunits. In vitro confirmation of nitrogenase-like features of a bacteriochlorophyll biosynthesis enzyme

2000

Fujita, Y.; Bauer, C.E.

J. Biol. Chem.

275

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393863

11033354

NADPH:protochlorophyllide oxidoreductase from Synechocystis: overexpression, purification and preliminary characterization

2000

Heyes, D.J.; Martin, G.E.M.; Reid, R.J.; Hunter, C.N.; Wilks, H.M.

FEBS Lett.

483

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393864

11601980

Tyr275 and Lys279 Stabilize NADPH within the Catalytic Site of NADPH:Protochlorophyllide Oxidoreductase and Are Involved in the Formation of the Enzyme Photoactive State

2001

Lebedev, N.; Karginova, O.; McIvor, W.; Timko, M.P.

Biochemistry

40

12562-12574

393865

11785941

POR C of Arabidopsis thaliana: a third light- and NADPH-dependent protochlorophyllide oxidoreductase that is differentially regulated by light

2001

Su, Q.; Frick, G.; Armstrong, G.; Apel, K.

Plant Mol. Biol.

47

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393866

11985616

The effects of low pH on the properties of protochlorophyllide oxidoreductase and the organization of prolamellar bodies of maize (Zea mays)

2002

Selstam, E.; Schelin, J.; Brain, T.; Williams, W.P.

Eur. J. Biochem.

269

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485107

-

Biosynthesis and inhibition of (-)-S-adenosyl-L-methionine:magnesium protoporphyrin methyltransferase of wheat

1976

Ellsworth, R.K.; St.Pierre, M.E.

Photosynthetica

10

291-301

654419

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Catalytic function of a novel protein protochlorophyllide oxidoreductase C of Arabidopsis thaliana

2002

Pattanayak, G.K.; Tripathy, B.C.

Biochem. Biophys. Res. Commun.

291

921-924

654705

12525180

Protochlorophyllide oxidoreductase: "dark" reactions of a light-driven enzyme

2003

Heyes, D.J.; Ruban, A.V.; Hunter, C.N.

Biochemistry

42

523-528

654842

12907304

Chlorophylls of the c family: absolute configuration and inhibition of NADPH:protochlorophyllide oxidoreductase

2003

Helfrich, M.; Bommer, B.; Oster, U.; Klement, H.; Mayer, K.; Larkum, A.W.; Rudiger, W.

Biochim. Biophys. Acta

1605

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656854

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Ultrafast enzymatic reaction dynamics in protochlorophyllide oxidoreductase

2003

Heyes, D.J.; Hunter, C.N.; van Stokkum, I.H.; van Grondelle, R.; Groot, M.L.

Nat. Struct. Biol.

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656904

16228553

POR structural domains important for the enzyme activity in R. capsulatus complementation system

2002

Lebedev, N.; Timko, M.P.

Photosynth. Res.

74

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656905

16228554

Identification of two differentially regulated isoforms of protochlorophyllide oxidoreductase (POR) from tobacco revealed a wide variety of light- and development-dependent regulations of POR gene expression among angiosperms

2002

Masuda, T.; Fusada, N.; Shiraishi, T.; Kuroda, H.; Awai, K.; Shimada, H.; Ohta, H.; Takamiya, K.i.

Photosynth. Res.

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656908

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Novel insights into the enzymology, regulation and physiological functions of light-dependent protochlorophyllide oxidoreductase in angiosperms

2004

Masuda, T.; Takamiya, K.i.

Photosynth. Res.

81

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656911

-

Mercury inhibits the activity of the NADPH:protochlorophyllide oxidoreductase (POR)

2002

Lenti, K.; Fodor, F.; Boddi, B.

Photosynthetica

40

145-151

656982

14581621

Functional analysis of isoforms of NADPH: protochlorophyllide oxidoreductase (POR), PORB and PORC, in Arabidopsis thaliana

2003

Masuda, T.; Fusada, N.; Oosawa, N.; Takamatsu, K.; Yamamoto, Y.Y.; Ohto, M.; Nakamura, K.; Goto, K.; Shibata, D.; Shirano, Y.; Hayashi, H.; Kato, T.; Tabata, S.; Shimada, H.; Ohta, H.; Takamiya, K.

Plant Cell Physiol.

44

963-974

657001

12848821

An Arabidopsis porB porC double mutant lacking light-dependent NADPH:protochlorophyllide oxidoreductases B and C is highly chlorophyll-deficient and developmentally arrested

2003

Frick, G.; Su, Q.; Apel, K.; Armstrong, G.A.

Plant J.

35

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657010

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A role of Toc33 in the protochlorophyllide-dependent plastid import pathway of NADPH:protochlorophyllide oxidoreductase (POR) A

2005

Reinbothe, S.; Pollmann, S.; Springer, A.; James, R.J.; Tichtinsky, G.; Reinbothe, C.

Plant J.

42

1-12

657112

100130130

LHPP, the light-harvesting NADPH:protochlorophyllide (Pchlide) oxidoreductase:Pchlide complex of etiolated plants, is developmentally expressed across the barley leaf gradient

2004

Reinbothe, C.; Pollmann, S.; Desvignes, C.; Weigele, M.; Beck, E.; Reinbothe, S.

Plant Sci.

167

1027-1041

663257

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A role for chlorophyllide a oxygenase in the regulated import and stabilization of light-harvesting chlorophyll a/b proteins

2006

Reinbothe, C.; Bartsch, S.; Eggink, L.L.; Hoober, J.K.; Brusslan, J.; Andrade-Paz, R.; Monnet, J.; Reinbothe, S.

Proc. Natl. Acad. Sci. USA

103

4777-4782

671845

16274361

Spectroscopic and kinetic characterization of the light-dependent enzyme protochlorophyllide oxidoreductase (POR) using monovinyl and divinyl substrates

2006

Heyes, D.J.; Kruk, J.; Hunter, C.N.

Biochem. J.

394

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672324

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Overexpression and characterization of dark-operative protochlorophyllide reductase from Rhodobacter capsulatus

2005

Nomata, J.; Swem, L.R.; Bauer, C.E.; Fujita, Y.

Biochim. Biophys. Acta

1708

229-237

676324

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Kinetic characterisation of the light-driven protochlorophyllide oxidoreductase (POR) from Thermosynechococcus elongatus

2005

McFarlane, M.J.; Hunter, C.N.; Heyes, D.J.

Photochem. Photobiol. Sci.

4

1055-1059

686758

18358835

NB-protein (BchN-BchB) of dark-operative protochlorophyllide reductase is the catalytic component containing oxygen-tolerant Fe-S clusters

2008

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582

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687626

17848549

Laser excitation studies of the product release steps in the catalytic cycle of the light-driven enzyme, protochlorophyllide oxidoreductase

2007

Heyes, D.J.; Sakuma, M.; Scrutton, N.S.

J. Biol. Chem.

282

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ATP-driven reduction by dark-operative protochlorophyllide oxidoreductase from Chlorobium tepidum mechanistically resembles nitrogenase catalysis

2008

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687767

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Substrate recognition of nitrogenase-like dark operative protochlorophyllide oxidoreductase from Prochlorococcus marinus

2008

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J. Biol. Chem.

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2007

Kovacevic, D.; Dewez, D.; Popovic, R.

Photosynthetica

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105-109

689772

17261815

A plant porphyria related to defects in plastid import of protochlorophyllide oxidoreductase A

2007

Pollmann, S.; Springer, A.; Buhr, F.; Lahroussi, A.; Samol, I.; Bonneville, J.M.; Tichtinsky, G.; von Wettstein, D.; Reinbothe, C.; Reinbothe, S.

Proc. Natl. Acad. Sci. USA

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689784

17483469

A substrate-independent, 14:3:3 protein-mediated plastid import pathway of NADPH:protochlorophyllide oxidoreductase A

2007

Schemenewitz, A.; Pollmann, S.; Reinbothe, C.; Reinbothe, S.

Proc. Natl. Acad. Sci. USA

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8538-8543

695583

19373814

Solvent-slaved protein motions accompany proton but not hydride tunneling in light-activated protochlorophyllide oxidoreductase

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696150

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Fong, A.; Archibald, J.M.

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Stoichiometry of ATP hydrolysis and chlorophyllide formation of dark-operative protochlorophyllide oxidoreductase from Rhodobacter capsulatus

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Nomata, J.; Terauchi, K.; Fujita, Y.

Biochem. Biophys. Res. Commun.

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704-709

737646

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Elucidation of the preferred routes of C8-vinyl reduction in chlorophyll and bacteriochlorophyll biosynthesis

2014

Canniffe, D.P.; Chidgey, J.W.; Hunter, C.N.

Biochem. J.

462

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738520

21764919

Multiple types of 8-vinyl reductases for (bacterio)chlorophyll biosynthesis occur in many green sulfur bacteria

2011

Liu, Z.; Bryant, D.A.

J. Bacteriol.

193

4996-4998

738542

26903415

Two unrelated 8-vinyl reductases ensure production of mature chlorophylls in Acaryochloris marina

2016

Chen, G.E.; Hitchcock, A.; Jackson, P.J.; Chaudhuri, R.R.; Dickman, M.J.; Hunter, C.N.; Canniffe, D.P.

J. Bacteriol.

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740022

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MGDG, PG and SQDG regulate the activity of light-dependent protochlorophyllide oxidoreductase

2017

Gabruk, M.; Mysliwa-Kurdziel, B.; Kruk, J.

Biochem. J.

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740071

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Light-dependent protochlorophyllide oxidoreductase: phylogeny, regulation, and catalytic properties

2015

Gabruk, M.; Mysliwa-Kurdziel, B.

Biochemistry

54

5255-5262

740086

26807652

Cross-species analysis of protein dynamics associated with hydride and proton transfer in the catalytic cycle of the light-driven enzyme protochlorophyllide oxidoreductase

2016

Hoeven, R.; Hardman, S.J.; Heyes, D.J.; Scrutton, N.S.

Biochemistry

55

903-913

740446

23954297

Nicotinamide is a specific inhibitor of dark-operative protochlorophyllide oxidoreductase, a nitrogenase-like enzyme, from Rhodobacter capsulatus

2013

Nomata, J.; Kondo, T.; Itoh, S.; Fujita, Y.

FEBS Lett.

587

3142-3147

740894

27285815

Multiple active site residues are important for photochemical efficiency in the light-activated enzyme protochlorophyllide oxidoreductase (POR)

2016

Menon, B.R.; Hardman, S.J.; Scrutton, N.S.; Heyes, D.J.

J. Photochem. Photobiol. B

161

236-243

741021

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Discovery of the first light-dependent protochlorophyllide oxidoreductase in anoxygenic phototrophic bacteria

2014

Kaschner, M.; Loeschcke, A.; Krause, J.; Minh, B.Q.; Heck, A.; Endres, S.; Svensson, V.; Wirtz, A.; von Haeseler, A.; Jaeger, K.E.; Drepper, T.; Krauss, U.

Mol. Microbiol.

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741099

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With or without light: comparing the reaction mechanism of dark-operative protochlorophyllide oxidoreductase with the energetic requirements of the light-dependent protochlorophyllide oxidoreductase

2014

Silva, P.J.

PeerJ.

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Transcriptional and post-translational control of chlorophyll biosynthesis by dark-operative protochlorophyllide oxidoreductase in Norway spruce

2017

Stolarik, T.; Hedtke, B.; Santrucek, J.; Ilik, P.; Grimm, B.; Pavlovic, A.

Photosynth. Res.

132

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741157

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Cell growth defect factor1/chaperone-like protein of POR1 plays a role in stabilization of light-dependent protochlorophyllide oxidoreductase in Nicotiana benthamiana and Arabidopsis

2013

Lee, J.Y.; Lee, H.S.; Song, J.Y.; Jung, Y.J.; Reinbothe, S.; Park, Y.I.; Lee, S.Y.; Pai, H.S.

Plant Cell

25

3944-3960

741184

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NADPH:protochlorophyllide oxidoreductase B (PORB) action in Arabidopsis thaliana revisited through transgenic expression of engineered barley PORB mutant proteins

2017

Buhr, F.; Lahroussi, A.; Springer, A.; Rustgi, S.; von Wettstein, D.; Reinbothe, C.; Reinbothe, S.

Plant Mol. Biol.

94

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741187

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RNAi based simultaneous silencing of all forms of light-dependent NADPH:protochlorophyllide oxidoreductase genes result in the accumulation of protochlorophyllide in tobacco (Nicotiana tabacum)

2013

Talaat, N.B.

Plant Physiol. Biochem.

71

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741255

27367227

Differential regulation of duplicate light-dependent protochlorophyllide oxidoreductases in the diatom Phaeodactylum tricornutum

2016

Hunsperger, H.; Ford, C.; Miller, J.; Cattolico, R.

PLoS ONE

11

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741337

25901327

Cell growth defect factor 1 is crucial for the plastid import of NADPH:protochlorophyllide oxidoreductase A in Arabidopsis thaliana

2015

Reinbothe, S.; Gray, J.; Rustgi, S.; von Wettstein, D.; Reinbothe, C.

Proc. Natl. Acad. Sci. USA

112

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741396

28078486

Two NADPH: protochlorophyllide oxidoreductase (POR) isoforms play distinct roles in environmental adaptation in rice

2017

Kwon, C.T.; Kim, S.H.; Song, G.; Kim, D.; Paek, N.C.

Rice (N.Y.)

10

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741827

26774340

Stoichiometry of ATP hydrolysis and chlorophyllide formation of dark-operative protochlorophyllide oxidoreductase from Rhodobacter capsulatus

2016

Nomata, J.; Terauchi, K.; Fujita, Y.

Biochem. Biophys. Res. Commun.

470

704-709

762601

29363234

Stepwise hydridet transfer in a biological system insights into the reaction mechanism of the light-dependent protochlorophyllide oxidoreductase

2018

Archipowa, N.; Kutta, R.J.; Heyes, D.J.; Scrutton, N.S.

Angew. Chem. Int. Ed. Engl.

57

2682-2686

762912

32180325

Chlorophyllide a oxidoreductase preferentially catalyzes 8-vinyl reduction over B-ring reduction of 8-vinyl chlorophyllide a in the late steps of bacteriochlorophyll biosynthesis

2020

Yamamoto, H.; Mizoguchi, T.; Tsukatani, Y.; Tamiaki, H.; Kurisu, G.; Fujita, Y.

ChemBioChem

21

1760-1766

763023

32866986

Dual role of the active site lid regions of protochlorophyllide oxidoreductase in photocatalysis and plant development

2021

Zhang, S.; Godwin, A.R.F.; Taylor, A.; Hardman, S.J.O.; Jowitt, T.A.; Johannissen, L.O.; Hay, S.; Baldock, C.; Heyes, D.J.; Scrutton, N.S.

FEBS J.

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763100

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The role of membranes and lipid-protein interactions in the Mg-branch of tetrapyrrole biosynthesis

2021

Solymosi, K.; Mysliwa-Kurdziel, B.

Front. Plant Sci.

12

663309

763334

32238622

Formation of prolamellar-body-like ultrastructures in etiolated cyanobacterial cells overexpressing light-dependent protochlorophyllide oxidoreductase in Leptolyngbya boryana

2020

Yamamoto, H.; Kojima-Ando, H.; Ohki, K.; Fujita, Y.

J. Gen. Appl. Microbiol.

66

129-139

763678

30291443

Evolution of light-independent protochlorophyllide oxidoreductase

2019

Vedalankar, P.; Tripathy, B.

Protoplasma

256

293-312

765263

29051378

Light-dependent accumulation of new bacteriochlorophyll-e bearing a vinyl group at the 8-position in the green sulfur bacterium Chlorobaculum limnaeum

2018

Mizoguchi, T.; Kinoshita, Y.; Harada, J.; Ogasawara, S.; Tamiaki, H.

J. Photochem. Photobiol. A

358

356-361

Links to other databases for protochlorophyllide

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