Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Qin, X.; Sun, L.; Wen, X.; Yang, X.; Tan, Y.; Jin, H.; Cao, Q.; Zhou, W.; Xi, Z.; Shen, Y.
    Structural insight into unique properties of protoporphyrinogen oxidase from Bacillus subtilis (2010), J. Struct. Biol., 170, 76-82.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.3.15 expressed in Escherichia coli BL21(DE3) cells Bacillus subtilis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.3.3.4 purified native and SeMet-labeled enzyme in complex with inhibitor acifluorfen, sitting-drop, vapor-diffusion method, 10 mg/ml wild-type bsPPO protein in 50 mM TrisHCl, pH 7.5, 200 mM sodium chloride, 5 mM DTT, 1 mM EDTA, and acifluorfen in a 1:5 ratio, equilibrating against a reservoir solution of 2.4 M ammonium phosphate dibasic, 0.1 M Tris-HCl, pH 7.5, 1 week, 20°C, X-ray diffraction structure determination and analysis at 2.8-3.5 A resolution Bacillus subtilis
1.3.3.15 in complex with acifluorfen, sitting drop vapor diffusion method, using 2.4 M ammonium phosphate dibasic, 0.1 M Tris-HCl pH 7.5 Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
1.3.3.4 F227R the mutant shows reduced activity compared to the wild-type enzyme Bacillus subtilis
1.3.3.4 I176A the mutant shows reduced activity compared to the wild-type enzyme Bacillus subtilis
1.3.3.4 K71A the mutant shows reduced activity compared to the wild-type enzyme Bacillus subtilis
1.3.3.4 P64A the mutant shows reduced activity compared to the wild-type enzyme Bacillus subtilis
1.3.3.15 F227R the mutant exhibits slight decrease in catalysis compared to the wild type enzyme Bacillus subtilis
1.3.3.15 I176A the mutation leads to about 30fold decrease in catalytic efficiency compared to the wild type enzyme Bacillus subtilis
1.3.3.15 K71A the mutation leads to about 50fold decrease in catalytic efficiency compared to the wild type enzyme Bacillus subtilis
1.3.3.15 P64A the mutant exhibits a 14fold decrease in catalysis compared to the wild type enzyme Bacillus subtilis
1.3.3.15 Y366N the mutation leads to about 100fold decrease in catalytic efficiency compared to the wild type enzyme Bacillus subtilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.3.4 acifluorfen a herbicide, binding structure, overview Bacillus subtilis
1.3.3.15 acifluorfen
-
 Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.3.4 0.001
-
 protoporphyrinogen IX mutant F227R, pH 7.5, temperature not specified in the publication Bacillus subtilis
1.3.3.4 0.001
-
 protoporphyrinogen IX mutant I176A, pH 7.5, temperature not specified in the publication Bacillus subtilis
1.3.3.4 0.001
-
 protoporphyrinogen IX mutant K71A, pH 7.5, temperature not specified in the publication Bacillus subtilis
1.3.3.4 0.001
-
 protoporphyrinogen IX mutant P64A, pH 7.5, temperature not specified in the publication Bacillus subtilis
1.3.3.4 0.001
-
 protoporphyrinogen IX wild-type enzyme, pH 7.5, temperature not specified in the publication Bacillus subtilis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.3.4 soluble Bacillus subtilis PPO is unique among PPO family members in that it is a soluble monomer Bacillus subtilis
-
-
1.3.3.15 soluble
-
 Bacillus subtilis
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.3.4 protoporphyrinogen IX + 3 O2 Bacillus subtilis
-
 protoporphyrin IX + 3 H2O2
-
 ?
1.3.3.4 protoporphyrinogen IX + 3 O2 Bacillus subtilis 168
-
 protoporphyrin IX + 3 H2O2
-
 ?
1.3.3.15 coproporphyrinogen III + O2 Bacillus subtilis
-
 coproporphyrin III + H2O
-
 ?
1.3.3.15 coproporphyrinogen III + O2 Bacillus subtilis 168
-
 coproporphyrin III + H2O
-
 ?
1.3.3.15 protoporphyrinogen IX + O2 Bacillus subtilis
-
 protoporphyrin IX + H2O
-
 ?
1.3.3.15 protoporphyrinogen IX + O2 Bacillus subtilis 168
-
 protoporphyrin IX + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.3.4 Bacillus subtilis P32397
-
-
1.3.3.15 Bacillus subtilis P32397
-
-
1.3.3.15 Bacillus subtilis 168 P32397
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.3.15 Ni-NTA column chromatography and S200 gel filtration Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.3.4 additional information bsPPO has a broader substrate specificity compared to other PPOs, substrate binding structure comparison of wild-type and mutant enzymes, overview Bacillus subtilis ?
-
 ?
1.3.3.4 additional information bsPPO has a broader substrate specificity compared to other PPOs, substrate binding structure comparison of wild-type and mutant enzymes, overview Bacillus subtilis 168 ?
-
 ?
1.3.3.4 protoporphyrinogen IX + 3 O2
-
 Bacillus subtilis protoporphyrin IX + 3 H2O2
-
 ?
1.3.3.4 protoporphyrinogen IX + 3 O2
-
 Bacillus subtilis 168 protoporphyrin IX + 3 H2O2
-
 ?
1.3.3.15 coproporphyrinogen III + O2
-
 Bacillus subtilis coproporphyrin III + H2O
-
 ?
1.3.3.15 coproporphyrinogen III + O2
-
 Bacillus subtilis 168 coproporphyrin III + H2O
-
 ?
1.3.3.15 protoporphyrinogen IX + O2
-
 Bacillus subtilis protoporphyrin IX + H2O
-
 ?
1.3.3.15 protoporphyrinogen IX + O2
-
 Bacillus subtilis 168 protoporphyrin IX + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.3.4 monomer Bacillus subtilis PPO is unique among PPO family members in that it is a soluble monomer Bacillus subtilis
1.3.3.4 More prototypical PPO enzyme structure consists of three domains: a FAD-binding domain, a substrate binding domain and a membrane-binding domain, structure analysis and comparison, overview Bacillus subtilis
1.3.3.15 monomer
-
 Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
1.3.3.4 PPO
-
 Bacillus subtilis
1.3.3.4 protoporphyrinogen IX oxidase
-
 Bacillus subtilis
1.3.3.15 PPO
-
 Bacillus subtilis
1.3.3.15 protoporphyrinogen IX oxidase
-
 Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3.3.4 0.0004
-
 protoporphyrinogen IX mutant K71A, pH 7.5, temperature not specified in the publication Bacillus subtilis
1.3.3.4 0.001
-
 protoporphyrinogen IX mutant I176A, pH 7.5, temperature not specified in the publication Bacillus subtilis
1.3.3.4 0.0027
-
 protoporphyrinogen IX mutant P64A, pH 7.5, temperature not specified in the publication Bacillus subtilis
1.3.3.4 0.0131
-
 protoporphyrinogen IX wild-type enzyme, pH 7.5, temperature not specified in the publication Bacillus subtilis
1.3.3.4 0.0181
-
 protoporphyrinogen IX mutant F227R, pH 7.5, temperature not specified in the publication Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.3.4 7.5
-
 assay at Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.3.4 FAD a FAD molecule is non-covalently bound to domain I, binding structure, overview Bacillus subtilis
1.3.3.15 FAD
-
 Bacillus subtilis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.3.3.15 0.03774
-
 acifluorfen wild type enzyme at pH 7.5, temperature not specified in the publication Bacillus subtilis

General Information

EC Number General Information Comment Organism
1.3.3.4 metabolism PPO plays an important part in the heme/chlorophyll biosynthetic pathway Bacillus subtilis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.3.3.4 0.016
-
 protoporphyrinogen IX mutant K71A, pH 7.5, temperature not specified in the publication Bacillus subtilis
1.3.3.4 0.027
-
 protoporphyrinogen IX mutant I176A, pH 7.5, temperature not specified in the publication Bacillus subtilis
1.3.3.4 0.057
-
 protoporphyrinogen IX mutant P64A, pH 7.5, temperature not specified in the publication Bacillus subtilis
1.3.3.4 0.464
-
 protoporphyrinogen IX mutant F227R, pH 7.5, temperature not specified in the publication Bacillus subtilis
1.3.3.4 0.784
-
 protoporphyrinogen IX wild-type enzyme, pH 7.5, temperature not specified in the publication Bacillus subtilis