Chlorophyllide-a oxygenase: Difference between revisions
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{{Short description|Class of enzymes}} |
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{{Infobox enzyme |
{{Infobox enzyme |
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| Name = Chlorophyllide-a oxygenase |
| Name = Chlorophyllide-a oxygenase |
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| EC_number = 1.13. |
| EC_number = 1.14.13.122 |
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| CAS_number = 216503-73-0 |
| CAS_number = 216503-73-0 |
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| GO_code = |
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| IUBMB_EC_number = 1/13/12/14 |
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| image = |
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'''Chlorophyllide-a oxygenase''' ({{EC number|1.13. |
'''Chlorophyllide-a oxygenase''' ({{EC number|1.14.13.122}}), ''chlorophyllide a oxygenase'', ''chlorophyll-b synthase'', ''CAO'') is an [[enzyme]] with [[List of enzymes|systematic name]] ''chlorophyllide-a:oxygen 7-oxidoreductase''.<ref>{{cite journal | vauthors = Espineda CE, Linford AS, Devine D, Brusslan JA | title = The AtCAO gene, encoding chlorophyll a oxygenase, is required for chlorophyll b synthesis in Arabidopsis thaliana | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 96 | issue = 18 | pages = 10507–11 | date = August 1999 | pmid = 10468639 | pmc = 17919 | doi = 10.1073/pnas.96.18.10507 | bibcode = 1999PNAS...9610507E | doi-access = free }}</ref><ref>{{cite journal | vauthors = Oster U, Tanaka R, Tanaka A, Rüdiger W | title = Cloning and functional expression of the gene encoding the key enzyme for chlorophyll b biosynthesis (CAO) from Arabidopsis thaliana | journal = The Plant Journal | volume = 21 | issue = 3 | pages = 305–10 | date = February 2000 | pmid = 10758481 | doi = 10.1046/j.1365-313x.2000.00672.x | doi-access = free }}</ref><ref>{{cite journal | vauthors = Eggink LL, LoBrutto R, Brune DC, Brusslan J, Yamasato A, Tanaka A, Hoober JK | title = Synthesis of chlorophyll b: localization of chlorophyllide a oxygenase and discovery of a stable radical in the catalytic subunit | journal = BMC Plant Biology | volume = 4 | pages = 5 | date = April 2004 | pmid = 15086960 | pmc = 406501 | doi = 10.1186/1471-2229-4-5 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Porra RJ, Schäfer W, Cmiel E, Katheder I, Scheer H | title = The derivation of the formyl-group oxygen of chlorophyll b in higher plants from molecular oxygen. Achievement of high enrichment of the 7-formyl-group oxygen from 18O2 in greening maize leaves | journal = European Journal of Biochemistry | volume = 219 | issue = 1–2 | pages = 671–9 | date = January 1994 | pmid = 8307032 | doi = 10.1111/j.1432-1033.1994.tb19983.x | url = https://epub.ub.uni-muenchen.de/2482/1/244.pdf | doi-access = free }}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]s |
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: (1) [[chlorophyllide a]] + O<sub>2</sub> + NADPH + H<sup>+</sup> <math>\rightleftharpoons</math> 7-hydroxychlorophyllide a + H<sub>2</sub>O + NADP<sup>+</sup> |
: (1) [[chlorophyllide|chlorophyllide ''a'']] + O<sub>2</sub> + NADPH + H<sup>+</sup> <math>\rightleftharpoons</math> 7-hydroxychlorophyllide a + H<sub>2</sub>O + NADP<sup>+</sup> |
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: (2) 7-hydroxychlorophyllide a + O<sub>2</sub> + NADPH + H<sup>+</sup> <math>\rightleftharpoons</math> [[chlorophyllide b]] + 2 H<sub>2</sub>O + NADP<sup>+</sup> |
: (2) 7-hydroxychlorophyllide a + O<sub>2</sub> + NADPH + H<sup>+</sup> <math>\rightleftharpoons</math> [[chlorophyllide|chlorophyllide ''b'']] + 2 H<sub>2</sub>O + NADP<sup>+</sup> |
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[[File:C-3 position Chlorophyll a.svg|thumb|left|class=skin-invert-image|Chlorophyllide ''a'', (R=H) is converted to chlorophyllide ''b'', in which the [[methyl group]] show in the green box is oxidised to a [[Aldehyde|formyl group]].]] |
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This enzyme contains a mononuclear iron centre. |
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This enzyme contains a mononuclear iron centre and is part of the [[biosynthetic pathway]] to [[chlorophyll]]s.<ref name="Review" >{{cite journal |title=Biosynthesis of chlorophylls from protoporphyrin IX |last =Willows | first =Robert D. | journal =Natural Product Reports | year =2003 | volume = 20 |issue = 6 | pages =327–341 |doi=10.1039/B110549N |pmid=12828371}}</ref><ref>{{cite journal |doi=10.1007/s11120-006-9076-6 |title=Recent advances in chlorophyll biosynthesis |year=2007 |last1=Bollivar |first1=David W. |journal=Photosynthesis Research |volume=90 |issue=2 |pages=173–194 |pmid=17370354 |s2cid=23808539 }}</ref> |
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==See also== |
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* [[Chlorophyllide|Biosynthesis of chlorophylls]] |
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== References == |
== References == |
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* {{MeshName|Chlorophyllide-a+oxygenase}} |
* {{MeshName|Chlorophyllide-a+oxygenase}} |
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{{Dioxygenases}} |
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{{Enzymes}} |
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{{Portal bar|Biology|border=no}} |
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Latest revision as of 22:47, 16 September 2024
Chlorophyllide-a oxygenase | |||||||||
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Identifiers | |||||||||
EC no. | 1.14.13.122 | ||||||||
CAS no. | 216503-73-0 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Chlorophyllide-a oxygenase (EC 1.14.13.122), chlorophyllide a oxygenase, chlorophyll-b synthase, CAO) is an enzyme with systematic name chlorophyllide-a:oxygen 7-oxidoreductase.[1][2][3][4] This enzyme catalyses the following chemical reactions
- (1) chlorophyllide a + O2 + NADPH + H+ 7-hydroxychlorophyllide a + H2O + NADP+
- (2) 7-hydroxychlorophyllide a + O2 + NADPH + H+ chlorophyllide b + 2 H2O + NADP+
This enzyme contains a mononuclear iron centre and is part of the biosynthetic pathway to chlorophylls.[5][6]
See also
[edit]References
[edit]- ^ Espineda CE, Linford AS, Devine D, Brusslan JA (August 1999). "The AtCAO gene, encoding chlorophyll a oxygenase, is required for chlorophyll b synthesis in Arabidopsis thaliana". Proceedings of the National Academy of Sciences of the United States of America. 96 (18): 10507–11. Bibcode:1999PNAS...9610507E. doi:10.1073/pnas.96.18.10507. PMC 17919. PMID 10468639.
- ^ Oster U, Tanaka R, Tanaka A, Rüdiger W (February 2000). "Cloning and functional expression of the gene encoding the key enzyme for chlorophyll b biosynthesis (CAO) from Arabidopsis thaliana". The Plant Journal. 21 (3): 305–10. doi:10.1046/j.1365-313x.2000.00672.x. PMID 10758481.
- ^ Eggink LL, LoBrutto R, Brune DC, Brusslan J, Yamasato A, Tanaka A, Hoober JK (April 2004). "Synthesis of chlorophyll b: localization of chlorophyllide a oxygenase and discovery of a stable radical in the catalytic subunit". BMC Plant Biology. 4: 5. doi:10.1186/1471-2229-4-5. PMC 406501. PMID 15086960.
- ^ Porra RJ, Schäfer W, Cmiel E, Katheder I, Scheer H (January 1994). "The derivation of the formyl-group oxygen of chlorophyll b in higher plants from molecular oxygen. Achievement of high enrichment of the 7-formyl-group oxygen from 18O2 in greening maize leaves" (PDF). European Journal of Biochemistry. 219 (1–2): 671–9. doi:10.1111/j.1432-1033.1994.tb19983.x. PMID 8307032.
- ^ Willows, Robert D. (2003). "Biosynthesis of chlorophylls from protoporphyrin IX". Natural Product Reports. 20 (6): 327–341. doi:10.1039/B110549N. PMID 12828371.
- ^ Bollivar, David W. (2007). "Recent advances in chlorophyll biosynthesis". Photosynthesis Research. 90 (2): 173–194. doi:10.1007/s11120-006-9076-6. PMID 17370354. S2CID 23808539.
External links
[edit]- Chlorophyllide-a+oxygenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)