Literature DB >> 2569862

Subunit interactions in Propionibacterium shermanii methylmalonyl-CoA mutase studied by analytical ultracentrifugation.

E N Marsh1, S E Harding, P F Leadlay.   

Abstract

The effect of increasing ionic strength on adenosylcobalamin-dependent methylmalonyl-CoA mutase from Propionibacterium shermanii was studied by using analytical ultracentrifugation. Both sedimentation-velocity and low-speed sedimentation-equilibration measurements show that the enzyme dissociates progressively into its two dissimilar subunits with increasing ionic strength. Equilibrium between the alpha beta-dimer and the separated subunits is rapidly established under these conditions. Dissociation is accompanied by loss of enzymic activity, but the position of the equilibrium is unaffected by the presence of either substrate or adenosylcobalamin cofactor.

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Year:  1989        PMID： 2569862      PMCID： PMC1138676          DOI： 10.1042/bj2600353

Source DB:  PubMed          Journal:  Biochem J        ISSN： 0264-6021            Impact factor:   3.857


  15 in total

1.  THE GLUTAMATE MUTASE SYSTEM. ASSAYS AND PROPERTIES.

Authors:  H A BARKER; V ROOZE; F SUZUKI; A A IODICE
Journal:  J Biol Chem       Date:  1964-10       Impact factor: 5.157

Review 2.  The mechanism of adenosylcobalamin-dependent reactions.

Authors:  B M Babior; J S Krouwer
Journal:  CRC Crit Rev Biochem       Date:  1979

3.  A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.

Authors:  M M Bradford
Journal:  Anal Biochem       Date:  1976-05-07       Impact factor: 3.365

4.  Studies on methylmalonyl-CoA mutase from Propionibacterium shermanii.

Authors:  B Zagalak; J Rétey
Journal:  Eur J Biochem       Date:  1974-05-15

5.  Propanediol dehydratase system. Role of monovalent cations in binding of vitamin B 12 coenzyme or its analogs to apoenzyme.

Authors:  T Toraya; Y Sugimoto; Y Tamao; S Shimizu; S Fukui
Journal:  Biochemistry       Date:  1971-08-31       Impact factor: 3.162

Review 6.  The determination of molecular weights of biological macromolecules by ultracentrifuge methods.

Authors:  J M Creeth; R H Pain
Journal:  Prog Biophys Mol Biol       Date:  1967       Impact factor: 3.667

7.  Some observations on a new type of point average molecular weight.

Authors:  J M Creeth; S E Harding
Journal:  J Biochem Biophys Methods       Date:  1982-12

8.  Purification and characterization of methylmalonyl-CoA epimerase from Propionibacterium shermanii.

Authors:  P F Leadlay
Journal:  Biochem J       Date:  1981-08-01       Impact factor: 3.857

9.  Proton transfer in methylmalonyl-CoA epimerase from Propionibacterium shermanii. Studies with specifically tritiated (2R)-methylmalonyl-CoA as substrate.

Authors:  P F Leadlay; J Q Fuller
Journal:  Biochem J       Date:  1983-09-01       Impact factor: 3.857

10.  Nicotinic acid metabolism. 8. Tracer studies on the intermediary roles of -methyleneglutarate, methylitaconate, dimethylmaleate, and pyruvate.

Authors:  H Kung; L Tsai; T C Stadtman
Journal:  J Biol Chem       Date:  1971-11       Impact factor: 5.157
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  7 in total

1.  Structures of the human GTPase MMAA and vitamin B12-dependent methylmalonyl-CoA mutase and insight into their complex formation.

Authors:  D Sean Froese; Grazyna Kochan; João R C Muniz; Xuchu Wu; Carina Gileadi; Emelie Ugochukwu; Ewelina Krysztofinska; Roy A Gravel; Udo Oppermann; Wyatt W Yue
Journal:  J Biol Chem       Date:  2010-09-28       Impact factor: 5.157

2.  Adenosylcobalamin-dependent methylmalonyl-CoA mutase from Propionibacterium shermanii. Active holoenzyme produced from Escherichia coli.

Authors:  N McKie; N H Keep; M L Patchett; P F Leadlay
Journal:  Biochem J       Date:  1990-07-15       Impact factor: 3.857

3.  Methylmalonyl-CoA mutase from Propionibacterium shermanii. Evidence for the presence of two masked cysteine residues.

Authors:  E N Marsh; P F Leadlay
Journal:  Biochem J       Date:  1989-06-01       Impact factor: 3.857

4.  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.

Authors:  Yejun Han; Aaron S Hawkins; Michael W W Adams; Robert M Kelly
Journal:  Appl Environ Microbiol       Date:  2012-06-29       Impact factor: 4.792

5.  Sleeping beauty mutase (sbm) is expressed and interacts with ygfd in Escherichia coli.

Authors:  D S Froese; C M Dobson; A P White; X Wu; D Padovani; R Banerjee; T Haller; J A Gerlt; M G Surette; R A Gravel
Journal:  Microbiol Res       Date:  2008-10-23       Impact factor: 5.415

6.  Methylmalonyl-CoA mutase from Propionibacterium shermanii: characterization of the cobalamin-inhibited form and subunit-cofactor interactions studied by analytical ultracentrifugation.

Authors:  E N Marsh; S E Harding
Journal:  Biochem J       Date:  1993-03-01       Impact factor: 3.857

7.  Clustering of mutations in methylmalonyl CoA mutase associated with mut- methylmalonic acidemia.

Authors:  A M Crane; F D Ledley
Journal:  Am J Hum Genet       Date:  1994-07       Impact factor: 11.025
  7 in total

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