Functional and structural characteristics of methylmalonyl-CoA mutase from Pyrococcus horikoshii

Bioscience, Biotechnology and Biochemistry

Volumn 79, Issue 5, 2015, Pages 710-717

  Yabuta, Yukinori ^a   Kamei, Yukiko ^a   Bito, Tomohiro ^a   Arima, Jiro ^a   Yoneda, Kazunari ^b   Sakuraba, Haruhiko ^c   Ohshima, Toshihisa ^d   Nakano, Yoshihisa ^a   Watanabe, Fumio ^a  

^a TOTTORI UNIVERSITY   (Japan)

^b TOKAI UNIVERSITY   (Japan)

^c OSAKA INSTITUTE OF TECHNOLOGY   (Japan)

^d Osaka Women's Junior College   (Japan)

Author keywords

5 deoxyadenosylcobalamin; Archaea; Methylmalonyl coa mutase; Pyrococcus horikoshii; Vitamin b12

Indexed keywords

ENCODING (SYMBOLS); GENES; RECOMBINANT PROTEINS;

5-DEOXYADENOSYLCOBALAMIN; ARCHAEA; METHYLMALONYL-COA MUTASE; PYROCOCCUS HORIKOSHII; VITAMIN B-12;

MICROORGANISMS;

COBAMAMIDE; METHYLMALONYL COENZYME A MUTASE; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; CHEMISTRY; ENZYMOLOGY; GENETICS; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN MULTIMERIZATION; PYROCOCCUS HORIKOSHII; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; CLONING, MOLECULAR; COBAMIDES; ELECTROPHORESIS, POLYACRYLAMIDE GEL; METHYLMALONYL-COA MUTASE; MOLECULAR SEQUENCE DATA; PROTEIN MULTIMERIZATION; PYROCOCCUS HORIKOSHII; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 84942083107     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1080/09168451.2014.993353     Document Type: Article

References (28)

1. Marsh EN, Leadlay PF. Methylmalonyl-CoA mutase from Propionibacterium shermanii. Evidence for the presence of two masked cysteine residues. Biochem. J. 1989;260:339-343.
2. Marsh EN, McKie N, Davis NK, Leadlay PF. Cloning and structural characterization of the genes coding for adenosylcobalamindependent methylmalonyl-CoA mutase from Propionibacterium shermanii. Biochem. J. 1989;260:345-352.
3. Jansen R, Kalousek F, Fenton WA, Rosenberg LE, Ledley FD. Cloning of full-length methylmalonyl-CoA mutase from a cDNA library using the polymerase chain reaction. Genomics. 1989;4:198-205.
4. Kolhouse JF, Utley C, Allen RH. Isolation and characterization of methylmalonyl-CoA mutase from human placenta. J. Biol. Chem. 1980;255:2708-2712.
5. Mancia F, Keep NH, Nakagawa A, Leadlay PF, McSweeney S, Rasmussen B, Bö secke P, Diat O, Evans PR. How coenzyme B12 radicals are generated: The crystal structure of methylmalonylcoenzyme A mutase at 2 å resolution. Structure. 1996;4:339-350.
6. Woese CR, Kandler O, Wheelis ML. Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eucarya. Proc. Nat. Acad. Sci. USA. 1990;87:4576-4579.
7. Han Y, Hawkins AS, Adams MW, Kelly RM. Epimerase (Msed-0639) and mutase (Msed-0638 and Msed-2055) convert (S)-methylmalonyl-coenzyme A (CoA) to succinyl-CoA in the Metallosphaera sedula 3-Hydroxypropionate/4-Hydroxybutyrate Cycle. Appl. Environ. Microbiol. 2012;78:6194-6202.
8. Kawakami R, Sakuraba H, Tsuge H, Goda S, Katunuma N, Ohshima T. A second novel dye-linked L-proline dehydrogenase complex is present in the hyperthermophilic archaeon Pyrococcus horikoshii OT-3. FEBS J. 2005;272:4044-4054.
9. Tanioka Y, Yabuta Y, Miyamoto E, Inui H, Watanabe F. Analysis of vitamin B12 in food by silica gel 60 TLC and bioautography with vitamin B12-dependent Escherichia coli 215. J. Liq. Chromatogr. Related Technol. 2008;31:1977-1985.
10. Gaire D, Sponne I, Droesch S, Charlier A, Nicolas JP, Lambert D. Comparison of two methods for the measurement of rat liver methylmalonyl-coenzyme A mutase activity: HPLC and radioisotopic assays. J. Nutr. Biochem. 1999;10:56-62.
11. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227:680-685.
12. Schägger H, von Jagow G. Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 1991;199:223-231.
13. Yabuta Y, Motoki T, Yoshimura K, Takeda T, Ishikawa T, Shigeoka S. Thylakoid membrane-bound ascorbate peroxidase is a limiting factor of antioxidative systems under photo-oxidative stress. Plant J. 2002;32:915-925.
14. González JM, Masuchi Y, Robb FT, Ammerman JW, Maeder DL, Yanagibayashi M, Tamaoka J, Kato C. Pyrococcus horikoshii sp. nov., a hyperthermophilic archaeon isolated from a hydrothermal vent at the Okinawa Trough. Extremophiles. 1998;2:123-130.
15. Kawarabayasi Y, Sawada M, Horikawa H, Haikawa Y, Hino Y, Yamamoto S, Sekine M, Baba S, Kosugi H, Hosoyama A, Nagai Y, Sakai M, Ogura K, Otsuka R, Nakazawa H, Takamiya M, Ohfuku Y, Funahashi T, Tanaka T, Kudoh Y, Yamazaki J, Kushida N, Oguchi A, Aoki K, Kikuchi H. Complete sequence and gene or ganization of the genome of a hyperthermophilic archaebacterium, Pyrococcus horikoshii OT3. DNA Res. 1998;5:55-76.
16. Hoffmann B, Oberhuber M, Stupperich E, Bothe H, Buckel W, Konrat R, Krautler B. Native corrinoids from Clostridium cochlearium are Adeninylcobamides: spectroscopic analysis and identification of pseudovitamin B12 and factor A. J. Bacteriol. 2000;182:4773-4782.
17. Santos F, Vera JL, Lamosa P, de Valdez G, de Vos WM, Santos H, Sesma F, Hugenholtz J. Pseudovitamin B12 is the corrinoid produced by Lactobacillus reuteri CRL1098 under anaerobic conditions. FEBS Lett. 2007;581:4865-4870.
18. Watanabe F, Yabuta Y, Tanioka Y, Bito T. Biologically active vitamin B12 compounds in foods for preventing deficiency among vegetarians and elderly subjects. J. Agric. Food. Chem. 2013;61:6769-6775.
19. Froese DS, Kochan G, Muniz JR, Wu X, Gileadi C, Ugochukwu E, Krysztofinska E, Gravel RA, Oppermann U, Yue WW. Structures of the human GTPase MMAA and vitamin B12-dependent methylmalonyl-CoA mutase and insight into their complex formation. J. Biol. Chem. 2010;285:38204-38213.
20. Lu WP, Schiau I, Cunningham JR, Ragsdale SW. Sequence and expression of the gene encoding the corrinoid/iron-sulfur protein from Clostridium thermoaceticum and reconstitution of the recombinant protein to full activity. J. Biol. Chem. 1993;268: 5605-5614.
21. Banerjee R, Ragsdale SW. The many faces of vitamin B12: catalysis by cobalamin-dependent enzymes. Annu. Rev. Biochem. 2003;72:209-247.
22. Berg IA, Kockelkorn D, Buckel W, Fuchs G. A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in archaea. Science. 2007;318:1782-1786.
23. McKie N, Keep NH, Patchett ML, Leadlay PF. Adenosylcobalamin- dependent methylmalonyl-CoA mutase from Propionibacterium shermanii. Active holoenzyme produced from Escherichia coli. Biochem. J. 1990;269:293-298.
24. Toraya T, Mori K. A reactivating factor for coenzyme B12-dependent diol dehydratase. J. Biol. Chem. 1999;274: 3372-3377.
25. Kajiura H, Mori K, Tobimatsu T, Toraya T. Characterization and mechanism of action of a reactivating factor for adenosylcobalamin- dependent glycerol dehydratase. J. Biol. Chem. 2001;276: 36514-36519.
26. Fukuoka M, Yamada S, Miyoshi S, Yamashita K, Yamanishi M, Zou X, Brown KL, Toraya T. Functions of the D-ribosyl moiety and the lower axial ligand of the nucleotide loop of coenzyme B12 in diol dehydratase and ethanolamine ammonia-lyase reactions. J. Biochem. 2002;132:935-943.
27. Padovani D, Banerjee R. Assembly and protection of the radical enzyme, methylmalonyl-CoA mutase, by its chaperone. Biochemistry. 2006;45:9300-9306.
28. Takahashi-Íñiguez T, García-Arellano H, Trujillo-Roldán MA, Flores ME. Protection and reactivation of human methylmalonyl- CoA mutase by MMAA protein. Biochem. Biophys. Res. Commun. 2011;404:443-447.