Functional and structural characteristics of methylmalonyl-CoA mutase from Pyrococcus horikoshii. Issue 5 (4th May 2015)

• Record Type: Journal Article
• Authors: Yabuta, Yukinori; Kamei, Yukiko; Bito, Tomohiro; Arima, Jiro; Yoneda, Kazunari; Sakuraba, Haruhiko; Ohshima, Toshihisa; Nakano, Yoshihisa; Watanabe, Fumio
• Is Part Of: Bioscience, biotechnology, and biochemistry. Volume 79:Issue 5(2015)
• Page Start: 710
• Page End: 717
• Publication Date: 2015-05-04
• Subjects: archaea -- 5′-deoxyadenosylcobalamin -- methylmalonyl-CoA mutase -- vitamin B12 -- Pyrococcus horikoshii; Biotechnology -- Periodicals; Biochemistry -- Periodicals; 660.6
• DOI: 10.1080/09168451.2014.993353
• Languages: English
• ISSNs: 0916-8451

Abstract

Abstract: Methylmalonyl-CoA mutase (MCM) requires 5′-deoxyadenosylcobalamin (AdoCbl) as a cofactor and is widely distributed in organisms from bacteria and animals. Although genes encoding putative MCMs are present in many archaea, they are separately encoded in large and small subunits. The large and small subunits of archaeal MCM are similar to the catalytic and AdoCbl-binding domains of human MCM, respectively. In Pyrococcus horikoshii OT3, putative genes PH1306 and PH0275 encode the large and small subunits, respectively. Because information on archaeal MCM is extremely restricted, we examined the functional and structural characteristics of P. horikoshii MCM . Reconstitution experiments using recombinant PH0275 and PH1306 showed that these proteins assemble in equimolar ratios and form of heterotetrameric complexes in the presence of AdoCbl. Subsequent immunoprecipitation experiments using anti-PH0275 and anti-PH1306 antibodies suggested that PH0275 and PH1306 form a complex in P. horikoshii cells in the presence of AdoCbl. Abstract: : The large (PH1306) and small (PH0275) subunits of Pyrococcus horikoshii methylmalonyl-CoA mutase form a heterotetrameric complex in the presence of AdoCbl.