EC Tree |
4. Lyases |
4.4 Carbon-sulfur lyases |
4.4.1 Carbon-sulfur lyases (only sub-subclass identified to date) |
ID: | 4.4.1.30 |
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Description: | Phycobiliprotein beta-cysteine-155 phycobilin lyase. |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.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 |
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 |
Title | Authors | Date | PubMed 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 X | 2014 Sep 26 | 25074932 |
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 BR | 2014 Jul 10 | 24768724 |
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 M | 2007 Nov 23 | 17895251 |
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 |
Title | Authors | Date | PubMed 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 X | 2014 Sep 26 | 25074932 |
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 BR | 2014 Jul 10 | 24768724 |
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 M | 2007 Nov 23 | 17895251 |