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2. Adenosylcobalamin-dependent methylmalonyl-CoA mutase from Propionibacterium shermanii. Active holoenzyme produced from Escherichia coli. McKie N; Keep NH; Patchett ML; Leadlay PF Biochem J; 1990 Jul; 269(2):293-8. PubMed ID: 1974759 [TBL] [Abstract][Full Text] [Related]
3. Methylmalonyl-CoA mutase from Propionibacterium shermanii: characterization of the cobalamin-inhibited form and subunit-cofactor interactions studied by analytical ultracentrifugation. Marsh EN; Harding SE Biochem J; 1993 Mar; 290 ( Pt 2)(Pt 2):551-5. PubMed ID: 8095783 [TBL] [Abstract][Full Text] [Related]
4. Interactions of methylmalonyl CoA mutase from normal human fibroblasts with adenosylcobalamin and methylmalonyl CoA: evidence for non-equivalent active sites. Willard HF; Rosenberg LE Arch Biochem Biophys; 1980 Mar; 200(1):130-9. PubMed ID: 6102452 [No Abstract] [Full Text] [Related]
6. The subunit structure of methylmalonyl-CoA mutase from Propionibacterium shermanii. Francalanci F; Davis NK; Fuller JQ; Murfitt D; Leadlay PF Biochem J; 1986 Jun; 236(2):489-94. PubMed ID: 2875711 [TBL] [Abstract][Full Text] [Related]
7. Crystallization and preliminary diffraction data for adenosylcobalamin-dependent methylmalonyl-CoA mutase from Propionibacterium shermanii. Marsh N; Leadlay PF; Evans PR J Mol Biol; 1988 Mar; 200(2):421-2. PubMed ID: 2897473 [TBL] [Abstract][Full Text] [Related]
8. Source of methylmalonyl-coenzyme A for erythromycin synthesis: methylmalonyl-coenzyme A mutase from Streptomyces erythreus. Hunaiti AA; Kolattukudy PE Antimicrob Agents Chemother; 1984 Feb; 25(2):173-8. PubMed ID: 6143534 [TBL] [Abstract][Full Text] [Related]
9. Methylmalonyl-CoA mutase from Propionibacterium shermanii. Evidence for the presence of two masked cysteine residues. Marsh EN; Leadlay PF Biochem J; 1989 Jun; 260(2):339-43. PubMed ID: 2569860 [TBL] [Abstract][Full Text] [Related]
10. Investigation of the mechanism of the methylmalonyl-CoA mutase reaction with the substrate analogue: ethylmalonyl-CoA. Rétey J; Smith EH; Zagalak B Eur J Biochem; 1978 Feb; 83(2):437-51. PubMed ID: 24538 [TBL] [Abstract][Full Text] [Related]
11. Quantitative measurement of the error in the cryptic stereospecificity of methylmalonyl-CoA mutase. Michenfelder M; Hull WE; Rétey J Eur J Biochem; 1987 Nov; 168(3):659-67. PubMed ID: 2889598 [TBL] [Abstract][Full Text] [Related]
12. On the mechanism of action of methylmalonyl-CoA mutase. Change of the steric course on isotope substitution. Wölfle K; Michenfelder M; König A; Hull WE; Rétey J Eur J Biochem; 1986 May; 156(3):545-54. PubMed ID: 2870921 [TBL] [Abstract][Full Text] [Related]
13. Proton transfer in methylmalonyl-CoA epimerase from Propionibacterium shermanii. The reaction of (2R)-methylmalonyl-CoA in tritiated water. Fuller JQ; Leadlay PF Biochem J; 1983 Sep; 213(3):643-50. PubMed ID: 6311170 [TBL] [Abstract][Full Text] [Related]
14. Cloning and structural characterization of the genes coding for adenosylcobalamin-dependent methylmalonyl-CoA mutase from Propionibacterium shermanii. Marsh EN; McKie N; Davis NK; Leadlay PF Biochem J; 1989 Jun; 260(2):345-52. PubMed ID: 2569861 [TBL] [Abstract][Full Text] [Related]
15. The error in the cryptic stereospecificity of methylmalonyl-CoA mutase. The use of carba-(dethia)-coenzyme A substrate analogues gives new insight into the enzyme mechanism. Hull WE; Michenfelder M; Rétey J Eur J Biochem; 1988 Apr; 173(1):191-201. PubMed ID: 2895708 [TBL] [Abstract][Full Text] [Related]
16. Homology modeling of human methylmalonyl-CoA mutase: a structural basis for point mutations causing methylmalonic aciduria. Thomä NH; Leadlay PF Protein Sci; 1996 Sep; 5(9):1922-7. PubMed ID: 8880917 [TBL] [Abstract][Full Text] [Related]
17. Proton transfer in methylmalonyl-CoA epimerase from Propionibacterium shermanii. Studies with specifically tritiated (2R)-methylmalonyl-CoA as substrate. Leadlay PF; Fuller JQ Biochem J; 1983 Sep; 213(3):635-42. PubMed ID: 6311169 [TBL] [Abstract][Full Text] [Related]
19. Reversible cleavage of the cobalt-carbon bond to coenzyme B12 catalysed by methylmalonyl-CoA mutase from Propionibacterium shermanii. The use of coenzyme B12 stereospecifically deuterated in position 5'. Gaudemer A; Zylber J; Zylber N; Baran-Marszac M; Hull WE; Fountoulakis M; König A; Wölfle K; Rétey J Eur J Biochem; 1981 Oct; 119(2):279-85. PubMed ID: 6118267 [TBL] [Abstract][Full Text] [Related]
20. The masked cysteine residues in methylmalonyl-CoA mutase from Propionibacterium shermanii are essential for catalytic activity. Roy I FEBS Lett; 1996 Sep; 394(2):126-8. PubMed ID: 8843148 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]