Magnesium chelatase
magnesium chelatase | |||||||||
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Identifiers | |||||||||
EC number | 6.6.1.1 | ||||||||
CAS number | 9074-88-8 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / EGO | ||||||||
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Magnesium chelatase, ChlI subunit | |||||||||
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Identifiers | |||||||||
Symbol | Mg_chelatse_chII | ||||||||
Pfam | PF01078 | ||||||||
InterPro | IPR000523 | ||||||||
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CobN/magnesium chelatase | |||||||||
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Identifiers | |||||||||
Symbol | CobN/Mg_chltase | ||||||||
Pfam | PF02514 | ||||||||
InterPro | IPR003672 | ||||||||
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Magnesium-chelatase is a three-component enzyme that catalyses the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of bacteriochlorophyll. 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:
+ ATP + H
2O ADP + phosphate + Mg-protoporphyrin IX + 2 H+
The 4 substrates of this enzyme are ATP, protoporphyrin IX, Mg2+, and H2O, whereas its 4 products are ADP, phosphate, Mg-protoporphyrin IX, and H+.
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 participates in porphyrin and chlorophyll metabolism.
References
- 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. 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.