| EC |
4.4.1.32 |
| Accepted name: |
C-phycocyanin α-cysteine-84 phycocyanobilin lyase |
| Reaction: |
[C-phycocyanin α-subunit]-Cys84-phycocyanobilin = apo-[C-phycocyanin α-subunit] + (2R,3E)-phycocyanobilin |
| Glossary: |
phycocyanobilin = 3,31-didehydro-2,3-dihydromesobiliverdin |
| Other name(s): |
cpcE (gene name); cpcF (gene name) |
| Systematic name: |
[C-phycocyanin α-subunit]-Cys84-phycocyanobilin:(2R,3E)-phycocyanobilin lyase |
| Comments: |
The enzyme, characterized from the cyanobacterium Synechococcus elongatus PCC 7942, catalyses the covalent attachment of the phycobilin chromophore phycocyanobilin to cysteine 84 of the α subunit of the phycobiliprotein C-phycocyanin. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Fairchild, C.D., Zhao, J., Zhou, J., Colson, S.E., Bryant, D.A. and Glazer, A.N. Phycocyanin α-subunit phycocyanobilin lyase. Proc. Natl. Acad. Sci. USA 89 (1992) 7017–7021. [DOI] [PMID: 1495995] |
| 2. |
Fairchild, C.D. and Glazer, A.N. Oligomeric structure, enzyme kinetics, and substrate specificity of the phycocyanin α subunit phycocyanobilin lyase. J. Biol. Chem. 269 (1994) 8686–8694. [PMID: 8132596] |
| 3. |
Bhalerao, R.P., Lind, L.K. and Gustafsson, P. Cloning of the cpcE and cpcF genes from Synechococcus sp. PCC 6301 and their inactivation in Synechococcus sp. PCC 7942. Plant Mol. Biol. 26 (1994) 313–326. [PMID: 7524727] |
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| [EC 4.4.1.32 created 2015] |
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