Magnesium-chelatase is a three-component enzyme (EC 6.6.1.1) that catalyses the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of chlorophyll and bacteriochlorophyll.[1][2] As a result, it is thought that Mg-chelatase has an important role in channeling intermediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth:
The four substrates of this enzyme are protoporphyrin IX, magnesium ion, adenosine triphosphate (ATP), and water. Its products are magnesium protoporphyrin IX, adenosine diphosphate (ADP), phosphate (Pi), and two protons.[3][4][5]
This enzyme belongs to the family of ligases, specifically those forming nitrogen-D-metal bonds in coordination complexes. The systematic name of this enzyme class is Mg-protoporphyrin IX magnesium-lyase. Other names in common use include protoporphyrin IX magnesium-chelatase, protoporphyrin IX Mg-chelatase, magnesium-protoporphyrin IX chelatase, magnesium-protoporphyrin chelatase, magnesium-chelatase, Mg-chelatase, and Mg-protoporphyrin IX magnesio-lyase. This enzyme is part of the biosynthetic pathway to chlorophylls.[6]
See also
References
- ^ 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.
- ^ Walker CJ, Weinstein JD (1991). "In vitro assay of the chlorophyll biosynthetic enzyme Mg-chelatase: resolution of the activity into soluble and membrane-bound fractions". Proc. Natl. Acad. Sci. U.S.A. 88 (13): 5789–93. Bibcode:1991PNAS...88.5789W. doi:10.1073/pnas.88.13.5789. PMC 51963. PMID 11607197.
- ^ Walker CJ, Willows RD (Oct 15, 1997). "Mechanism and regulation of Mg-chelatase". Biochem. J. 327 (2): 321–33. doi:10.1042/bj3270321. PMC 1218797. PMID 9359397.
- ^ Al-Karadaghi S; Hansson, A; Hansson, M; Olsen, JG; Gough, S; Willows, RD; Al-Karadaghi, S (2001). "Interplay between an AAA module and an integrin I domain may regulate the function of magnesium chelatase". J. Mol. Biol. 311 (1): 111–22. doi:10.1006/jmbi.2001.4834. PMID 11469861.
- ^ Enzyme 6.6.1.1 at KEGG Pathway Database.
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