1.3.7.5: phycocyanobilin:ferredoxin oxidoreductase
This is an abbreviated version!
For detailed information about phycocyanobilin:ferredoxin oxidoreductase, go to the full flat file.
Word Map on EC 1.3.7.5
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1.3.7.5
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bilins
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cyanobacteria
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ixalpha
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tetrapyrrole
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chromophore
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phytochrome
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light-harvesting
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synechocystis
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phycobiliproteins
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ferredoxins
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vinyl
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four-electron
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d-ring
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phycobilisomes
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phytochromobilin
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substrate-free
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phycoerythrobilin
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light-sensing
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biliproteins
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antenna
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holophytochrome
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two-electron
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nostoc
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apophytochrome
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cyanobacteriochromes
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photoreversible
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phycobilin
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cyanophage
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fdbrs
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reddish
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photoactive
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phycocyanin
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prochlorococcus
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proton-donating
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myovirus
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protein-substrate
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hydronium
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analysis
- 1.3.7.5
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bilins
- cyanobacteria
- ixalpha
- tetrapyrrole
- chromophore
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phytochrome
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light-harvesting
- synechocystis
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phycobiliproteins
- ferredoxins
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vinyl
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four-electron
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d-ring
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phycobilisomes
- phytochromobilin
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substrate-free
- phycoerythrobilin
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light-sensing
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biliproteins
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antenna
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holophytochrome
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two-electron
- nostoc
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apophytochrome
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cyanobacteriochromes
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photoreversible
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phycobilin
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cyanophage
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fdbrs
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reddish
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photoactive
- phycocyanin
- prochlorococcus
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proton-donating
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myovirus
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protein-substrate
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hydronium
- analysis
Reaction
+ 4 oxidized ferredoxin = + 4 reduced ferredoxin
Synonyms
3Z-phycocyanobilin:ferredoxin oxidoreductase, AmPcyAc, AmPcyAp, bilin reductase, FDBR, ferredoxin-dependent biliverdin reductase, ferredoxin:3Z-phycocyanobilin oxidoreductase, HY2 protein, oxidoreductase, ferredoxin:3Z-phycocyanobilin, Pcb:Fd oxidoreductase, PCB:ferredoxin oxidoreductase, PcyA, PCYA1, phycocyanobilin synthase, phycocyanobilin-ferredoxin oxidoreductase, phycocyanobilin:ferredoxin oxidoreductase, SyPcyA
ECTree
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General Information
General Information on EC 1.3.7.5 - phycocyanobilin:ferredoxin oxidoreductase
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evolution
malfunction
metabolism
physiological function
additional information
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comparison and discrimination of two bilin reductase families in bilin amide usage for photoconversions of BV-type and phytobilin-type phytochromes, mechanistic differences, overview
evolution
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synthesis of linear tetrapyrrole chromophores in cyanobacteria, algae, and plants, ooverview
evolution
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the enzyme is a member of the ferredoxin-dependent biliverdin reductase (FDBR) family
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
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
evolution
phycocyanobilin:ferredoxin oxidoreductase (PcyA) is a member of the ferredoxin-dependent bilin reductase (FDBR) family
evolution
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comparison and discrimination of two bilin reductase families in bilin amide usage for photoconversions of BV-type and phytobilin-type phytochromes, mechanistic differences, overview
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evolution
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synthesis of linear tetrapyrrole chromophores in cyanobacteria, algae, and plants, ooverview
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evolution
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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
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evolution
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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
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because PcyA and PebA, EC 1.3.7.6/1.3.7.3, utilize the same substrate, biliverdin IXalpha, severe overexpression of pebA can limit the availability of phycocyanobilin, which appears to be required for viability when cells are grown in continuous light
malfunction
both the pcya1-1 mutant with the C-terminal extension of PCYA1 eliminated and efficient knockdown of PCYA1 expression by artificial microRNA exhibit no significant impact on algal phototrophic growth and photosynthetic proteins accumulation, indicating that the conserved FDBR domain is sufficient and minimally required for bilin biosynthesis and functioning. Chlamydomonas PCYA1 uniquely interacts with light-dependent protochlorophyllide oxidoreductase LPOR (protochlorophyllide reductase, EC 1.3.1.33) but not with ferredoxin:protochlorophyllide reductase DPOR (EC 1.3.7.7). The CTE domain of PCYA1 is dispensable for phototrophic growth and photosynthetic proteins accumulation
malfunction
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both the pcya1-1 mutant with the C-terminal extension of PCYA1 eliminated and efficient knockdown of PCYA1 expression by artificial microRNA exhibit no significant impact on algal phototrophic growth and photosynthetic proteins accumulation, indicating that the conserved FDBR domain is sufficient and minimally required for bilin biosynthesis and functioning. Chlamydomonas PCYA1 uniquely interacts with light-dependent protochlorophyllide oxidoreductase LPOR (protochlorophyllide reductase, EC 1.3.1.33) but not with ferredoxin:protochlorophyllide reductase DPOR (EC 1.3.7.7). The CTE domain of PCYA1 is dispensable for phototrophic growth and photosynthetic proteins accumulation
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malfunction
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because PcyA and PebA, EC 1.3.7.6/1.3.7.3, utilize the same substrate, biliverdin IXalpha, severe overexpression of pebA can limit the availability of phycocyanobilin, which appears to be required for viability when cells are grown in continuous light
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Thermosynechococcus vestitus
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PcyA is involved in the phycocyanobilin biosynthetic pathway, in which PcyA first forms a stable complexes with the biliverdin IXa molecule
metabolism
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phycocyanobilin:ferredoxin oxidoreductase, PcyA, is a key enzyme in the biogenesis of heme-derived linear tetrapyrroles, phytobilins, it catalyzes the overall four-electron reduction of biliverdin IXalpha to phycocyanobilin, the common chromophore precursor for both classes of biliproteins
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
metabolism
ferredoxin-dependent biliverdin reductase, PCYA1, is a key enzyme involved in the biosynthesis of bilins, mechanism of bilin-mediated regulation of chlorophyll biosynthesis, and regulatory mechanisms of tetrapyrrole biosynthesis in Chlamydomonas reinhardtii, overview
metabolism
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ferredoxin-dependent biliverdin reductase, PCYA1, is a key enzyme involved in the biosynthesis of bilins, mechanism of bilin-mediated regulation of chlorophyll biosynthesis, and regulatory mechanisms of tetrapyrrole biosynthesis in Chlamydomonas reinhardtii, overview
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metabolism
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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
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unlike other ferredoxin-dependent bilin reductases that catalyze a two-electron reduction, PcyA sequentially reduces D-ring (exo) and A-ring (endo) vinyl groups of biliverdin IXalpha to yield phycocyanobilin, a key pigment precursor of the light-harvesting antennae complexes of red algae, cyanobacteria, and cryptophytes
physiological function
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bilin reductase PcyA catalyzes the proton-coupled four-electron reduction of biliverdin IXa's two vinyl groups to produce phycocyanobilin, an essential chromophore for phytochromes, cyanobacteriochromes and phycobiliproteins
physiological function
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the pcyA gene of Synechococcus sp. strain PCC 7002 is essential
physiological function
in Chlamydomonas reinhardtii, bilins are not only essential retrograde signals to mitigate oxidative stress during diurnal dark-to-light transitions, they are also required for chlorophyll accumulation and maintenance of a functional photosynthetic apparatus in the light. The ferredoxin-dependent biliverdin reductase, FDBR, is involved in the biosynthesis of bilins. Chlamydomonas phycocyanobilin:ferredoxin oxidoreductase PCYA1 FDBR domain specifically interacts with the rate-limiting chlorophyll biosynthetic enzyme LPOR (light-dependent protochlorophyllide oxidoreductase). CrPCYA1 is a key enzyme involved in bilin biosynthesis in Chlamydomonas. Regulatory role of PCYA1 in chlorophyll biosynthesis via interaction with key Chl biosynthetic enzyme. Chlamydomonas PCYA1 contains unique N- and C-terminal extensions which exhibit autoactivation activity in yeast two-hybrid system
physiological function
phycocyanobilin (PCB) is synthesized by phycocyanobilin:ferredoxin oxidoreductase (PcyA). The reaction of PcyA starts from biliverdin IXalpha (BV), which is a product of the heme oxygenase-mediated cleavage of the heme macrocycle, to PCB through four-electron reduction
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
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
physiological function
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in Chlamydomonas reinhardtii, bilins are not only essential retrograde signals to mitigate oxidative stress during diurnal dark-to-light transitions, they are also required for chlorophyll accumulation and maintenance of a functional photosynthetic apparatus in the light. The ferredoxin-dependent biliverdin reductase, FDBR, is involved in the biosynthesis of bilins. Chlamydomonas phycocyanobilin:ferredoxin oxidoreductase PCYA1 FDBR domain specifically interacts with the rate-limiting chlorophyll biosynthetic enzyme LPOR (light-dependent protochlorophyllide oxidoreductase). CrPCYA1 is a key enzyme involved in bilin biosynthesis in Chlamydomonas. Regulatory role of PCYA1 in chlorophyll biosynthesis via interaction with key Chl biosynthetic enzyme. Chlamydomonas PCYA1 contains unique N- and C-terminal extensions which exhibit autoactivation activity in yeast two-hybrid system
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physiological function
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the pcyA gene of Synechococcus sp. strain PCC 7002 is essential
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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
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physiological function
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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
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cyanobacteria utilize phycocyanobilin:ferredoxin oxidoreductase (PcyA) to perform a two-step reaction, the enzyme first reduces the 18-vinyl side chain of the D-ring and subsequently reduces the vinyl side chain of the pyrrole A ring to yield phycocyanobilin
additional information
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the fully conserved residue His74 plays a critical role in the H-bonding network that permits proton transfer, molecular dynamics simulations, overview. A conserved buried water molecule that bridges His74 and catalytically essential His88 is not required for activity. The crucial active site residue Asp105 is more dynamic in H74A compared to wild-type PcyA and the two other His74 variants, supporting the conclusion that the Ala74 mutation has increased the flexibility of the active site. Structure analysis of recombinant wild-type and mutant enzymes, overview
additional information
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the interconversion occurs via semireduced bilin radical intermediates that are profoundly stabilized by selected mutations of two critical catalytic residues, Asp105 and His88. Mechanistic scheme for PcyA-mediated reduction of both vinyl groups of biliverdin wherein an axial water molecule, which prematurely binds and ejects from both mutants upon one electron reduction, is required for catalytic turnover of the semireduced state, structure-function relationship, overview
additional information
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the NADPH-dependent biliverdin reductases, BVR and BvdR, are less accommodating to amidation of the propionic acid side chains of biliverdin IXR than PcyA, which does not require free carboxylic acid side chains to yield its phytobilin product, phycocyanobilin
additional information
besides the putative chloroplast transit peptide (TP) and the conserved ferredoxin-dependent biliverdin reductase (FDBR) domain, Chlamydomonas CrPCYA1 contains additional N-terminal extension (NTE) and C-terminal extension (CTE), approximately 120 and 108 amino acids, respectively
additional information
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besides the putative chloroplast transit peptide (TP) and the conserved ferredoxin-dependent biliverdin reductase (FDBR) domain, Chlamydomonas CrPCYA1 contains additional N-terminal extension (NTE) and C-terminal extension (CTE), approximately 120 and 108 amino acids, respectively
additional information
quantum mechanical/molecular mechanical (QM/MM) studies investigating the most probable protonation states of active site amino acids and bound substrate based on a recently reported neutron diffraction structure of phycocyanobilin: ferredoxin oxidoreductase (PcyA), overview. The hydronium ion (H3O+) is energetically unfavorable, preferentially protonating the neighboring His88 residue and that the C-ring of BV is not protonated. The hydronium ion forms hydrogen bonds with His88 (Nepsilon), His74 (Ndelta) and Leu243 (Carbonyl O) residues
additional information
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the NADPH-dependent biliverdin reductases, BVR and BvdR, are less accommodating to amidation of the propionic acid side chains of biliverdin IXR than PcyA, which does not require free carboxylic acid side chains to yield its phytobilin product, phycocyanobilin
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additional information
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besides the putative chloroplast transit peptide (TP) and the conserved ferredoxin-dependent biliverdin reductase (FDBR) domain, Chlamydomonas CrPCYA1 contains additional N-terminal extension (NTE) and C-terminal extension (CTE), approximately 120 and 108 amino acids, respectively
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additional information
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cyanobacteria utilize phycocyanobilin:ferredoxin oxidoreductase (PcyA) to perform a two-step reaction, the enzyme first reduces the 18-vinyl side chain of the D-ring and subsequently reduces the vinyl side chain of the pyrrole A ring to yield phycocyanobilin
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