The Enzyme Database

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EC 1.3.1.80      
Transferred entry: red chlorophyll catabolite reductase. Now classified as EC 1.3.7.12, red chlorophyll catabolite reductase
[EC 1.3.1.80 created 2007, deleted 2016]
 
 
EC 1.3.7.12     
Accepted name: red chlorophyll catabolite reductase
Reaction: primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster = red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
For diagram of chlorophyll catabolism, click here
Glossary: red chlorophyll catabolite = RCC = (7S,8S,101R)-8-(2-carboxyethyl)-17-ethyl-19-formyl-101-(methoxycarbonyl)-3,7,13,18-tetramethyl-2-vinyl-8,23-dihydro-7H-10,12-ethanobiladiene-ab-1,102(21H)-dione
primary fluorescent chlorophyll catabolite = pFCC = (82R,12S,13S)-12-(2-carboxyethyl)-3-ethyl-1-formyl-82-(methoxycarbonyl)-2,7,13,17-tetramethyl-18-vinyl-12,13-dihydro-8,10-ethanobilene-b-81,19(16H)-dione
Other name(s): RCCR; RCC reductase; red Chl catabolite reductase
Systematic name: primary fluorescent chlorophyll catabolite:ferredoxin oxidoreductase
Comments: The enzyme participates in chlorophyll degradation, which occurs during leaf senescence and fruit ripening in higher plants. The reaction requires reduced ferredoxin, which is generated from NADPH produced either through the pentose-phosphate pathway or by the action of photosystem I [1,2]. This reaction takes place while red chlorophyll catabolite is still bound to EC 1.14.15.17, pheophorbide a oxygenase [3]. Depending on the plant species used as the source of enzyme, one of two possible C-1 epimers of primary fluorescent chlorophyll catabolite (pFCC), pFCC-1 or pFCC-2, is normally formed, with all genera or species within a family producing the same isomer [3,4]. After modification and export, pFCCs are eventually imported into the vacuole, where the acidic environment causes their non-enzymic conversion into colourless breakdown products called non-fluorescent chlorophyll catabolites (NCCs) [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Rodoni, S., Mühlecker, W., Anderl, M., Kräutler, B., Moser, D., Thomas, H., Matile, P. and Hörtensteiner, S. Chlorophyll breakdown in senescent chloroplasts. Cleavage of pheophorbide a in two enzymic steps. Plant Physiol. 115 (1997) 669–676. [PMID: 12223835]
2.  Wüthrich, K.L., Bovet, L., Hunziker, P.E., Donnison, I.S. and Hörtensteiner, S. Molecular cloning, functional expression and characterisation of RCC reductase involved in chlorophyll catabolism. Plant J. 21 (2000) 189–198. [DOI] [PMID: 10743659]
3.  Pružinská, A., Anders, I., Aubry, S., Schenk, N., Tapernoux-Lüthi, E., Müller, T., Kräutler, B. and Hörtensteiner, S. In vivo participation of red chlorophyll catabolite reductase in chlorophyll breakdown. Plant Cell 19 (2007) 369–387. [DOI] [PMID: 17237353]
4.  Hörtensteiner, S. Chlorophyll degradation during senescence. Annu. Rev. Plant Biol. 57 (2006) 55–77. [DOI] [PMID: 16669755]
5.  Rodoni, S., Vicentini, F., Schellenberg, M., Matile, P. and Hörtensteiner, S. Partial purification and characterization of red chlorophyll catabolite reductase, a stroma protein involved in chlorophyll breakdown. Plant Physiol. 115 (1997) 677–682. [PMID: 12223836]
[EC 1.3.7.12 created 2007 as EC 1.3.1.80, transferred 2016 to EC 1.3.7.12]
 
 
EC 1.14.12.20      
Transferred entry: pheophorbide a oxygenase. Now classified as EC 1.14.15.17, pheophorbide a oxygenase.
[EC 1.14.12.20 created 2007, deleted 2016]
 
 
EC 1.14.15.17     
Accepted name: pheophorbide a oxygenase
Reaction: pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster (overall reaction)
(1a) pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = epoxypheophorbide a + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(1b) epoxypheophorbide a + H2O = red chlorophyll catabolite (spontaneous)
For diagram of chlorophyll catabolism, click here
Glossary: red chlorophyll catabolite = RCC = (7S,8S,101R)-8-(2-carboxyethyl)-8,23-dihydro-17-ethyl-19-formyl-101-(methoxycarbonyl)-3,7,13,18-tetramethyl-2-vinyl-7H-10,12-ethanobiladiene-ab-1,102(21H)-dione
Other name(s): pheide a monooxygenase; pheide a oxygenase; PaO; PAO
Systematic name: pheophorbide-a,ferredoxin:oxygen oxidoreductase (biladiene-forming)
Comments: This enzyme catalyses a key reaction in chlorophyll degradation, which occurs during leaf senescence and fruit ripening in higher plants. The enzyme from Arabidopsis contains a Rieske-type iron-sulfur cluster [2] and requires reduced ferredoxin, which is generated either by NADPH through the pentose-phosphate pathway or by the action of photosystem I [4]. While still attached to this enzyme, the product is rapidly converted into primary fluorescent chlorophyll catabolite by the action of EC 1.3.7.12, red chlorophyll catabolite reductase [2,6]. Pheophorbide b acts as an inhibitor. In 18O2 labelling experiments, only the aldehyde oxygen is labelled, suggesting that the other oxygen atom may originate from H2O [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hörtensteiner, S., Wüthrich, K.L., Matile, P., Ongania, K.H. and Kräutler, B. The key step in chlorophyll breakdown in higher plants. Cleavage of pheophorbide a macrocycle by a monooxygenase. J. Biol. Chem. 273 (1998) 15335–15339. [DOI] [PMID: 9624113]
2.  Pružinská, A., Tanner, G., Anders, I., Roca, M. and Hörtensteiner, S. Chlorophyll breakdown: pheophorbide a oxygenase is a Rieske-type iron-sulfur protein, encoded by the accelerated cell death 1 gene. Proc. Natl. Acad. Sci. USA 100 (2003) 15259–15264. [DOI] [PMID: 14657372]
3.  Chung, D.W., Pružinská, A., Hörtensteiner, S. and Ort, D.R. The role of pheophorbide a oxygenase expression and activity in the canola green seed problem. Plant Physiol. 142 (2006) 88–97. [DOI] [PMID: 16844830]
4.  Rodoni, S., Mühlecker, W., Anderl, M., Kräutler, B., Moser, D., Thomas, H., Matile, P. and Hörtensteiner, S. Chlorophyll breakdown in senescent chloroplasts. Cleavage of pheophorbide a in two enzymic steps. Plant Physiol. 115 (1997) 669–676. [PMID: 12223835]
5.  Hörtensteiner, S. Chlorophyll degradation during senescence. Annu. Rev. Plant Biol. 57 (2006) 55–77. [DOI] [PMID: 16669755]
6.  Pružinská, A., Anders, I., Aubry, S., Schenk, N., Tapernoux-Lüthi, E., Müller, T., Kräutler, B. and Hörtensteiner, S. In vivo participation of red chlorophyll catabolite reductase in chlorophyll breakdown. Plant Cell 19 (2007) 369–387. [DOI] [PMID: 17237353]
[EC 1.14.15.17 created 2007 as EC 1.14.12.20, transferred 2016 to EC 1.14.15.17]
 
 


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