[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/cobalt-chelatase-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/cobalt-chelatase-wikipedia\/","headline":"Cobalt chelatase – Wikipedia","name":"Cobalt chelatase – Wikipedia","description":"From Wikipedia, the free encyclopedia Enzyme Cobalt chelatase (EC 6.6.1.2) is an enzyme that catalyzes the chemical reaction ATP +","datePublished":"2019-11-05","dateModified":"2019-11-05","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/wikimedia.org\/api\/rest_v1\/media\/math\/render\/svg\/1c37b981df851b9e54e489e017b1481e37d418f3","url":"https:\/\/wikimedia.org\/api\/rest_v1\/media\/math\/render\/svg\/1c37b981df851b9e54e489e017b1481e37d418f3","height":"","width":""},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/cobalt-chelatase-wikipedia\/","wordCount":2613,"articleBody":"From Wikipedia, the free encyclopediaEnzymeCobalt chelatase (EC 6.6.1.2) is an enzyme that catalyzes the chemical reactionATP + hydrogenobyrinic acid a,c-diamide + Co2+ + H2O \u21cc{displaystyle rightleftharpoons } ADP + phosphate + cob(II)yrinic acid a,c-diamide + H+The four substrates of this enzyme are ATP, hydrogenobyrinic acid a,c-diamide, Co2+, and H2O; its four products are ADP, phosphate, cob(II)yrinic acid a,c-diamide, and H+.The aerobic cobalt chelatase (aerobic cobalamin biosynthesis pathway)[2][3] consists of three subunits, CobT, CobN (InterPro:\u00a0IPR003672) and CobS (InterPro:\u00a0IPR006537).The macrocycle of vitamin B12 can be complexed with metal via the ATP-dependent reactions in the aerobic pathway (e.g., in Pseudomonas denitrificans) or via ATP-independent reactions of sirohydrochlorin in the anaerobic pathway (e.g., in Salmonella typhimurium).[4][5] The corresponding cobalt chelatases are not homologous. However, aerobic cobalt chelatase subunits CobN and CobS are homologous to Mg-chelatase subunits BchH and BchI, respectively.[5] CobT, too, has been found to be remotely related to the third subunit of Mg-chelatase, BchD (involved in bacteriochlorophyll synthesis, e.g., in Rhodobacter capsulatus).[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 hydrogenobyrinic-acid-a,c-diamide:cobalt cobalt-ligase (ADP-forming). Other names in common use include hydrogenobyrinic acid a,c-diamide cobaltochelatase, CobNST, and CobNCobST. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in aerobic bacteria.See also[edit]References[edit]^ Rom\u00e3o, C\u00e9lia V.; Ladakis, Dimitrios; Lobo, Susana A. L.; Carrondo, Maria A.; Brindley, Amanda A.; Deery, Evelyne; Matias, Pedro M.; Pickersgill, Richard W.; Saraiva, L\u00edgia M.; Warren, Martin J. (4 January 2011). “Evolution in a family of chelatases facilitated by the introduction of active site asymmetry and protein oligomerization”. Proceedings of the National Academy of Sciences. 108 (1): 97\u2013102. doi:10.1073\/pnas.1014298108. PMC\u00a03017170. PMID\u00a021173279.^ Crouzet J, Cameron B, Cauchois L, Rigault S, Blanche F, Guilhot C, Levy-schil S, Rouyez MC (1991). “Genetic and sequence analyses of a Pseudomonas denitrificans DNA fragment containing two cob genes”. J. Bacteriol. 173 (19): 6058\u20136065. doi:10.1128\/jb.173.19.6058-6065.1991. PMC\u00a0208352. PMID\u00a01917840.^ Crouzet J, Cameron B, Blanche F, Thibaut D, Debussche L, Couder M (1992). “Assay, purification, and characterization of cobaltochelatase, a unique complex enzyme catalyzing cobalt insertion in hydrogenobyrinic acid a,c-diamide during coenzyme B12 biosynthesis in Pseudomonas denitrificans”. J. Bacteriol. 174 (22): 7445\u20137451. doi:10.1128\/jb.174.22.7445-7451.1992. PMC\u00a0207441. PMID\u00a01429466.^ Roth JR, Lawrence JG, Bobik TA (1996). “Cobalamin (coenzyme B12): synthesis and biological significance” (PDF). Annu. Rev. Microbiol. 50: 137\u2013181. doi:10.1146\/annurev.micro.50.1.137. PMID\u00a08905078. S2CID\u00a036290299. Archived from the original (PDF) on 2019-03-07.^ a b c Willows RD, Al-Karadaghi S, Hansson M, Fodje MN, Hansson A, Olsen JG, Gough 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\u2013122. doi:10.1006\/jmbi.2001.4834. PMID\u00a011469861.Further reading[edit]Debussche L, Couder M, Thibaut D, Cameron B, Crouzet J, Blanche F (1992). “Assay, purification, and characterization of cobaltochelatase, a unique complex enzyme catalyzing cobalt insertion in hydrogenobyrinic acid a,c-diamide during coenzyme B12 biosynthesis in Pseudomonas denitrificans”. J. Bacteriol. 174 (22): 7445\u201351. doi:10.1128\/JB.174.22.7445-7451.1992. PMC\u00a0207441. PMID\u00a01429466.Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC (2002). “The biosynthesis of adenosylcobalamin (vitamin B12)”. Nat. Prod. Rep. 19 (4): 390\u2013412. doi:10.1039\/b108967f. PMID\u00a012195810.  "},{"@context":"http:\/\/schema.org\/","@type":"BreadcrumbList","itemListElement":[{"@type":"ListItem","position":1,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/#breadcrumbitem","name":"Enzyklop\u00e4die"}},{"@type":"ListItem","position":2,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/cobalt-chelatase-wikipedia\/#breadcrumbitem","name":"Cobalt chelatase – Wikipedia"}}]}]