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:4.4.1.32
Description:C-phycocyanin alpha-cysteine-84 phycocyanobilin lyase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.4.1.32
BRENDA Enzyme Link: BRENDA 4.4.1.32
KEGG Enzyme Link: KEGG4.4.1.32
BioCyc Enzyme Link: BioCyc 4.4.1.32
ExPASy Enzyme Link: ExPASy4.4.1.32
EC2PDB Enzyme Link: EC2PDB 4.4.1.32
ExplorEnz Enzyme Link: ExplorEnz 4.4.1.32
PRIAM enzyme-specific profiles Link: PRIAM 4.4.1.32
IntEnz Enzyme Link: IntEnz 4.4.1.32
MEDLINE Enzyme Link: MEDLINE 4.4.1.32
MSA:

4.4.1.32;

Phylogenetic Tree:

4.4.1.32;

Uniprot:
M-CSA:
RHEA:45524 [C-phycocyanin alpha-subunit]-Cys(84)-phycocyanobilin = (2R,3E)-phycocyanobilin + apo-[C-phycocyanin alpha-subunit]
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
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References

TitleAuthorsDatePubMed ID
Oligomeric structure, enzyme kinetics, and substrate specificity of the phycocyanin alpha subunit phycocyanobilin lyase.Fairchild CD, Glazer AN1994 Mar 258132596
Cloning of the cpcE and cpcF genes from Synechococcus sp. PCC 6301 and their inactivation in Synechococcus sp. PCC 7942.Bhalerao RP, Lind LK, Gustafsson P1994 Oct7524727
Phycocyanin alpha-subunit phycocyanobilin lyase.Fairchild CD, Zhao J, Zhou J, Colson SE, Bryant DA, Glazer AN1992 Aug 11495995