1.3.7.6: phycoerythrobilin synthase
This is an abbreviated version!
For detailed information about phycoerythrobilin synthase, go to the full flat file.
Word Map on EC 1.3.7.6
-
1.3.7.6
-
tetrapyrrole
-
cyanobacteria
-
light-harvesting
-
cyanophage
-
phycobiliproteins
-
heme
-
oceanic
-
phycobilisome
-
chromophore
-
fdbrs
-
ferredoxin-dependent
-
open-chain
-
synechococcus
-
myovirus
-
phycobilin
-
antenna
-
metagenomes
-
phycocyanobilin:ferredoxin
-
oxygenase
-
peba
-
prochlorococcus
-
reductases
-
phycocyanobilin
-
algae
- 1.3.7.6
- tetrapyrrole
- cyanobacteria
-
light-harvesting
-
cyanophage
-
phycobiliproteins
- heme
-
oceanic
-
phycobilisome
- chromophore
-
fdbrs
-
ferredoxin-dependent
-
open-chain
- synechococcus
-
myovirus
-
phycobilin
-
antenna
- metagenomes
-
phycocyanobilin:ferredoxin
- oxygenase
-
peba
- prochlorococcus
- reductases
- phycocyanobilin
- algae
Reaction
+ 2 oxidized ferredoxin = + 2 reduced ferredoxin + 4 H+
Synonyms
EBK42635, FDBR, ferredoxin-dependent bilin reductase, PcyX, PEB synthase, PebA, PebB, PebS, PhiPcyX, phycoerythrobilin synthase
ECTree
Advanced search results
Engineering
Engineering on EC 1.3.7.6 - phycoerythrobilin synthase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
D105E
D206E
D206N
C71A
-
site-directed mutagenesis, mutant shows reduced activity compared to wild-type
H200Q
-
site-directed mutagenesis, the PcyX mutant shows a faster turnover compared with to wild-type enzyme
H69Q
-
site-directed mutagenesis, altered substrate biliverdin binding compared to wild-type, the mutant shows highly reduced activity compared to wild-type
M67I
-
site-directed mutagenesis, mutant shows highly reduced activity compared to wild-type
additional information
-
site-directed mutagenesis, the mutant catalyzes only the first reaction step, i.e. the formation of 15,16-dihydrobiliverdin, reaction of EC 1.3.7.2
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
-
site-directed mutagenesis, the mutant catalyzes only the second reaction step, i.e. the formation of (3Z)-phycoerythrobilin from 15,16-dihydrobiliverdin, reaction of EC 1.3.7.3
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
-
site-directed mutagenesis, the mutant catalyzes only the first reaction step, i.e. the formation of 15,16-dihydrobiliverdin, reaction of EC 1.3.7.2
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
development and evaluation of an improved method for high yield production and purification of phycoerythrobilin (PEB) in Escherichia coli via heterologous expression where the two required enzymes heme oxygenase and PEB synthase subsequently convert the substrate heme provided by the host cell. Experiments in shaking flasks result in the highest product yield of 0.680 mg PEB per g cell dry weight, by induction with 0.1 mM IPTG. Scale-up to batch-operated fermentation in a 2 L bioreactor reached product concentrations up to 5.02 mg PEB/l by adjustment of aeration, induction time, media composition and supplementation of precursors, separation of PEB from developed foam above the culture, detailed overview
additional information
-
because PcyA, EC 1.3.7.5, and PebA 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, phenotype, overview
additional information
-
because PcyA, EC 1.3.7.5, and PebA 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, phenotype, overview
-
additional information
-
a conserved aspartate-histidine pair is critical for activity. The same residues are part of a catalytic Asp-His-Glu triad in PcyA (EC 1.3.7.2), including an additional Glu. While this Glu residue is replaced by Asp in PcyX, it is not involved in catalysis. Substitution back to a Glu fails to convert PcyX to a PcyA