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Literature summary for 1.3.7.5 extracted from

  • Miyake, K.; Fushimi, K.; Kashimoto, T.; Maeda, K.; Ni-Ni-Win, K.; Kimura, H.; Sugishima, M.; Ikeuchi, M.; Narikawa, R.
    Functional diversification of two bilin reductases for light perception and harvesting in unique cyanobacterium Acaryochloris marina MBIC 11017 (2020), FEBS J., 287, 4016-4031 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
Acaryochloris marina strain 11017 encodes two PcyA homologues, AmPcyAc and AmPcyAp. AmPcyAc is encoded on the main chromosome with most photoreceptor genes, whereas AmPcyAp is encoded on a plasmid with PBS-related genes, these PcyA homologues share 56% sequence identity. Cloning of gene pcyA or AM1_5311 and recombinant expression of the His-tagged enzyme in Escherichia coli strain C41, phylogenetic analysis and tree, quantitative real-time PCR enzyme expression analysis Acaryochloris marina
Acaryochloris marina strain 11017 encodes two PcyA homologues, AmPcyAc and AmPcyAp. AmPcyAc is encoded on the main chromosome with most photoreceptor genes, whereas AmPcyAp is encoded on a plasmid with PBS-related genes, these PcyA homologues share 56% sequence identity. Cloning of gene pcyA or AM1_C0185 and recombinant expression of the His-tagged enzyme in Escherichia coli strain C41, phylogenetic analysis and tree, quantitative real-time PCR enzyme expression analysis Acaryochloris marina
gene pcyA, phylogenetic analysis and tree, recombinant expression of His-tagged enzyme in Escherichia coli strain C41, coexpression with heme oxygenase 1 (HO1) Synechocystis sp. PCC 6803

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ in cofactor ferredoxin Synechocystis sp. PCC 6803
Fe2+ in cofactor ferredoxin Acaryochloris marina

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
biliverdin IXalpha + 4 reduced ferredoxin Synechocystis sp. PCC 6803
-
(3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
?
biliverdin IXalpha + 4 reduced ferredoxin Acaryochloris marina
-
(3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
?
biliverdin IXalpha + 4 reduced ferredoxin Acaryochloris marina MBIC 11017
-
(3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
?

Organism

Organism UniProt Comment Textmining
Acaryochloris marina A8ZMS5 gene pcyA or AM1_C0185 encoding enzyme AmPcyAp
-
Acaryochloris marina B0CAR8 gene pcyA or AM1_5311 encoding enzyme AmPcyAc
-
Acaryochloris marina MBIC 11017 A8ZMS5 gene pcyA or AM1_C0185 encoding enzyme AmPcyAp
-
Acaryochloris marina MBIC 11017 B0CAR8 gene pcyA or AM1_5311 encoding enzyme AmPcyAc
-
Synechocystis sp. PCC 6803 Q55891
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain C41 by nickel affinity chromatography and dialysis Synechocystis sp. PCC 6803
recombinant His-tagged enzyme from Escherichia coli strain C41 by nickel affinity chromatography and dialysis Acaryochloris marina

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
biliverdin IXalpha + 4 reduced ferredoxin
-
Synechocystis sp. PCC 6803 (3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
?
biliverdin IXalpha + 4 reduced ferredoxin
-
Acaryochloris marina (3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
?
biliverdin IXalpha + 4 reduced ferredoxin via the intermediate 181,182-dihydrobiliverdin (181/182-DHBV) Acaryochloris marina (3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
?
biliverdin IXalpha + 4 reduced ferredoxin via the intermediate 181/182-dihydrobiliverdin (181/182-DHBV) Acaryochloris marina (3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
?
biliverdin IXalpha + 4 reduced ferredoxin
-
Acaryochloris marina MBIC 11017 (3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
?
biliverdin IXalpha + 4 reduced ferredoxin via the intermediate 181,182-dihydrobiliverdin (181/182-DHBV) Acaryochloris marina MBIC 11017 (3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
?
biliverdin IXalpha + 4 reduced ferredoxin via the intermediate 181/182-dihydrobiliverdin (181/182-DHBV) Acaryochloris marina MBIC 11017 (3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
?

Subunits

Subunits Comment Organism
? x * 30100, recombinant enzyme AmPcyAp, SDS-PAGE Acaryochloris marina
? x * 30200, recombinant enzyme AmPcyAc, SDS-PAGE Acaryochloris marina
? x * 30400, recombinant enzyme AmPcyAp, SDS-PAGE Synechocystis sp. PCC 6803

Synonyms

Synonyms Comment Organism
AmPcyAc
-
Acaryochloris marina
AmPcyAp
-
Acaryochloris marina
HY2 protein
-
Synechocystis sp. PCC 6803
HY2 protein
-
Acaryochloris marina
PcyA
-
Synechocystis sp. PCC 6803
PcyA
-
Acaryochloris marina
phycocyanobilin:ferredoxin oxidoreductase
-
Synechocystis sp. PCC 6803
phycocyanobilin:ferredoxin oxidoreductase
-
Acaryochloris marina
SyPcyA
-
Synechocystis sp. PCC 6803

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
28
-
assay at Synechocystis sp. PCC 6803

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
assay at Synechocystis sp. PCC 6803

Cofactor

Cofactor Comment Organism Structure
Ferredoxin
-
Synechocystis sp. PCC 6803
Ferredoxin
-
Acaryochloris marina

General Information

General Information Comment Organism
evolution Acaryochloris marina strain 11017 evolved to utilize specific PcyA enzymes for sensing wide range of spectrum upon both PCB and 181/182-DHBV binding and harvesting short-wavelength orange light upon only PCB binding. Phycocyanin a from Acaryochloris marina strain 11017 binds only phycocyanobilin (PCB) but not 181/182-DHBV Acaryochloris marina
evolution Acaryochloris marina strain 11017 evolved to utilize specific PcyA enzymes for sensing wide range of spectrum upon both PCB and 181/182-DHBV binding and harvesting shortwavelength orange light upon only PCB binding. Phycocyanin a from Acaryochloris marina strain 11017 binds only phycocyanobilin (PCB) but not 181/182-DHBV Acaryochloris marina
metabolism Acaryochloris marina strain 11017 exceptionally encodes two PcyA homologues, AmPcyAc and AmPcyAp. The enzymes AmPcyAc and AmPcyAp show completely different kinetics especially for 181/182-DHBV accumulation. High accumulation of 181/182-DHBV for extended periods is observed during the reaction catalyzed by AmPcyAc, whereas 181/182-DHBV is transiently accumulated for a short period during the reaction catalyzed by AmPcyAp. Phycocyanin a from Acaryochloris marina strain 11017 binds only phycocyanobilin (PCB) but not 181/182-DHBV Acaryochloris marina
physiological function phycocyanobilin:ferredoxin oxidoreductase (PcyA) catalyzes PCB synthesis from biliverdin via the intermediate 181/182-dihydrobiliverdin (181/182-DHBV), resulting in the stepwise shortening of the absorbing wavelengths. Cyanobacteriochromes (CBCRs) sense longer wavelength far-red light through 181/182-DHBV incorporation, whereas phycocyanobilin (PCB) only harvests orange light through PCB incorporation, suggesting functional diversification of PcyA as AmPcyAc and AmPcyAp to provide 181/182-DHBV and PCB to the light perception and harvesting systems, respectively. While most cyanobacteria utilize chlorophyll a as the photosynthetic reaction center pigment, Acaryochloris marina 11017 exceptionally utilizes chlorophyll d that absorbs longer wavelength far-red light than chlorophyll a Acaryochloris marina
physiological function phycocyanobilin:ferredoxin oxidoreductase (PcyA) catalyzes PCB synthesis from biliverdin via the intermediate 181/182-dihydrobiliverdin (181/182-DHBV), resulting in the stepwise shortening of the absorbing wavelengths. Cyanobacteriochromes (CBCRs) sense longer wavelength far-red light through 181/182-DHBV incorporation, whereas phycocyanobilin (PCB) only harvests orange light through PCB incorporation, suggesting functional diversification of PcyA as AmPcyAc and AmPcyAp to provide 181/182-DHBV and PCB to the light perception and harvesting systems, respectively. While most cyanobacteria utilize chlorophyll a as the photosynthetic reaction center pigment, Acaryochloris marina strain 11017 exceptionally utilizes chlorophyll d that absorbs longer wavelength far-red light than chlorophyll a Acaryochloris marina