HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 1.3.7.2 - 15,16-dihydrobiliverdin:ferredoxin oxidoreductase
for references in articles please use BRENDA:EC1.3.7.2
Word Map on EC 1.3.7.2
- 1.3.7.2
-
bilins
- ixalpha
- tetrapyrrole
-
a-ring
- phycocyanobilin
-
phycocyanobilin:ferredoxin
-
light-harvesting
- cyanobacteria
-
reductases
- phycoerythrobilin
- chlorophyll
- synechococcus
-
substrate-bound
- oxygenase
-
phytochrome
-
four-electron
-
phycobiliproteins
-
catabolite
-
proton-donating
- heme
-
substrate-free
-
chromophore
- algae
-
oceanic
-
sandwich
- epr
- nostoc
- prochlorococcus
-
phycobilisomes
- pheophorbide
-
cyanophage
-
antenna
-
enzyme-bound
-
alpha-helices
- cryptomonads
- synechocystis
-
apophytochromes
-
vinyl
-
two-electron
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
1.3.7.2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
15,16-dihydrobiliverdin:ferredoxin oxidoreductase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
15,16-dihydrobiliverdin + oxidized ferredoxin = biliverdin IXalpha + reduced ferredoxin
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
15,16-dihydrobiliverdin:ferredoxin oxidoreductase
Catalyses the two-electron reduction of biliverdin IXalpha at the C15 methine bridge. It has been proposed that this enzyme and EC 1.3.7.3, phycoerythrobilin:ferredoxin oxidoreductase, function as a dual enzyme complex in the conversion of biliverdin IXalpha into phycoerythrobilin.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
347401-20-1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
additional information
evolution
the enzyme belongs to the ferredoxin-dependent bilin reductase family. All members of the FDBR family are radical enzymes
evolution
-
the enzyme belongs to the ferredoxin-dependent bilin reductase family. All members of the FDBR family are radical enzymes
-
metabolism
PebB, phycoerythrobilinPEB:ferredoxin oxidoreductase, EC 1.3.7.3, acts in tandem with PebA, 15,16-DHBV:ferredoxin oxidoreductase, 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
-
PebB, phycoerythrobilinPEB:ferredoxin oxidoreductase, EC 1.3.7.3, acts in tandem with PebA, 15,16-DHBV:ferredoxin oxidoreductase, 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
-
additional information
the highly conserved aspartate residue Asp105 is 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
-
the highly conserved aspartate residue Asp105 is 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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 + oxidized ferrdoxin
biliverdin IXalpha + reduced ferrdoxin
the 15,16-DHBV:ferredoxin oxidoreductase PebA reduces biliverdin IXalpha at the C15C16 double bond to produce 15,16-dihydrobiliverdin
-
-
r
15,16-dihydrobiliverdin + oxidized ferrdoxin
biliverdin IXalpha + reduced ferrdoxin
the 15,16-DHBV:ferredoxin oxidoreductase PebA reduces biliverdin IXalpha at the C15C16 double bond to produce 15,16-dihydrobiliverdin, assay under anaerobic conditions
-
-
r
15,16-dihydrobiliverdin + oxidized ferrdoxin
biliverdin IXalpha + reduced ferrdoxin
the 15,16-DHBV:ferredoxin oxidoreductase PebA reduces biliverdin IXalpha at the C15C16 double bond to produce 15,16-dihydrobiliverdin
-
-
r
15,16-dihydrobiliverdin + oxidized ferrdoxin
biliverdin IXalpha + reduced ferrdoxin
the 15,16-DHBV:ferredoxin oxidoreductase PebA reduces biliverdin IXalpha at the C15C16 double bond to produce 15,16-dihydrobiliverdin, assay under anaerobic conditions
-
-
r
15,16-dihydrobiliverdin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
-
?
15,16-dihydrobiliverdin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
-
-
?
15,16-dihydrobiliverdin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
biosynthesis of bilin pigments, functions with EC1.3.7.3. as a dual enzyme complex in the conversion of biliverdin IXa into phycoerythrobilin
-
-
?
15,16-dihydrobiliverdin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
-
-
?
15,16-dihydrobiliverdin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
biosynthesis of bilin pigments, functions with EC1.3.7.3. as a dual enzyme complex in the conversion of biliverdin IXa into phycoerythrobilin
-
-
?
15,16-dihydrobiliverdin + reduced ferredoxin
phycoerythrobilin + oxidized ferredoxin
-
-
-
r
15,16-dihydrobiliverdin + reduced ferredoxin
phycoerythrobilin + oxidized ferredoxin
-
-
-
r
biliverdin IXa + reduced ferredoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
-
-
-
r
biliverdin IXa + reduced ferredoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
-
-
-
r
biliverdin IXa + reduced ferredoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
-
-
-
-
r
biliverdin IXa + reduced ferredoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
-
-
-
-
r
biliverdin IXalpha + reduced ferredoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
-
-
-
-
?
biliverdin IXalpha + reduced ferredoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
-
-
-
-
?
biliverdin IXalpha + reduced ferredoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
-
-
-
?
biliverdin IXalpha + reduced ferredoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
-
-
-
?
phytochromobilin + biliverdin IXa + reduced ferredoxin
phycoerythrobilin
-
-
-
-
r
phytochromobilin + biliverdin IXa + reduced ferredoxin
phycoerythrobilin
-
-
-
-
r
additional information
?
-
-
does not convert 3E-phycocyanobilin
-
-
-
additional information
?
-
does not convert 3E-phycocyanobilin
-
-
-
additional information
?
-
does not convert 3E-phycocyanobilin
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
biliverdin IXalpha + reduced ferredoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
-
-
-
-
?
15,16-dihydrobiliverdin + oxidized ferrdoxin
biliverdin IXalpha + reduced ferrdoxin
Q02189
the 15,16-DHBV:ferredoxin oxidoreductase PebA reduces biliverdin IXalpha at the C15C16 double bond to produce 15,16-dihydrobiliverdin
-
-
r
15,16-dihydrobiliverdin + oxidized ferrdoxin
biliverdin IXalpha + reduced ferrdoxin
Q02189
the 15,16-DHBV:ferredoxin oxidoreductase PebA reduces biliverdin IXalpha at the C15C16 double bond to produce 15,16-dihydrobiliverdin
-
-
r
15,16-dihydrobiliverdin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
biosynthesis of bilin pigments, functions with EC1.3.7.3. as a dual enzyme complex in the conversion of biliverdin IXa into phycoerythrobilin
-
-
?
15,16-dihydrobiliverdin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
biosynthesis of bilin pigments, functions with EC1.3.7.3. as a dual enzyme complex in the conversion of biliverdin IXa into phycoerythrobilin
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
insensitivity toward metal chelators like 0.01 mM EDTA, 0.005 mM o-phenanthroline, or 0.005 mM 2,2'-dipyridyl
-
additional information
insensitivity toward metal chelators like 0.01 mM EDTA, 0.005 mM o-phenanthroline, or 0.005 mM 2,2'-dipyridyl
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
ORGANISM
UNIPROT
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
PebA in complex with substrate biliverdin IXalpha, hanging drop vapour diffusion method, 12-20 mg/ml protein in 0.1 M HEPE, pH 7.0, and 28% PEG 4000, 18°C, X-ray diffraction structure determination and analysis at 1.55 A resolution
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by two affinity chromatography steps to 90% purity and a third gel filtration step
GST-tagged PebA forms inactive aggregates
by two affinity chromatography steps to 90% purity and a third gel filtration step
by two affinity chromatography steps to 90% purity and a third gel filtration step
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression in Escherichia coli
gene pebA, recombinant expression of wild-type and mutant enzymes, native and selenomethionine-labeled PebA
into pGEX-6P-3 vector for N-terminal fusion with glutathione S-transferase and transformed in Escherichia coli BL21(lambdaDE3) cells
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LINKS TO OTHER DATABASES (specific for EC-Number 1.3.7.2)
html completed
Use of this online version of BRENDA is free but requires a license. See terms of use.
Information
