Enzyme

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     4. Lyases
        4.4 Carbon-sulfur lyases
            4.4.1 Carbon-sulfur lyases (only sub-subclass identified to date)
ID:4.4.1.30
Description:Phycobiliprotein beta-cysteine-155 phycobilin lyase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.4.1.30
BRENDA Enzyme Link: BRENDA 4.4.1.30
KEGG Enzyme Link: KEGG4.4.1.30
BioCyc Enzyme Link: BioCyc 4.4.1.30
ExPASy Enzyme Link: ExPASy4.4.1.30
EC2PDB Enzyme Link: EC2PDB 4.4.1.30
ExplorEnz Enzyme Link: ExplorEnz 4.4.1.30
PRIAM enzyme-specific profiles Link: PRIAM 4.4.1.30
IntEnz Enzyme Link: IntEnz 4.4.1.30
MEDLINE Enzyme Link: MEDLINE 4.4.1.30
MSA:

4.4.1.30;

Phylogenetic Tree:

4.4.1.30;

Uniprot:
M-CSA:
RHEA:45516 [phycoerythrocyanin beta-subunit]-Cys(155)-phycocyanobilin = (2R,3E)-phycocyanobilin + apo-[phycoerythrocyanin beta-subunit]-Cys(155)
RULE(radius=1) [*:1]-[CH;+0:2](-[S;H0;+0:3]-[*:4])-[CH;+0:5](-[*:6])-[*:7]>>[*:1]-[CH;+0:2]=[C;H0;+0:5](-[*:6])-[*:7].[*:4]-[SH;+0:3]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Structure and mechanism of the phycobiliprotein lyase CpcT.Zhou W, Ding WL, Zeng XL, Dong LL, Zhao B, Zhou M, Scheer H, Zhao KH, Yang X2014 Sep 2625074932
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 β-subunit of phycocyanin in Arthrospira platensis FACHB314.Zhang R, Feng XT, Wu F, Ding Y, Zang XN, Zhang XC, Yuan DY, Zhao BR2014 Jul 1024768724
Lyase activities of CpcS- and CpcT-like proteins from Nostoc PCC7120 and sequential reconstitution of binding sites of phycoerythrocyanin and phycocyanin beta-subunits.Zhao KH, Zhang J, Tu JM, Böhm S, Plöscher M, Eichacker L, Bubenzer C, Scheer H, Wang X, Zhou M2007 Nov 2317895251

RHEA:45512 [C-phycocyanin beta-subunit]-Cys(155)-phycocyanobilin = (2R,3E)-phycocyanobilin + apo-[C-phycocyanin beta-subunit]-Cys(155)
RULE(radius=1) [*:1]-[CH;+0:2](-[S;H0;+0:3]-[*:4])-[CH;+0:5](-[*:6])-[*:7]>>[*:1]-[CH;+0:2]=[C;H0;+0:5](-[*:6])-[*:7].[*:4]-[SH;+0:3]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Structure and mechanism of the phycobiliprotein lyase CpcT.Zhou W, Ding WL, Zeng XL, Dong LL, Zhao B, Zhou M, Scheer H, Zhao KH, Yang X2014 Sep 2625074932
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 β-subunit of phycocyanin in Arthrospira platensis FACHB314.Zhang R, Feng XT, Wu F, Ding Y, Zang XN, Zhang XC, Yuan DY, Zhao BR2014 Jul 1024768724
Lyase activities of CpcS- and CpcT-like proteins from Nostoc PCC7120 and sequential reconstitution of binding sites of phycoerythrocyanin and phycocyanin beta-subunits.Zhao KH, Zhang J, Tu JM, Böhm S, Plöscher M, Eichacker L, Bubenzer C, Scheer H, Wang X, Zhou M2007 Nov 2317895251