Information on EC 4.4.1.30 - phycobiliprotein beta-cysteine-155 phycobilin lyase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.4.1.30
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RECOMMENDED NAME
GeneOntology No.
phycobiliprotein beta-cysteine-155 phycobilin lyase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[C-phycocyanin beta-subunit]-Cys155-phycocyanobilin = apo-[C-phycocyanin beta-subunit] + (2R,3E)-phycocyanobilin
show the reaction diagram
[phycoerythrocyanin beta-subunit]-Cys155-phycocyanobilin = apo-[phycoerythrocyanin beta-subunit] + (2R,3E)-phycocyanobilin
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
[phycobiliprotein beta-subunit]-Cys155-phycocyanobilin:phycocyanobilin lyase
The enzyme, found in cyanobacteria and red algae, catalyses the attachment of the phycobilin chromophore phycocyanobilin to cysteine 155 of the beta subunits of the phycobiliproteins C-phycocyanin and phycoerythrocyanin. The numbering used here corresponds to the enzyme from Anabaena, and could vary slightly in other organisms.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
cpcT null mutant contains 40% less phycocyanin than wild type and produces smaller phycobilisomes with red-shifted absorbance and fluorescence emission maxima. Phycocyanin from the cpcT mutant has an absorbance maximum at 634 nm compared with 626 nm for the wild-type. The phycocyanin beta-subunit from the cpcT mutant has slightly smaller apparent molecular weight on SDS-PAGE. No phycocyanobilin chromophore is bound to the peptide containing Cys153 derived from the phycocyanin beta-subunit of the cpcT mutant
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
apo-[C-phycocyanin beta-subunit] + (2R,3E)-phycocyanobilin
[C-phycocyanin beta-subunit]-Cys155-phycocyanobilin
show the reaction diagram
apo-[phycocyanin beta-subunit] + phycocyanobilin
[phycocyanin beta-subunit]-Cys153-phycocyanobilin
show the reaction diagram
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CpcT is a phycocyanobilin lyase that specifically attaches phycocyanobilin to Cys153 of the phycocyanin beta-subunit
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?
apo-[phycocyanin beta-subunit] + phycocyanobilin
[phycocyanin beta-subunit]-Cys155-phycocyanobilin
show the reaction diagram
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-
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?
apo-[phycoerythrin alpha-subunit] + phycoerythrobilin
[phycoerythrin beta-subunit]-Cys82-phycoerythrobilin
show the reaction diagram
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CpeS bilin lyase ligates phycoerythrobilin at both Cys82 and Cys139 of phycoerythrin alpha-subunit, but very inefficiently
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?
apo-[phycoerythrocyanin beta-subunit] + (2R,3E)-phycocyanobilin
[phycoerythrocyanin beta-subunit]-Cys155-phycocyanobilin
show the reaction diagram
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-
-
-
?
additional information
?
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isoform CpcT1 cannot bind phycobilin
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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
apo-[C-phycocyanin beta-subunit] + (2R,3E)-phycocyanobilin
[C-phycocyanin beta-subunit]-Cys155-phycocyanobilin
show the reaction diagram
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-
-
-
?
apo-[phycoerythrocyanin beta-subunit] + (2R,3E)-phycocyanobilin
[phycoerythrocyanin beta-subunit]-Cys155-phycocyanobilin
show the reaction diagram
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-
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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the in vitro reconstitutions required no cofactors
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.29
calculated from sequence
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22800
x * 22800, calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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at the concentration of 0.003 mM, the enzyme is mostly monomeric in the absence of phycocyanobilin, but it tends to dimerize in the presence of 0.006 mM phycocyanobilin
monomer
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at the concentration of 0.003 mM, the enzyme is mostly monomeric in the absence of phycocyanobilin, but it tends to dimerize in the presence of 0.006 mM phycocyanobilin
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of the apoenzyme and its complex with phycocyanobilin at 1.95 and 2.50 A resolution
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
overexpression in Escherichia coli BL21(DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C116S
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in vitro assay,11% of wild-type activity
C137S
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in vitro assay, 11% of wild-type activity
D163A
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lyase activity is less than 5% compared to wild-type enzyme
D163V
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lyase activity is less than 5% compared to wild-type enzyme
D63N
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lyase activity is about 70% compared to wild-type enzyme
E111Q
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lyase activity is about 75% compared to wild-type enzyme
H33F
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in vitro assay, 14% of wild-type activity
K87M
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lyase activity is about 70% compared to wild-type enzyme
M118A
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lyase activity is about 25% compared to wild-type enzyme
N83A
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lyase activity is about 35% compared to wild-type enzyme
Q55A
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lyase activity is about 30% compared to wild-type enzyme
R141I
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lyase activity is about 15% compared to wild-type enzyme
R66A
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in vitro assay, 15% of wild-type activity
R68A
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lyase activity is about 10% compared to wild-type enzyme
R97A
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in vitro assay, 37% of wild-type activity. Contrary to wild-type,a great deal of alpha helix is involved in circular dichroism
S150A
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lyase activity is about 125% compared to wild-type enzyme
S161V
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lyase activity is about 105% compared to wild-type enzyme
W13S
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in vitro assay, 22% of wild-type activity. Contrary to wild-type,a great deal of alpha helix is involved in circular dichroism
W175S
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in vitro assay, 14% of wild-type activity
Y59A
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lyase activity is about 35% compared to wild-type enzyme
Y65F
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lyase activity is less than 5% compared to wild-type enzyme
additional information
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chemical modification of arginine, histidine, tryptophan, lysine and amino acid carboxyl groups of isoform CpcT1 decreases activity to 30-84% of wild-type