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Information on EC 1.3.7.3 - phycoerythrobilin:ferredoxin oxidoreductase
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1.3.7.3 phycoerythrobilin:ferredoxin oxidoreductaseIUBMB Comments
Catalyses the two-electron reduction of the C2 and C31 diene system of 15,16-dihydrobiliverdin. Specific for 15,16-dihydrobiliverdin. It has been proposed that this enzyme and EC 1.3.7.2, 15,16-dihydrobiliverdin:ferredoxin oxidoreductase, function as a dual enzyme complex in the conversion of biliverdin IXalpha to phycoerythrobilin.
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Word Map
- 1.3.7.3
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bilins
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light-harvesting
- biliverdin
- cyanobacteria
- tetrapyrrole
- phycocyanobilin
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ferredoxin-dependent
- algae
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phycobiliproteins
- chromophore
- reductases
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phycocyanobilin:ferredoxin
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phytochromes
- heme
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open-chain
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two-electron
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phycobilins
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ixalpha
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four-electron
- cryptophytes
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apophytochrome
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d-ring
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phycobilisomes
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guillardia
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neutron
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pink
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fdbrs
- theta
- oxygenases
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peba
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biliproteins
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vinyl
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
bilin reductase, phycoerythrobilin:ferredoxin oxidoreductase, peb:ferredoxin oxidoreductase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bilin reductase
ferredoxin:3Z-phycoerythrobilin oxidoreductase
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GtPEBB
oxidoreductase, ferredoxin:3Z-phycoerythrobilin
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PEB:ferredoxin oxidoreductase
PebB
PebB
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(3Z)-phycoerythrobilin + oxidized ferredoxin = 15,16-dihydrobiliverdin + reduced ferredoxin + 2 H+
(3Z)-phycoerythrobilin + oxidized ferredoxin = 15,16-dihydrobiliverdin + reduced ferredoxin + 2 H+
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(3Z)-phycoerythrobilin + oxidized ferredoxin = 15,16-dihydrobiliverdin + reduced ferredoxin + 2 H+
analysis of the reaction mechanism, after binding of 15,16-dihydrobiliverdin (DHBV) to the enzyme, Asp99 delivers a proton to the A-ring oxygen, forming a positively charged DHBVH+. After acceptance of an electron from ferredoxin, the A-ring pyrrole proton tautomerizes to the C2 position and is stabilized there. This is facilitated by the catalytic action of the axial water, which is activated/positioned by Asp219 and (indirectly) by Arg215. For the second protonation step, the reprotonation of the A-ring nitrogen, uptake of another electron, and a final tautomerization to yield the product PEB is assumed, flipped binding mode for PEB biosynthesis
(3Z)-phycoerythrobilin + oxidized ferredoxin = 15,16-dihydrobiliverdin + reduced ferredoxin + 2 H+
analysis of the reaction mechanism, after binding of 15,16-dihydrobiliverdin (DHBV) to the enzyme, Asp99 delivers a proton to the A-ring oxygen, forming a positively charged DHBVH+. After acceptance of an electron from ferredoxin, the A-ring pyrrole proton tautomerizes to the C2 position and is stabilized there. This is facilitated by the catalytic action of the axial water, which is activated/positioned by Asp219 and (indirectly) by Arg215. For the second protonation step, the reprotonation of the A-ring nitrogen, uptake of another electron, and a final tautomerization to yield the product PEB is assumed, flipped binding mode for PEB biosynthesis
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(3Z)-phycoerythrobilin:ferredoxin oxidoreductase
Catalyses the two-electron reduction of the C2 and C31 diene system of 15,16-dihydrobiliverdin. Specific for 15,16-dihydrobiliverdin. It has been proposed that this enzyme and EC 1.3.7.2, 15,16-dihydrobiliverdin:ferredoxin oxidoreductase, function as a dual enzyme complex in the conversion of biliverdin IXalpha to phycoerythrobilin.
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CAS REGISTRY NUMBER
COMMENTARY
347401-21-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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-
-
?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
3E-isomer occurs by non-enzyme-mediated side reaction caused by heat and reduced gluthathione
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-
?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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3E-isomer occurs by non-enzyme-mediated side reaction caused by heat and reduced gluthathione
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?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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biosynthesis of bilin pigments, functions with EC1.3.7.2. as a dual enzyme complex in the conversion of biliverdin Ixa into phycoerythrobilin
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?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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3E-isomer occurs by non-enzyme-mediated side reaction caused by heat and reduced gluthathione
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-
?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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biosynthesis of bilin pigments, functions with EC1.3.7.2. as a dual enzyme complex in the conversion of biliverdin Ixa into phycoerythrobilin
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?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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-
-
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?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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-
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?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
DHBV
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?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
DHBV
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?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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-
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?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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-
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r
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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-
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r
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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-
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?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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-
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r
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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-
-
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?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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r
additional information
?
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enzyme acts via a substrate radical mechanism. No substrate: biliverdin IXalpha
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?
additional information
?
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the open-chain tetrapyrrole substrate DHBV is bound in an unexpected flipped orientation within the canonical FDBR active site. Two central aspartate residues Asp99 and Asp219 as essential for catalytic activity. In addition, the conserved Arg215 plays a critical role in substrate specificity, binding orientation, and active site integrity
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additional information
?
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the open-chain tetrapyrrole substrate DHBV is bound in an unexpected flipped orientation within the canonical FDBR active site. Two central aspartate residues Asp99 and Asp219 as essential for catalytic activity. In addition, the conserved Arg215 plays a critical role in substrate specificity, binding orientation, and active site integrity
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additional information
?
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the open-chain tetrapyrrole substrate DHBV is bound in an unexpected flipped orientation within the canonical FDBR active site. Two central aspartate residues Asp99 and Asp219 as essential for catalytic activity. In addition, the conserved Arg215 plays a critical role in substrate specificity, binding orientation, and active site integrity
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additional information
?
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the enzyme performs substrate channeling with the 15,16-dihydrobiliverdin:ferredoxin oxidoreductase catalyzing the former catalytic step. Both enzymes transiently interact and that transfer of the intermediate is facilitated by a significantly higher binding affinity of DHBV toward phycoerythrobilin:ferredoxin oxidoreductase
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additional information
?
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development of an on-column assay with substrate channeling for FDBRs, transient interaction of both PebA and PebB during the conversion of biliverdin IXa (BV) to phycoerythrobilin (PEB) via 15,16-dihydrobiliverdin (DHBV)
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
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the enzyme performs substrate channeling with the 15,16-dihydrobiliverdin:ferredoxin oxidoreductase catalyzing the former catalytic step. Both enzymes transiently interact and that transfer of the intermediate is facilitated by a significantly higher binding affinity of DHBV toward phycoerythrobilin:ferredoxin oxidoreductase
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(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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biosynthesis of bilin pigments, functions with EC1.3.7.2. as a dual enzyme complex in the conversion of biliverdin Ixa into phycoerythrobilin
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?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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biosynthesis of bilin pigments, functions with EC1.3.7.2. as a dual enzyme complex in the conversion of biliverdin Ixa into phycoerythrobilin
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?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
the gene pebB is localized on the plastid of the cryptophyte or cryptomonad
UniProt
brenda
the gene pebB is localized on the plastid of the cryptophyte or cryptomonad
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
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the enzyme belongs to the the ferredoxin-dependent bilin reductase family. All members of the FDBR family are radical enzymes
evolution
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the enzyme belongs to the the ferredoxin-dependent bilin reductase family. All members of the FDBR family are radical enzymes
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metabolism
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PebB, i.e. phycoerythrobilinPEB:ferredoxin oxidoreductase, acts in tandem with PebA, i.e. 15,16-DHBV:ferredoxin oxidoreductase, EC 1.3.7.2, which reduces biliverdin IXalpha at the C15-C16 double bond to produce 15,16-dihydrobiliverdin. Both enzymes function in close contact for metabolic channeling of 15,16-dihydrobiliverdin
metabolism
during the biosynthesis of light-harvesting phycobilins in cyanobacteria, two members of the ferredoxin-dependent bilin reductases are involved in the reduction of the open-chain tetrapyrrole biliverdin IXa to the pink pigment phycoerythrobilin. The first reaction is catalyzed by 15,16-dihydrobiliverdin:ferredoxin oxidoreductase (PebA, EC 1.3.7.2) and produces the unstable intermediate 15,16-dihydrobiliverdin (DHBV). This intermediate is subsequently channeled to and converted by phycoerythrobilin:ferredoxin oxidoreductase to the final product phycoerythrobilin. An on-column assay employing immobilized enzyme in combination with UV-Vis and fluorescence spectroscopy reveals that both enzymes transiently interact and that transfer of the intermediate is facilitated by a significantly higher binding affinity of DHBV toward phycoerythrobilin:ferredoxin oxidoreductase (PebB). The intermediate DHBV is transferred via proximity channeling
metabolism
phycobilins are light-harvesting pigments of cyanobacteria, red algae, and cryptophytes. The biosynthesis of phycoerythrobilin (PEB) is catalyzed by the subsequent action of two ferredoxin-dependent bilin reductases (FDBRs). 15,16-Dihydrobiliverdin (DHBV):ferredoxin oxidoreductase (PebA) catalyzes the two-electron reduction of biliverdin IXalpha to 15,16-DHBV, and PEB:ferredoxin oxidoreductase (PebB) reduces this intermediate further to PEB. The biosynthetic intermediate DHBV is transferred via proximity channeling to PEB:ferredoxin oxidoreductase (PebB). PebB is thus far the only FDBR member that cannot use BV as a substrate. In contrast the semireduced 15,16-DHBV is employed. Upon binding, this substrate is also protonated by the central aspartate. During the reaction, a second aspartate residue gets involved and likely serves as a proton donor for the proton coupled electron transfer to the A-ring of the tetrapyrrole molecule. This reaction catalyzed by PebB is a formal reduction of the 2,3,31,32-dien system of the A-ring of 15,16-DHBV
metabolism
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PebB, i.e. phycoerythrobilinPEB:ferredoxin oxidoreductase, acts in tandem with PebA, i.e. 15,16-DHBV:ferredoxin oxidoreductase, EC 1.3.7.2, which reduces biliverdin IXalpha at the C15-C16 double bond to produce 15,16-dihydrobiliverdin. Both enzymes function in close contact for metabolic channeling of 15,16-dihydrobiliverdin
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metabolism
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phycobilins are light-harvesting pigments of cyanobacteria, red algae, and cryptophytes. The biosynthesis of phycoerythrobilin (PEB) is catalyzed by the subsequent action of two ferredoxin-dependent bilin reductases (FDBRs). 15,16-Dihydrobiliverdin (DHBV):ferredoxin oxidoreductase (PebA) catalyzes the two-electron reduction of biliverdin IXalpha to 15,16-DHBV, and PEB:ferredoxin oxidoreductase (PebB) reduces this intermediate further to PEB. The biosynthetic intermediate DHBV is transferred via proximity channeling to PEB:ferredoxin oxidoreductase (PebB). PebB is thus far the only FDBR member that cannot use BV as a substrate. In contrast the semireduced 15,16-DHBV is employed. Upon binding, this substrate is also protonated by the central aspartate. During the reaction, a second aspartate residue gets involved and likely serves as a proton donor for the proton coupled electron transfer to the A-ring of the tetrapyrrole molecule. This reaction catalyzed by PebB is a formal reduction of the 2,3,31,32-dien system of the A-ring of 15,16-DHBV
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physiological function
phycobilins are light-harvesting pigments of cyanobacteria, red algae, and cryptophytes. The biosynthesis of phycoerythrobilin (PEB) is catalyzed by the subsequent action of two ferredoxin-dependent bilin reductases (FDBRs). 15,16-Dihydrobiliverdin (DHBV):ferredoxin oxidoreductase (PebA) catalyzes the two-electron reduction of biliverdin IXalpha to 15,16-DHBV, and PEB:ferredoxin oxidoreductase (PebB) reduces this intermediate further to PEB
physiological function
phycobilisomes are composed of a core of allophycocyanin (APC) and radiating rods of phycocyanin (PC) and, depending on the species, phycoerythrin (PE) and phycoerythrocyanin (PEC), respectively. The individual phycobiliproteins are constituted of alpha- and beta-subunits building heterodimers and ultimately heterohexamers. Each subunit has between one and three covalently linked phycobilins bound. The two most abundant phycobilins in cyanobacteria are phycocyanobilin (PCB) and phycoerythrobilin (PEB) which are attached via conserved cysteine residues. During the biosynthesis of light-harvesting phycobilins in cyanobacteria, two members of the ferredoxin-dependent bilin reductases are involved in the reduction of the open-chain tetrapyrrole biliverdin IXa to the pink pigment phycoerythrobilin. The first reaction is catalyzed by 15,16-dihydrobiliverdin:ferredoxin oxidoreductase (PebA, UniProt ID Q02189) and produces the unstable intermediate 15,16-dihydrobiliverdin (DHBV). This intermediate is subsequently converted by phycoerythrobilin:ferredoxin oxidoreductase (PebB) to the final product phycoerythrobilin
physiological function
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phycobilins are light-harvesting pigments of cyanobacteria, red algae, and cryptophytes. The biosynthesis of phycoerythrobilin (PEB) is catalyzed by the subsequent action of two ferredoxin-dependent bilin reductases (FDBRs). 15,16-Dihydrobiliverdin (DHBV):ferredoxin oxidoreductase (PebA) catalyzes the two-electron reduction of biliverdin IXalpha to 15,16-DHBV, and PEB:ferredoxin oxidoreductase (PebB) reduces this intermediate further to PEB
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additional information
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the highly conserved aspartate residues Asp107 and Asp231 are critical for the reduction. In addition to the importance of certain catalytic residues, the shape of the active site and consequently the binding of the substrate highly determines the catalytic properties
additional information
structure comparisons of Synechococcus WH8020 PebA and Guillardia theta PebB, overview. The Asp-99/Asp-219 pair is structurally conserved in most FDBRs, while the corresponding residues are relevant for PebB, for PebA only the homologue of Asp99 (Asp84) is essential for catalytic activity. The homologue of Asp219 (Asp205) is not essential and is rotated out of the active site. PebB binds DHBV analogous to the binding of BV in PebA/PebS
additional information
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structure comparisons of Synechococcus WH8020 PebA and Guillardia theta PebB, overview. The Asp-99/Asp-219 pair is structurally conserved in most FDBRs, while the corresponding residues are relevant for PebB, for PebA only the homologue of Asp99 (Asp84) is essential for catalytic activity. The homologue of Asp219 (Asp205) is not essential and is rotated out of the active site. PebB binds DHBV analogous to the binding of BV in PebA/PebS
additional information
the structures of PebB exhibit the typical alpha/beta/alpha-sandwich fold with a central antiparallel beta-sheet, flanked by alpha-helices. The open-chain tetrapyrrole substrate DHBV is bound in an unexpected flipped orientation within the canonical FDBR active site. Two central aspartate residues Asp99 and Asp219 as essential for catalytic activity. In addition, the conserved Arg215 plays a critical role in substrate specificity, binding orientation, and active site integrity. Because these critical residues are conserved within certain FDBRs displaying A-ring reduction activity, it is proposed that they present a conserved mechanism for this reaction. The flipped substrate-binding mode indicates that two-electron reducing FDBRs utilize the same primary site within the binding pocket and that substrate orientation is the determinant for Aor D-ring regiospecificity. Enzyme structure-function analysis, overview
additional information
-
the structures of PebB exhibit the typical alpha/beta/alpha-sandwich fold with a central antiparallel beta-sheet, flanked by alpha-helices. The open-chain tetrapyrrole substrate DHBV is bound in an unexpected flipped orientation within the canonical FDBR active site. Two central aspartate residues Asp99 and Asp219 as essential for catalytic activity. In addition, the conserved Arg215 plays a critical role in substrate specificity, binding orientation, and active site integrity. Because these critical residues are conserved within certain FDBRs displaying A-ring reduction activity, it is proposed that they present a conserved mechanism for this reaction. The flipped substrate-binding mode indicates that two-electron reducing FDBRs utilize the same primary site within the binding pocket and that substrate orientation is the determinant for Aor D-ring regiospecificity. Enzyme structure-function analysis, overview
additional information
-
the highly conserved aspartate residues Asp107 and Asp231 are critical for the reduction. In addition to the importance of certain catalytic residues, the shape of the active site and consequently the binding of the substrate highly determines the catalytic properties
-
additional information
-
structure comparisons of Synechococcus WH8020 PebA and Guillardia theta PebB, overview. The Asp-99/Asp-219 pair is structurally conserved in most FDBRs, while the corresponding residues are relevant for PebB, for PebA only the homologue of Asp99 (Asp84) is essential for catalytic activity. The homologue of Asp219 (Asp205) is not essential and is rotated out of the active site. PebB binds DHBV analogous to the binding of BV in PebA/PebS
-
additional information
-
the structures of PebB exhibit the typical alpha/beta/alpha-sandwich fold with a central antiparallel beta-sheet, flanked by alpha-helices. The open-chain tetrapyrrole substrate DHBV is bound in an unexpected flipped orientation within the canonical FDBR active site. Two central aspartate residues Asp99 and Asp219 as essential for catalytic activity. In addition, the conserved Arg215 plays a critical role in substrate specificity, binding orientation, and active site integrity. Because these critical residues are conserved within certain FDBRs displaying A-ring reduction activity, it is proposed that they present a conserved mechanism for this reaction. The flipped substrate-binding mode indicates that two-electron reducing FDBRs utilize the same primary site within the binding pocket and that substrate orientation is the determinant for Aor D-ring regiospecificity. Enzyme structure-function analysis, overview
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Show AA Sequence and Transmembrane Helices (334 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the structures of PebB exhibit the typical alpha/beta/alpha-sandwich fold with a central antiparallel beta-sheet, flanked by alpha-helices. Enzyme structure-function analysis, overview
additional information
-
the structures of PebB exhibit the typical alpha/beta/alpha-sandwich fold with a central antiparallel beta-sheet, flanked by alpha-helices. Enzyme structure-function analysis, overview
additional information
-
the structures of PebB exhibit the typical alpha/beta/alpha-sandwich fold with a central antiparallel beta-sheet, flanked by alpha-helices. Enzyme structure-function analysis, overview
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified substrate-free and -bound wild-type, selenomethionine-labeled enzyme PebB, hanging drop vapor diffusion method, mixing of 0.001 ml of 7 mg/ml protein solution with or without substrate, and 0.001 ml of reservoir solution containing 0.1 M Tris, pH 8.5, 34.5% PEG 3350, and 0.15 M ammonium sulfate, 4 days, 4°C, method optimization, X-ray diffraction structure determination and analysis at 1.90 A and 1.65 A, respectively
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
analysis wether addition of PebB to the immobilized PebA-DHBV complex will result in the interaction of PebA and PebB and, therefore, cause retention of PebB on the column. Retention of PebB on the immobilized PebA column is not observed, but a transfer of almost all PebA-bound DHBV to PebB is seen, DHBV is washed off the column with regular washing buffer. in Synechococcus sp. WH8020, the genes encoding for pebA and pebB share an overlapping region. The pebA stop codon TGA is part of the pebB start codon ATG. In order to generate a translational fusion between pebA and pebB, a guanine base is inserted into the start-stop region of the pebAB-operon generating an artificial fusion of both enzymes, termed PebAgB. The newly generated codon GTG encodes for a valine residue, which now serves as a diminutive linker between PebA and PebB. This fusion protein is significantly different to the phage encoded PebS (EC 1.3.7.6), which is a homologue to PebA. But the fusion protein PebAgB shows PebS-like activity. Comparison of the PebAgB-catalyzed conversion of BV with an assay containing both PebA and PebB reveals no significant changes in velocity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by two affinity chromatography steps to 90% purity and a third gel filtration step
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recombinant GST-tagged or His-tagged PebB from Escherichia coli BL21(DE3) by glutathione or nickel affinity chromatography, gel filtration, and ultrafiltration, recombinant tagged PebAgB by affinity chromatography
recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli by DNA removal from cell extract, ultracentrifugation at 220000 x g, glutathione affinity chromatography and cleavage of the tag through TEV protease, followed by dialysis and a second step of glutathione affinity chromatography to remove that tag, gel filtration, and ultrafiltration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene pebB, in Synechococcus sp. WH8020, the genes encoding for pebA and pebB share an overlapping region. The pebA stop codon TGA is part of the pebB start codon ATG, recombinant expression of a translational fusion between pebA and pebB, N-terminally Strep-tagged and C-terminally His-tagged PebAgB, recombinant expression of GST-tagged or His-tagged PebB in Escherichia coli BL21(DE3)
gene pebB, recombinant expression of the codon optimized gene, without signal peptide, in Escherichia coli, expression of GST-tagged wild-type and mutant enzymes in Escherichia coli
into pASK-IBA45+ and transformed in Escherichia coli DH10B cells
into vector pKT270, co-expression with cyanobacterial phytochrome 1 in Escherichia coli JM109
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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metabolic engineering of bacteria for the production of various bilins for assembly into phytochromes will facilitate the molecular analysis of photoreceptors
additional information
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metabolic engineering of bacteria for the production of various bilins for assembly into phytochromes will facilitate the molecular analysis of photoreceptors
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Frankenberg, N.; Mukougawa, K.; Kohchi, T.; Lagarias, J.C.
Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms
Plant Cell
13
965-978
2001
Prochlorococcus sp., Synechococcus sp., Nostoc punctiforme (Q93TM8)
brenda
Alvey, R.M.; Karty, J.A.; Roos, E.; Reilly, J.P.; Kehoe, D.M.
Lesions in phycoerythrin chromophore biosynthesis in Fremyella diplosiphon reveal coordinated light regulation of apoprotein and pigment biosynthetic enzyme gene expression
Plant Cell
15
2448-2463
2003
Microchaete diplosiphon
brenda
Mukougawa, K.; Kanamoto, H.; Kobayashi, T.; Yokota, A.; Kohchi, T.
Metabolic engineering to produce phytochromes with phytochromobilin, phycocyanobilin, or phycoerythrobilin chromophore in Escherichia coli
FEBS Lett.
580
1333-1338
2006
Synechococcus sp., Synechococcus sp. W8020
brenda
Dammeyer, T.; Frankenberg-Dinkel, N.
Insights into phycoerythrobilin biosynthesis point toward metabolic channeling
J. Biol. Chem.
281
27081-27089
2006
Synechococcus sp., Microchaete diplosiphon (Q6UR87), Microchaete diplosiphon, Synechococcus sp. WH8020, Microchaete diplosiphon Fd33 (Q6UR87)
brenda
Busch, A.W.; Reijerse, E.J.; Lubitz, W.; Frankenberg-Dinkel, N.; Hofmann, E.
Structural and mechanistic insight into the ferredoxin-mediated two-electron reduction of bilins
Biochem. J.
439
257-264
2011
Synechococcus sp., Synechococcus sp. WH8020
brenda
Overkamp, K.; Gasper, R.; Kock, K.; Herrmann, C.; Hofmann, E.; Frankenberg-Dinkel, N.
Insights into the biosynthesis and assembly of cryptophycean phycobiliproteins
J. Biol. Chem.
289
26691-26707
2014
Guillardia theta
brenda
Aras, M.; Hartmann, V.; Hartmann, J.; Nowaczyk, M.M.; Frankenberg-Dinkel, N.
Proximity channeling during cyanobacterial phycoerythrobilin synthesis
FEBS J.
287
284-294
2020
Synechococcus sp. WH 8020 (Q02190)
brenda
Sommerkamp, J.; Frankenberg-Dinkel, N.; Hofmann, E.
Crystal structure of the first eukaryotic bilin reductase GtPEBB reveals a flipped binding mode of dihydrobiliverdin
J. Biol. Chem.
294
13889-13901
2019
Guillardia theta (L1IWQ9), Guillardia theta, Guillardia theta CCMP2712 (L1IWQ9)
brenda
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Release 2023.1 (January 2023)
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