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Literature summary for 1.3.7.6 extracted from

  • Busch, A.W.; Reijerse, E.J.; Lubitz, W.; Hofmann, E.; Frankenberg-Dinkel, N.
    Radical mechanism of cyanophage phycoerythrobilin synthase (PebS) (2011), Biochem. J., 433, 469-476.
    View publication on PubMed
Search for more literature for 1.3.7.6

Protein Variants

Protein Variants Comment Organism
D105E site-directed mutagenesis, the mutant fully retains the ability to catalyse the first reduction at the 15,16-methine bridge, but cannot catalyse the second reduction at the A-ring 2,3,31,32-diene system, thereby yielding 15,16-DHBV as the final product Prochlorococcus phage P-SSM2
D206E site-directed mutagenesis, the mutant fully retains the ability to catalyse the first reduction at the 15,16-methine bridge, but cannot catalyse the second reduction at the A-ring 2,3,31,32-diene system, however, in this mutant the reaction can be pushed further to produce (3Z)-phycoerythrobilin by a 10fold increase in ferredoxin concentration Prochlorococcus phage P-SSM2
D206N site-directed mutagenesis, the mutant fully retains the ability to catalyse the first reduction at the 15,16-methine bridge, but cannot catalyse the second reduction at the A-ring 2,3,31,32-diene system, thereby yielding 15,16-DHBV as the final product Prochlorococcus phage P-SSM2

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
biliverdin IXalpha + 2 reduced ferredoxin Prochlorococcus phage P-SSM2 a two-step reaction via intermediate 15,16-dihydrobiliverdin, the single steps form the reactions of EC 1.3.7.2 and 1.3.7.3, overview (3Z)-phycoerythrobilin + 2 oxidized ferredoxin
-
 ?

Organism

Organism UniProt Comment Textmining
Prochlorococcus phage P-SSM2
-
 Prochlorococcus-infecting
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
biliverdin IXalpha + 2 reduced ferredoxin a two-step reaction via intermediate 15,16-dihydrobiliverdin, the single steps form the reactions of EC 1.3.7.2 and 1.3.7.3, overview Prochlorococcus phage P-SSM2 (3Z)-phycoerythrobilin + 2 oxidized ferredoxin
-
 ?
biliverdin IXalpha + 2 reduced ferredoxin ferredoxin from Synechococcus sp. PCC 7002 or from cyanophage P-SSM2 Prochlorococcus phage P-SSM2 (3Z)-phycoerythrobilin + 2 oxidized ferredoxin
-
 ?

Synonyms

Synonyms Comment Organism
PEB synthase
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 Prochlorococcus phage P-SSM2
PebS
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 Prochlorococcus phage P-SSM2
phycoerythrobilin synthase
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 Prochlorococcus phage P-SSM2

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
17
-
 assay at Prochlorococcus phage P-SSM2

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Prochlorococcus phage P-SSM2

Cofactor

Cofactor Comment Organism Structure
Ferredoxin
-
 Prochlorococcus phage P-SSM2

General Information

General Information Comment Organism
evolution the enzyme belongs to the ferredoxin-dependent bilin reductase family Prochlorococcus phage P-SSM2
additional information PebS-catalysed PEB synthesis proceeds via a radical mechanism and both aspartate residues involved, Asp105 and Asp206, are important for stereospecific substrate protonation and conversion. Both Asp residues are highly conserved throughout the family of ferredoxin-dependent bilin reductases, bilin radical intermediates during PebS reaction, and superposition of the active site of the wild-type enzyme, the D105N and D206N mutant with bound substrate biliverdin Prochlorococcus phage P-SSM2