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IUBMB CommentsThe 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.
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[C-phycocyanin beta-subunit]-Cys155-phycocyanobilin = apo-[C-phycocyanin beta-subunit] + (2R,3E)-phycocyanobilin
[phycoerythrocyanin beta-subunit]-Cys155-phycocyanobilin = apo-[phycoerythrocyanin beta-subunit] + (2R,3E)-phycocyanobilin
[C-phycocyanin beta-subunit]-Cys155-phycocyanobilin = apo-[C-phycocyanin beta-subunit] + (2R,3E)-phycocyanobilin
(1)
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[C-phycocyanin beta-subunit]-Cys155-phycocyanobilin = apo-[C-phycocyanin beta-subunit] + (2R,3E)-phycocyanobilin
(1)
[C-phycocyanin beta-subunit]-Cys155-phycocyanobilin = apo-[C-phycocyanin beta-subunit] + (2R,3E)-phycocyanobilin
(1)
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[phycoerythrocyanin beta-subunit]-Cys155-phycocyanobilin = apo-[phycoerythrocyanin beta-subunit] + (2R,3E)-phycocyanobilin
(2)
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[phycoerythrocyanin beta-subunit]-Cys155-phycocyanobilin = apo-[phycoerythrocyanin beta-subunit] + (2R,3E)-phycocyanobilin
(2)
[phycoerythrocyanin beta-subunit]-Cys155-phycocyanobilin = apo-[phycoerythrocyanin beta-subunit] + (2R,3E)-phycocyanobilin
(2)
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apo-[C-phycocyanin beta-subunit] + (2R,3E)-phycocyanobilin
[C-phycocyanin beta-subunit]-Cys155-phycocyanobilin
apo-[phycocyanin beta-subunit] + phycocyanobilin
[phycocyanin beta-subunit]-Cys153-phycocyanobilin
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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
apo-[phycoerythrin alpha-subunit] + phycoerythrobilin
[phycoerythrin beta-subunit]-Cys82-phycoerythrobilin
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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
additional information
?
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apo-[C-phycocyanin beta-subunit] + (2R,3E)-phycocyanobilin
[C-phycocyanin beta-subunit]-Cys155-phycocyanobilin
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?
apo-[C-phycocyanin beta-subunit] + (2R,3E)-phycocyanobilin
[C-phycocyanin beta-subunit]-Cys155-phycocyanobilin
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?
apo-[C-phycocyanin beta-subunit] + (2R,3E)-phycocyanobilin
[C-phycocyanin beta-subunit]-Cys155-phycocyanobilin
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?
apo-[C-phycocyanin beta-subunit] + (2R,3E)-phycocyanobilin
[C-phycocyanin beta-subunit]-Cys155-phycocyanobilin
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?
apo-[phycocyanin beta-subunit] + phycocyanobilin
[phycocyanin beta-subunit]-Cys155-phycocyanobilin
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?
apo-[phycocyanin beta-subunit] + phycocyanobilin
[phycocyanin beta-subunit]-Cys155-phycocyanobilin
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-
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?
apo-[phycoerythrocyanin beta-subunit] + (2R,3E)-phycocyanobilin
[phycoerythrocyanin beta-subunit]-Cys155-phycocyanobilin
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?
apo-[phycoerythrocyanin beta-subunit] + (2R,3E)-phycocyanobilin
[phycoerythrocyanin beta-subunit]-Cys155-phycocyanobilin
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?
additional information
?
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isoform CpcT1 cannot bind phycobilin
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?
additional information
?
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isoform CpcT1 cannot bind phycobilin
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?
additional information
?
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the enzyme specifically binds bilins with a reduced 15,16-double bond. The complex with phycoerythrobilin is highly stable and displays a strong red fluorescence. CpeT does not transfer phycoerythrobilin to the host phycobiliprotein beta-subunit but is able to assist the host layse
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?
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apo-[C-phycocyanin beta-subunit] + (2R,3E)-phycocyanobilin
[C-phycocyanin beta-subunit]-Cys155-phycocyanobilin
apo-[phycoerythrocyanin beta-subunit] + (2R,3E)-phycocyanobilin
[phycoerythrocyanin beta-subunit]-Cys155-phycocyanobilin
apo-[C-phycocyanin beta-subunit] + (2R,3E)-phycocyanobilin
[C-phycocyanin beta-subunit]-Cys155-phycocyanobilin
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?
apo-[C-phycocyanin beta-subunit] + (2R,3E)-phycocyanobilin
[C-phycocyanin beta-subunit]-Cys155-phycocyanobilin
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?
apo-[phycoerythrocyanin beta-subunit] + (2R,3E)-phycocyanobilin
[phycoerythrocyanin beta-subunit]-Cys155-phycocyanobilin
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?
apo-[phycoerythrocyanin beta-subunit] + (2R,3E)-phycocyanobilin
[phycoerythrocyanin beta-subunit]-Cys155-phycocyanobilin
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?
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?
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x * 22800, calculated from sequence
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x * 22800, calculated from sequence
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dimer
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
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
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monomer
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
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C116S
in vitro assay,11% of wild-type activity
C137S
in vitro assay, 11% of wild-type activity
D163A
lyase activity is less than 5% compared to wild-type enzyme
D163V
lyase activity is less than 5% compared to wild-type enzyme
D63N
lyase activity is about 70% compared to wild-type enzyme
E111Q
lyase activity is about 75% compared to wild-type enzyme
H33F
in vitro assay, 14% of wild-type activity
K87M
lyase activity is about 70% compared to wild-type enzyme
M118A
lyase activity is about 25% compared to wild-type enzyme
N83A
lyase activity is about 35% compared to wild-type enzyme
Q55A
lyase activity is about 30% compared to wild-type enzyme
R141I
lyase activity is about 15% compared to wild-type enzyme
R66A
in vitro assay, 15% of wild-type activity
R68A
lyase activity is about 10% compared to wild-type enzyme
R97A
in vitro assay, 37% of wild-type activity. Contrary to wild-type,a great deal of alpha helix is involved in circular dichroism
S150A
lyase activity is about 125% compared to wild-type enzyme
S161V
lyase activity is about 105% compared to wild-type enzyme
W13S
in vitro assay, 22% of wild-type activity. Contrary to wild-type,a great deal of alpha helix is involved in circular dichroism
W175S
in vitro assay, 14% of wild-type activity
Y59A
lyase activity is about 35% compared to wild-type enzyme
Y65F
lyase activity is less than 5% compared to wild-type enzyme
C116S
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in vitro assay,11% of wild-type activity
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E111Q
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lyase activity is about 75% compared to wild-type enzyme
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H33F
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in vitro assay, 14% of wild-type activity
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N83A
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lyase activity is about 35% compared to wild-type enzyme
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Q55A
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lyase activity is about 30% compared to wild-type enzyme
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R66A
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in vitro assay, 15% of wild-type activity
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R68A
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lyase activity is about 10% compared to wild-type enzyme
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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
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Y65F
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lyase activity is less than 5% compared to wild-type enzyme
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additional information
chemical modification of arginine, histidine, tryptophan, lysine and amino acid carboxyl groups of isoform CpcT1 decreases activity to 30-84% of wild-type
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
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Zhang, J.; Sun, Y.; Zhao, K.; Zhou, M.
Identification of amino acid residues essential to the activity of lyase CpcT1 from Nostoc sp. PCC7120
Gene
511
88-95
2012
Nostoc sp. (Q8YLF9), Nostoc sp. PCC 7120 (Q8YLF9)
brenda
Zhang, R.; Feng, X.T.; Wu, F.; Ding, Y.; Zang, X.N.; Zhang, X.C.; Yuan, D.Y.; Zhao, B.R.
Molecular cloning and expression analysis of a new bilin lyase: the cpcT gene encoding a bilin lyase responsible for attachment of phycocyanobilin to Cys-153 on the beta-subunit of phycocyanin in Arthrospira platensis FACHB314
Gene
544
191-197
2014
Arthrospira platensis, Arthrospira platensis FACHB314
brenda
Shen, G.; Saunee, N.; Williams, S.; Gallo, E.; Schluchter, W.; Bryant, D.
Identification and characterization of a new class of bilin lyase: The cpcT gene encodes a bilin lyase responsible for attachment of phycocyanobilin to Cys-153 on the beta-subunit of phycocyanin in Synechococcus sp. PCC 7002
J. Biol. Chem.
281
17768-17778
2006
Synechococcus sp. (B1XI94)
brenda
Zhao, K.; Zhang, J.; Tu, J.; Bhm, S.; Plscher, M.; Eichacker, L.; Bubenzer, C.; Scheer, H.; Wang, X.; Zhou, M.
Lyase activities of CpcS- and CpcT-like proteins from Nostoc PCC7120 and sequential reconstitution of binding sites of phycoerythrocyanin and phycocyanin beta-subunits
J. Biol. Chem.
282
34093-34103
2007
Nostoc sp. (Q8YLF9), Nostoc sp., Nostoc sp. PCC 7120 (Q8YLF9)
brenda
Biswas, A.; Boutaghou, M.; Alvey, R.; Kronfel, C.; Cole, R.; Bryant, D.; Schluchter, W.
Characterization of the activities of the CpeY, CpeZ, and CpeS bilin lyases in phycoerythrin biosynthesis in Fremyella diplosiphon strain UTEX 481
J. Biol. Chem.
286
35509-35521
2011
Microchaete diplosiphon (Q9ALZ8)
brenda
Zhou, W.; Ding, W.L.; Zeng, X.L.; Dong, L.L.; Zhao, B.; Zhou, M.; Scheer, H.; Zhao, K.H.; Yang, X.
Structure and mechanism of the phycobiliprotein lyase CpcT
J. Biol. Chem.
289
26677-26689
2014
Nostoc sp. (Q8YLF9), Nostoc sp. PCC 7120 (Q8YLF9)
brenda
Gasper, R.; Schwach, J.; Hartmann, J.; Holtkamp, A.; Wiethaus, J.; Riedel, N.; Hofmann, E.; Frankenberg-Dinkel, N.
Distinct features of cyanophage-encoded T-type phycobiliprotein lyase PhiCpeT The role of auxiliary metabolic genes
J. Biol. Chem.
292
3089-3098
2017
Prochlorococcus phage P-HM1 (E3SMK9)
brenda