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Journal articles on the topic 'Methylmalonyl coenzyme A mutase'

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Author: Grafiati

Published: 10 December 2022

Last updated: 28 January 2023

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1

Vrijbloed, Jan W., Katja Zerbe-Burkhardt, Ananda Ratnatilleke, Andreas Grubelnik-Leiser, and John A. Robinson. "Insertional Inactivation of Methylmalonyl Coenzyme A (CoA) Mutase and Isobutyryl-CoA Mutase Genes in Streptomyces cinnamonensis: Influence on Polyketide Antibiotic Biosynthesis." Journal of Bacteriology 181, no. 18 (September 15, 1999): 5600–5605. http://dx.doi.org/10.1128/jb.181.18.5600-5605.1999.

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ABSTRACT The coenzyme B12-dependent isobutyryl coenzyme A (CoA) mutase (ICM) and methylmalonyl-CoA mutase (MCM) catalyze the isomerization of n-butyryl-CoA to isobutyryl-CoA and of methylmalonyl-CoA to succinyl-CoA, respectively. The influence that both mutases have on the conversion of n- and isobutyryl-CoA to methylmalonyl-CoA and the use of the latter in polyketide biosynthesis have been investigated with the polyether antibiotic (monensin) producer Streptomyces cinnamonensis. Mutants prepared by inserting a hygromycin resistance gene (hygB) into either icmA or mutB, encoding the large subunits of ICM and MCM, respectively, have been characterized. The icmA::hygB mutant was unable to grow on valine or isobutyrate as the sole carbon source but grew normally on butyrate, indicating a key role for ICM in valine and isobutyrate metabolism in minimal medium. ThemutB::hygB mutant was unable to grow on propionate and grew only weakly on butyrate and isobutyrate as sole carbon sources. 13C-labeling experiments show that in both mutants butyrate and acetoacetate may be incorporated into the propionate units in monensin A without cleavage to acetate units. Hence, n-butyryl-CoA may be converted into methylmalonyl-CoA through a carbon skeleton rearrangement for which neither ICM nor MCM alone is essential.

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2

Botella, Laure, Nic D. Lindley, and Lothar Eggeling. "Formation and Metabolism of Methylmalonyl Coenzyme A in Corynebacterium glutamicum." Journal of Bacteriology 191, no. 8 (February 20, 2009): 2899–901. http://dx.doi.org/10.1128/jb.01756-08.

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ABSTRACT Genome sequence information suggests that B12-dependent mutases are present in a number of bacteria, including members of the suborder Corynebacterineae like Mycobacterium tuberculosis and Corynebacterium glutamicum. We here functionally identify a methylmalonyl coenzyme A (CoA) mutase in C. glutamicum that is retained in all of the members of the suborder Corynebacterineae and is encoded by NCgl1471, NCgl1472, and NCgl1470. In addition, we observe the presence of methylmalonate in C. glutamicum, reaching concentrations of up to 757 nmol g (dry weight)−1 in propionate-grown cells, whereas in Escherichia coli no methylmalonate was detectable. As demonstrated with a mutase deletion mutant, the presence of methylmalonate in C. glutamicum is independent of mutase activity but possibly due to propionyl-CoA carboxylase activity. During growth on propionate, increased mutase activity has severe cellular consequences, resulting in growth arrest and excretion of succinate. The physiological context of the mutase present in members of the suborder Corynebacterineae is discussed.

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3

Zhang, Weiwen, and Kevin A. Reynolds. "MeaA, a Putative Coenzyme B12-Dependent Mutase, Provides Methylmalonyl Coenzyme A for Monensin Biosynthesis in Streptomyces cinnamonensis." Journal of Bacteriology 183, no. 6 (March 15, 2001): 2071–80. http://dx.doi.org/10.1128/jb.183.6.2071-2080.2001.

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ABSTRACT The ratio of the major monensin analogs produced byStreptomyces cinnamonensis is dependent upon the relative levels of the biosynthetic precursors methylmalonyl-coenzyme A (CoA) (monensin A and monensin B) and ethylmalonyl-CoA (monensin A). ThemeaA gene of this organism was cloned and sequenced and was shown to encode a putative 74-kDa protein with significant amino acid sequence identity to methylmalonyl-CoA mutase (MCM) (40%) and isobutyryl-CoA mutase (ICM) large subunit (36%) and small subunit (52%) from the same organism. The predicted C terminus of MeaA contains structural features highly conserved in all coenzyme B12-dependent mutases. Plasmid-based expression of meaA from the ermE∗ promoter in the S. cinnamonensis C730.1 strain resulted in a decreased ratio of monensin A to monensin B, from 1:1 to 1:3. Conversely, this ratio increased to 4:1 in a meaA mutant, S. cinnamonensis WM2 (generated from the C730.1 strain by insertional inactivation of meaA by using the erythromycin resistance gene). In both of these experiments, the overall monensin titers were not significantly affected. Monensin titers, however, did decrease over 90% in an S. cinnamonensis WD2 strain (anicm meaA mutant). Monensin titers in the WD2 strain were restored to at least wild-type levels by plasmid-based expression of the meaA gene or the Amycolatopsis mediterranei mutAB genes (encoding MCM). In contrast, growth of the WD2 strain in the presence of 0.8 M valine led only to a partial restoration (<25%) of monensin titers. These results demonstrate that themeaA gene product is significantly involved in methylmalonyl-CoA production in S. cinnamonensis and that under the tested conditions the presence of both MeaA and ICM is crucial for monensin production in the WD2 strain. These results also indicate that valine degradation, implicated in providing methylmalonyl-CoA precursors for many polyketide biosynthetic processes, does not do so to a significant degree for monensin biosynthesis in the WD2 mutant.

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4

Carlucci, Filippo, Francesca Rosi, Valentina Tommassini, and Antonella Tabucchi. "CE assay of methylmalonyl-coenzyme-A mutase activity." ELECTROPHORESIS 28, no. 12 (June 2007): 1921–25. http://dx.doi.org/10.1002/elps.200700031.

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5

Zhao, Yimin, Martina Michenfelder, and János Rétey. "Synthesis, characterization, and enzymic conversion of nonhydrolysable analogues of propionylcoenzyme A." Canadian Journal of Chemistry 72, no. 1 (January 1, 1994): 164–69. http://dx.doi.org/10.1139/v94-025.

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We describe the synthesis of three novel analogues of propionyl-coenzyme A, in which the sulfur atom has been replaced by methylene, ethylene, and thiomethylene, respectively. All three analogues, propionyl-dethia(carba)-CoA (1), propionyl-dethia(dicarba)-CoA (2), and S-(2-oxobutanyl)-CoA (3) were characterized by 1H and 31P NMR spectroscopy and FAB mass spectrometry. Propionyl-CoA–oxaloacetate transcarboxylase from Propionibacterium shermanii accepted the novel analogues as substrates and carboxylated them to the corresponding methylmalonyl-CoA analogues (4–6). The latter were further converted into the succinyl-CoA analogues by the coenzyme-B12-dependent methylmalonyl-CoA mutase from the same organism. The succinyl-CoA analogues, succinyl-dethia(carba)-CoA (7), succinyl-dethia(dicarba)-CoA (8), and 4-carboxy(2-oxobutanyl)-CoA (9) were obtained on a preparative scale and their Michaelis constants (Km) with methylmalonyl-CoA mutase were determined to be 0.136, 2.20, and 0.132 mM, respectively (Km for succinyl-CoA is 0.025 mM). The Vmax values for 7, 8, and 9 are 1.1, 0.013, and 0.0047 µmol min−1 U−1, respectively (Vmax for succinyl CoA is 1.0). The utility of the novel coenzyme A analogues in enzyme mechanistic studies is discussed.

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6

Banerjee, R., and M. Vlasie. "Controlling the reactivity of radical intermediates by coenzyme B12-dependent methylmalonyl-CoA mutase." Biochemical Society Transactions 30, no. 4 (August 1, 2002): 621–24. http://dx.doi.org/10.1042/bst0300621.

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Adenosylcobalamin or coenzyme B12-dependent enzymes are members of the still relatively small group of radical enzymes and catalyse 1,2-rearrangement reactions. A member of this family is methylmalonyl-CoA mutase, which catalyses the isomerization of methylmalonyl-CoA to succinyl-CoA and, unlike the others, is present in both bacteria and animals. Enzymes that catalyse some of the most chemically challenging reactions are the ones that tend to deploy radical chemistry. The use of radical intermediates in an active site lined with amino acid side chains that threaten to extinguish the reaction by presenting alternative groups for abstraction poses the conundrum of how the enzymes control their reactivity. In this review, insights into this issue that have emerged from kinetic, mutagenesis and structural studies are described for methylmalonyl-CoA mutase.

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7

Watanabe, Fumio, Yoshiyuki Tamura, Hisako Saido, and Yoshihisa Nakano. "Enzymatic Assay for Adenosylcobalamin-dependent Methylmalonyl Coenzyme A Mutase." Bioscience, Biotechnology, and Biochemistry 57, no. 9 (January 1993): 1593–94. http://dx.doi.org/10.1271/bbb.57.1593.

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8

Keep, N. H., G. A. Smith, M. C. W. Evans, G. P. Diakun, and P. F. Leadlay. "The synthetic substrate succinyl(carbadethia)-CoA generates cob(II)alamin on adenosylcobalamin-dependent methylmalonyl-CoA mutase." Biochemical Journal 295, no. 2 (October 15, 1993): 387–92. http://dx.doi.org/10.1042/bj2950387.

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Succinyl(carbadethia)-coenzyme A, a synthetic substrate for adenosylcobalamin-dependent methylmalonyl-CoA mutase, has been prepared by a simplified procedure. When recombinant mutase was mixed with the synthetic substrate, the u.v./visible absorption spectrum of the bound cofactor changed rapidly to resemble that of cob(II)alamin, with an absorption maximum at 467 nm. Addition of the natural substrates, in contrast, produced only minor changes in the u.v./visible spectrum. The recent report of the generation of a complex e.p.r. spectrum on addition of substrate to the holo-methylmalonyl-CoA mutase was confirmed with the recombinant enzyme. The signals observed were stronger when the succinyl(carbadethia) analogue was used. Cobalt K-edge X-ray absorption spectroscopy confirmed that the addition of this analogue to holoenzyme leads to the generation of a cob(II)alamin-like species. These results strongly support the generation of cob(II)alamin during the 1,2-skeletal rearrangement catalysed by methylmalonyl-CoA mutase, as required if this enzyme follows the reaction pathway involving radical intermediates previously proposed for other adenosylcobalamin-dependent enzymes.

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9

Riedel, B., P. M. Ueland, and A. M. Svardal. "Fully automated assay for cobalamin-dependent methylmalonyl CoA mutase." Clinical Chemistry 41, no. 8 (August 1, 1995): 1164–70. http://dx.doi.org/10.1093/clinchem/41.8.1164.

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Abstract We constructed a fully automated assay for the cobalamin-dependent enzyme methylmalonyl coenzyme A (CoA) mutase. The assay involves preincubation of the enzyme with adenosylcobalamin, incubation with substrate, termination of the reaction by adding trichloroacetic acid, filtration to remove precipitated protein, and finally analysis of the filtrate (containing methylmalonyl CoA and the product succinyl CoA) by HPLC. These steps were carried out by an inexpensive programmable autosampler equipped with thermostated sample racks and mobile disposable extraction column racks used here as a sample filtering device. A central element in the developmental work was to measure stability of reagents, enzyme, and product against the storage conditions during unattended analysis and the time table of the program. We evaluated the performance of the method by measuring methylmalonyl CoA mutase activity in rat liver, human fibroblasts, and human glioma cells. The within-run imprecisions (CV) were 2-10% for measuring enzyme activity in 20 replicate samples of a homogenate (test of the automated assay), and 7-12% for measuring enzyme activity in homogenates from 20 culture dishes (test of the total procedure). The method allows the unattended analysis of 56 samples per 24 h. This strategy for automation may be easily adapted for other enzyme assays.

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10

Bito, Tomohiro, Mariko Bito, Tomomi Hirooka, Naho Okamoto, Naoki Harada, Ryoichi Yamaji, Yoshihisa Nakano, Hiroshi Inui, and Fumio Watanabe. "Biological Activity of Pseudovitamin B12 on Cobalamin-Dependent Methylmalonyl-CoA Mutase and Methionine Synthase in Mammalian Cultured COS-7 Cells." Molecules 25, no. 14 (July 17, 2020): 3268. http://dx.doi.org/10.3390/molecules25143268.

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Adenyl cobamide (commonly known as pseudovitamin B12) is synthesized by intestinal bacteria or ingested from edible cyanobacteria. The effect of pseudovitamin B12 on the activities of cobalamin-dependent enzymes in mammalian cells has not been studied well. This study was conducted to investigate the effects of pseudovitamin B12 on the activities of the mammalian vitamin B12-dependent enzymes methionine synthase and methylmalonyl-CoA mutase in cultured mammalian COS-7 cells to determine whether pseudovitamin B12 functions as an inhibitor or a cofactor of these enzymes. Although the hydoroxo form of pseudovitamin B12 functions as a coenzyme for methionine synthase in cultured cells, pseudovitamin B12 does not activate the translation of methionine synthase, unlike the hydroxo form of vitamin B12 does. In the second enzymatic reaction, the adenosyl form of pseudovitamin B12 did not function as a coenzyme or an inhibitor of methylmalonyl-CoA mutase. Experiments on the cellular uptake were conducted with human transcobalamin II and suggested that treatment with a substantial amount of pseudovitamin B12 might inhibit transcobalamin II-mediated absorption of a physiological trace concentration of vitamin B12 present in the medium.

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11

Sharar, Sam R., Charles M. Haberkern, Rhona Jack, and C. Ronald Scott. "Anesthetic Management of a Child With Methylmalonyl-Coenzyme A Mutase Deficiency." Anesthesia & Analgesia 73, no. 4 (October 1991): 499???501. http://dx.doi.org/10.1213/00000539-199110000-00025.

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12

Dhansura, Tasneem, Nabila Shaikh, MukhtadirGulam Hashmi, and Chandrakant Shah. "Anaesthetic considerations in a patient with methylmalonyl-coenzyme A mutase deficiency." Indian Journal of Anaesthesia 61, no. 12 (2017): 1018. http://dx.doi.org/10.4103/ija.ija_463_17.

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13

Dai, Siyu, Yanting Yang, Yaqian Li, and Hongqian Liu. "Impaired Function of a Rare Mutation in the MMUT Gene Causes Methylmalonic Acidemia in a Chinese Patient." Genetics Research 2022 (July 22, 2022): 1–6. http://dx.doi.org/10.1155/2022/5611697.

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Methylmalonic acidemia (MMA) is an autosomal recessive metabolic disorder mainly caused by mutations in the methylmalonyl coenzyme A mutase (MCM) gene (MMUT) and leads to the reduced activity of MCM. In this study, a 3-year-old girl was diagnosed with carnitine deficiency secondary to methylmalonic acidemia by tandem mass spectrometry (MS/MS) and gas chromatography/mass spectrometry (GS/MS). Whole-exome sequencing (WES) was performed on the patient and identified two compound heterozygous mutations in MMUT: c.554C>T (p. S185F) and c.729–730insTT (p. D244Lfs ∗ 39). Bioinformatics analysis predicted that the rare missense mutation of c.554C>T would be damaging. Moreover, this rare mutation resulted in the reduced levels of MMUT mRNA and MMUT protein. Collectively, our findings provide a greater understanding of the effects of MMUT variants and will facilitate the diagnosis and treatment of patients with MMA.

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14

Han, Yejun, Aaron S. Hawkins, Michael W. W. Adams, and Robert M. Kelly. "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." Applied and Environmental Microbiology 78, no. 17 (June 29, 2012): 6194–202. http://dx.doi.org/10.1128/aem.01312-12.

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ABSTRACTCrenarchaeotal genomes encode the 3-hydroxypropionate/4-hydroxybutyrate (3-HP/4-HB) cycle for carbon dioxide fixation. Of the 13 enzymes putatively comprising the cycle, several of them, including methylmalonyl-coenzyme A (CoA) epimerase (MCE) and methylmalonyl-CoA mutase (MCM), which convert (S)-methylmalonyl-CoA to succinyl-CoA, have not been confirmed and characterized biochemically. In the genome ofMetallosphaera sedula(optimal temperature [Topt], 73°C), the gene encoding MCE (Msed_0639) is adjacent to that encoding the catalytic subunit of MCM-α (Msed_0638), while the gene for the coenzyme B12-binding subunit of MCM (MCM-β) is located remotely (Msed_2055). The expression of all three genes was significantly upregulated under autotrophic compared to heterotrophic growth conditions, implying a role in CO2fixation. Recombinant forms of MCE and MCM were produced inEscherichia coli; soluble, active MCM was produced only if MCM-α and MCM-β were coexpressed. MCE is a homodimer and MCM is a heterotetramer (α2β2) with specific activities of 218 and 2.2 μmol/min/mg, respectively, at 75°C. The heterotetrameric MCM differs from the homo- or heterodimeric orthologs in other organisms. MCE was activated by divalent cations (Ni2+, Co2+, and Mg2+), and the predicted metal binding/active sites were identified through sequence alignments with less-thermophilic MCEs. The conserved coenzyme B12-binding motif (DXHXXG-SXL-GG) was identified inM. sedulaMCM-β. The two enzymes together catalyzed the two-step conversion of (S)-methylmalonyl-CoA to succinyl-CoA, consistent with their proposed role in the 3-HP/4-HB cycle. Based on the highly conserved occurrence of single copies of MCE and MCM inSulfolobaceaegenomes, theM. sedulaenzymes are likely to be representatives of these enzymes in the 3-HP/4-HB cycle in crenarchaeal thermoacidophiles.

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15

Weichler, Maria-Teresa, Nadya Kurteva-Yaneva, Denise Przybylski, Judith Schuster, Roland H. Müller, Hauke Harms, and Thore Rohwerder. "Thermophilic Coenzyme B12-Dependent Acyl Coenzyme A (CoA) Mutase from Kyrpidia tusciae DSM 2912 Preferentially Catalyzes Isomerization of (R)-3-Hydroxybutyryl-CoA and 2-Hydroxyisobutyryl-CoA." Applied and Environmental Microbiology 81, no. 14 (April 24, 2015): 4564–72. http://dx.doi.org/10.1128/aem.00716-15.

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ABSTRACTThe recent discovery of a coenzyme B12-dependent acyl-coenzyme A (acyl-CoA) mutase isomerizing 3-hydroxybutyryl- and 2-hydroxyisobutyryl-CoA in the mesophilic bacteriumAquincola tertiaricarbonisL108 (N. Yaneva, J. Schuster, F. Schäfer, V. Lede, D. Przybylski, T. Paproth, H. Harms, R. H. Müller, and T. Rohwerder, J Biol Chem 287:15502–15511, 2012,http://dx.doi.org/10.1074/jbc.M111.314690) could pave the way for a complete biosynthesis route to the building block chemical 2-hydroxyisobutyric acid from renewable carbon. However, the enzyme catalyzes only the conversion of the stereoisomer (S)-3-hydroxybutyryl-CoA at reasonable rates, which seriously hampers an efficient combination of mutase and well-established bacterial poly-(R)-3-hydroxybutyrate (PHB) overflow metabolism. Here, we characterize a new 2-hydroxyisobutyryl-CoA mutase found in the thermophilic knallgas bacteriumKyrpidia tusciaeDSM 2912. Reconstituted mutase subunits revealed highest activity at 55°C. Surprisingly, already at 30°C, isomerization of (R)-3-hydroxybutyryl-CoA was about 7,000 times more efficient than with the mutase from strain L108. The most striking structural difference between the two mutases, likely determining stereospecificity, is a replacement of active-site residue Asp found in strain L108 at position 117 with Val in the enzyme from strain DSM 2912, resulting in a reversed polarity at this binding site. Overall sequence comparison indicates that both enzymes descended from different prokaryotic thermophilic methylmalonyl-CoA mutases. Concomitant expression of PHB enzymes delivering (R)-3-hydroxybutyryl-CoA (beta-ketothiolase PhaA and acetoacetyl-CoA reductase PhaB fromCupriavidus necator) with the new mutase inEscherichia coliJM109 and BL21 strains incubated on gluconic acid at 37°C led to the production of 2-hydroxyisobutyric acid at maximal titers of 0.7 mM. Measures to improve production inE. coli, such as coexpression of the chaperone MeaH and repression of thioesterase II, are discussed.

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16

Evans, P. R., and F. Mancia. "How coenzyme B12radicals are generated: methylmalonyl-CoA mutase at 2 Å resolution." Acta Crystallographica Section A Foundations of Crystallography 52, a1 (August 8, 1996): C69. http://dx.doi.org/10.1107/s0108767396096316.

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17

Crane, A. M., R. Jansen, E. R. Andrews, and F. D. Ledley. "Cloning and expression of a mutant methylmalonyl coenzyme A mutase with altered cobalamin affinity that causes mut- methylmalonic aciduria." Journal of Clinical Investigation 89, no. 2 (February 1, 1992): 385–91. http://dx.doi.org/10.1172/jci115597.

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18

Aldor, Ilana S., Seon-Won Kim, Kristala L. Jones Prather, and Jay D. Keasling. "Metabolic Engineering of a Novel Propionate-Independent Pathway for the Production of Poly(3-Hydroxybutyrate-co-3-Hydroxyvalerate) in Recombinant Salmonella enterica Serovar Typhimurium." Applied and Environmental Microbiology 68, no. 8 (August 2002): 3848–54. http://dx.doi.org/10.1128/aem.68.8.3848-3854.2002.

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ABSTRACT A pathway was metabolically engineered to produce poly(3-hydroxybutyrate-co-3-hydroxyvalerate) (PHBV), a biodegradable thermoplastic with proven commercial applications, from a single, unrelated carbon source. An expression system was developed in which a prpC strain of Salmonella enterica serovar Typhimurium, with a mutation in the ability to metabolize propionyl coenzyme A (propionyl-CoA), served as the host for a plasmid harboring the Acinetobacter polyhydroxyalkanoate synthesis operon (phaBCA) and a second plasmid with the Escherichia coli sbm and ygfG genes under an independent promoter. The sbm and ygfG genes encode a novel (2R)-methylmalonyl-CoA mutase and a (2R)-methylmalonyl-CoA decarboxylase, respectively, which convert succinyl-CoA, derived from the tricarboxylic acid cycle, to propionyl-CoA, an essential precursor of 3-hydroxyvalerate (HV). The S. enterica system accumulated PHBV with significant HV incorporation when the organism was grown aerobically with glycerol as the sole carbon source. It was possible to vary the average HV fraction in the copolymer by adjusting the arabinose or cyanocobalamin (precursor of coenzyme B12) concentration in the medium.

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19

González-Montaña, Jose-Ramiro, Francisco Escalera-Valente, Angel J. Alonso, Juan M. Lomillos, Roberto Robles, and Marta E. Alonso. "Relationship between Vitamin B12 and Cobalt Metabolism in Domestic Ruminant: An Update." Animals 10, no. 10 (October 12, 2020): 1855. http://dx.doi.org/10.3390/ani10101855.

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Cobalt, as a trace element, is essential for rumen microorganisms for the formation of vitamin B12. In the metabolism of mammals, vitamin B12 is an essential part of two enzymatic systems involved in multiple metabolic reactions, such as in the metabolism of carbohydrates, lipids, some amino acids and DNA. Adenosylcobalamin and methylcobalamin are coenzymes of methylmalonyl coenzyme A (CoA) mutase and methionine synthetase and are essential for obtaining energy through ruminal metabolism. Signs of cobalt deficiency range from hyporexia, reduced growth and weight loss to liver steatosis, anemia, impaired immune function, impaired reproductive function and even death. Cobalt status in ruminant animals can be assessed by direct measurement of blood or tissue concentrations of cobalt or vitamin B12, as well as the level of methylmalonic acid, homocysteine or transcobalamin in blood; methylmalonic acid in urine; some variables hematological; food consumption or growth of animals. In general, it is assumed that the requirement for cobalt (Co) is expressed around 0.11 ppm (mg/kg) in the dry matter (DM) diet; current recommendations seem to advise increasing Co supplementation and placing it around 0.20 mg Co/kg DM. Although there is no unanimous criterion about milk production, fattening or reproductive rates in response to increased supplementation with Co, in some investigations, when the total Co of the diet was approximately 1 to 1.3 ppm (mg/kg), maximum responses were observed in the milk production.

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20

BermÃºdez, Omaira, Patricia Padilla, Carlos HuitrÃ³n, and MarÄ±Äa Elena Flores. "Influence of carbon and nitrogen source on synthesis of NADP+-isocitrate dehydrogenase, methylmalonyl-coenzyme A mutase, and methylmalonyl-coenzyme A decarboxylase inSaccharopolyspora erythraeaCA340." FEMS Microbiology Letters 164, no. 1 (July 1998): 77–82. http://dx.doi.org/10.1111/j.1574-6968.1998.tb13070.x.

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21

Sun, Fangping, and Tamis Darbre. "The Co(i) induced methylmalonyl-succinyl rearrangement in a model for the coenzyme B12 dependent methylmalonyl-CoA mutase." Organic & Biomolecular Chemistry 1, no. 18 (2003): 3154. http://dx.doi.org/10.1039/b305782h.

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22

VALENCE, FLORENCE, ROMAIN RICHOUX, ANNE THIERRY, AIRI PALVA, and SYLVIE LORTAL. "Autolysis of Lactobacillus helveticus and Propionibacterium freudenreichii in Swiss cheeses: first evidence by using species-specific lysis markers." Journal of Dairy Research 65, no. 4 (November 1998): 609–20. http://dx.doi.org/10.1017/s0022029998003021.

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Lactobacillus helveticus and Propionibacterium freudenreichii are essential starters in Swiss cheesemaking and the release of their intracellular enzymes through autolysis could significantly influence ripening. To provide evidence of this lysis, cheese made from microfiltered thermized milk inoculated with Lb. helveticus ITGLH77, Prop. freudenreichii ITGP23 and a commercial Streptococcus thermophilus was assayed. Starter viability was determined and lysis was monitored during ripening by protein analysis with SDS-PAGE of aqueous cheese extracts and by immunoblot detection of intracellular proteins: dipeptidase (PepD) for Lb. helveticus and methylmalonyl coenzyme A mutase for Prop. freudenreichii. We verified that the species specificity of these lysis markers was towards the cytoplasms of all the species currently used in Swiss cheese. Lb. helveticus exhibited an almost complete loss of viability (99·9%) from the beginning of ripening in the cold room; concomitantly PepD appeared in the cheese extracts and was detected until the end of ripening. Damaged Lb. helveticus cells were also visualized by scanning electron microscopy. In addition, free PepD was also successfully detected in commercial Swiss-related cheeses. All these results clearly demonstrated the autolysis of Lb. helveticus in Swiss cheese. Prop. freudenreichii ITGP23 grew during warm room ripening and no loss of viability was detected after maximal growth (109 cfu/g cheese). Free methylmalonyl-coenzyme A mutase was detected at the end of ripening during cold storage, when the cheese extracts were concentrated 20-fold, demonstrating that the autolysis of Prop. freudenreichii was tardy and limited.

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23

Ruetz, Markus, Gregory C. Campanello, Meredith Purchal, Hongying Shen, Liam McDevitt, Harsha Gouda, Shoko Wakabayashi, et al. "Itaconyl-CoA forms a stable biradical in methylmalonyl-CoA mutase and derails its activity and repair." Science 366, no. 6465 (October 31, 2019): 589–93. http://dx.doi.org/10.1126/science.aay0934.

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Itaconate is an immunometabolite with both anti-inflammatory and bactericidal effects. Its coenzyme A (CoA) derivative, itaconyl-CoA, inhibits B12-dependent methylmalonyl-CoA mutase (MCM) by an unknown mechanism. We demonstrate that itaconyl-CoA is a suicide inactivator of human and Mycobacterium tuberculosis MCM, which forms a markedly air-stable biradical adduct with the 5′-deoxyadenosyl moiety of the B12 coenzyme. Termination of the catalytic cycle in this way impairs communication between MCM and its auxiliary repair proteins. Crystallography and spectroscopy of the inhibited enzyme are consistent with a metal-centered cobalt radical ~6 angstroms away from the tertiary carbon-centered radical and suggest a means of controlling radical trajectories during MCM catalysis. Mycobacterial MCM thus joins enzymes in the glyoxylate shunt and the methylcitrate cycle as targets of itaconate in pathogen propionate metabolism.

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24

Padmakumar, Rugmini, Shinichi Taoka, Raghavaikamal Padmakumar, and Ruma Banerjee. "Coenzyme B12 Is Coordinated by Histidine and Not Dimethylbenzimidazole on Methylmalonyl-CoA Mutase." Journal of the American Chemical Society 117, no. 26 (July 1995): 7033–34. http://dx.doi.org/10.1021/ja00131a039.

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25

Paizs, Csaba, Tanja Diemer, and János Rétey. "The putative coenzyme B12-dependent methylmalonyl-CoA mutase from potatoes is a phosphatase." Bioorganic Chemistry 36, no. 6 (December 2008): 261–64. http://dx.doi.org/10.1016/j.bioorg.2008.06.002.

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26

Bermúdez, O. "Influence of carbon and nitrogen source on synthesis of NADP+-isocitrate dehydrogenase, methylmalonyl-coenzyme A mutase, and methylmalonyl-coenzyme A decarboxylase in Saccharopolyspora erythraea CA340." FEMS Microbiology Letters 164, no. 1 (July 1, 1998): 77–82. http://dx.doi.org/10.1016/s0378-1097(98)00198-0.

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27

Mancia, Filippo, Nicholas H. Keep, Atsushi Nakagawa, Peter F. Leadlay, Sean McSweeney, Bjarne Rasmussen, Peter Bö secke, Olivier Diat, and Philip R. Evans. "How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 å resolution." Structure 4, no. 3 (March 1996): 339–50. http://dx.doi.org/10.1016/s0969-2126(96)00037-8.

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28

Savvi, Suzana, Digby F. Warner, Bavesh D. Kana, John D. McKinney, Valerie Mizrahi, and Stephanie S. Dawes. "Functional Characterization of a Vitamin B12-Dependent Methylmalonyl Pathway in Mycobacterium tuberculosis: Implications for Propionate Metabolism during Growth on Fatty Acids." Journal of Bacteriology 190, no. 11 (March 28, 2008): 3886–95. http://dx.doi.org/10.1128/jb.01767-07.

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ABSTRACT Mycobacterium tuberculosis is predicted to subsist on alternative carbon sources during persistence within the human host. Catabolism of odd- and branched-chain fatty acids, branched-chain amino acids, and cholesterol generates propionyl-coenzyme A (CoA) as a terminal, three-carbon (C3) product. Propionate constitutes a key precursor in lipid biosynthesis but is toxic if accumulated, potentially implicating its metabolism in M. tuberculosis pathogenesis. In addition to the well-characterized methylcitrate cycle, the M. tuberculosis genome contains a complete methylmalonyl pathway, including a mutAB-encoded methylmalonyl-CoA mutase (MCM) that requires a vitamin B12-derived cofactor for activity. Here, we demonstrate the ability of M. tuberculosis to utilize propionate as the sole carbon source in the absence of a functional methylcitrate cycle, provided that vitamin B12 is supplied exogenously. We show that this ability is dependent on mutAB and, furthermore, that an active methylmalonyl pathway allows the bypass of the glyoxylate cycle during growth on propionate in vitro. Importantly, although the glyoxylate and methylcitrate cycles supported robust growth of M. tuberculosis on the C17 fatty acid heptadecanoate, growth on valerate (C5) was significantly enhanced through vitamin B12 supplementation. Moreover, both wild-type and methylcitrate cycle mutant strains grew on B12-supplemented valerate in the presence of 3-nitropropionate, an inhibitor of the glyoxylate cycle enzyme isocitrate lyase, indicating an anaplerotic role for the methylmalonyl pathway. The demonstrated functionality of MCM reinforces the potential relevance of vitamin B12 to mycobacterial pathogenesis and suggests that vitamin B12 availability in vivo might resolve the paradoxical dispensability of the methylcitrate cycle for the growth and persistence of M. tuberculosis in mice.

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29

Scheuring, Eva, Rugmini Padmakumar, Ruma Banerjee, and Mark R. Chance. "Extended X-ray Absorption Fine Structure Analysis of Coenzyme B12Bound to Methylmalonyl-Coenzyme A Mutase Using Global Mapping Techniques†." Journal of the American Chemical Society 119, no. 50 (December 1997): 12192–200. http://dx.doi.org/10.1021/ja9635239.

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30

Vlasie, Monica, Shantanu Chowdhury, and Ruma Banerjee. "Importance of the Histidine Ligand to Coenzyme B12in the Reaction Catalyzed by Methylmalonyl-CoA Mutase." Journal of Biological Chemistry 277, no. 21 (March 13, 2002): 18523–27. http://dx.doi.org/10.1074/jbc.m111809200.

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31

Birch, A., A. Leiser, and J. A. Robinson. "Cloning, sequencing, and expression of the gene encoding methylmalonyl-coenzyme A mutase from Streptomyces cinnamonensis." Journal of Bacteriology 175, no. 11 (1993): 3511–19. http://dx.doi.org/10.1128/jb.175.11.3511-3519.1993.

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32

Zhao, Ymin, Peter Such, and János Rétey. "Radical Intermediates in the Coenzyme B12 Dependent Methylmalonyl-CoA Mutase Reaction Shown by ESR Spectroscopy." Angewandte Chemie International Edition in English 31, no. 2 (February 1992): 215–16. http://dx.doi.org/10.1002/anie.199202151.

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33

Aliarabi, H., S. Bisheh Sari, M. M. Tabatabaei, A. Ahmadi, P. Zamani, D. Alipour, and Z. Zamani. "Effect of cobalt supplementation on performance of Mehraban lambs." Proceedings of the British Society of Animal Science 2009 (April 2009): 167. http://dx.doi.org/10.1017/s1752756200030064.

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A major physiological effect of cobalt deficiency is loss of appetite (Smith, 1997). Rumen micro-organisms require cobalt for the synthesis of Vitamin B12, which acts as a cofactor for protein and energy metabolism enzymes, namely methylmalonyl coenzyme A mutase and methionine synthase (Kennedy et, al. 1992). Cobalt deficiency, therefore, impairs the energy and protein metabolism and thus growth and development of the deficient animal, which can be defined as changes in the weight, shape and size of the body. Sheep tend to be extremely susceptible to Co deficiency and develop a normocytic and normochromic anaemia, anorexia, reduced weight gains and photosensitivity (Vellema et al., 1996). The present study was designed to evaluate the effects of dietary Co level on performance of Mehraban male lambs.

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34

Kumar, Neeraj, Shubin Liu, and Pawel M. Kozlowski. "Charge Separation Propensity of the Coenzyme B12–Tyrosine Complex in Adenosylcobalamin-Dependent Methylmalonyl–CoA Mutase Enzyme." Journal of Physical Chemistry Letters 3, no. 8 (April 9, 2012): 1035–38. http://dx.doi.org/10.1021/jz300102s.

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35

Yamanishi, Mamoru, Tetyana Labunska, and Ruma Banerjee. "Mirror “Base-off” Conformation of Coenzyme B12in Human Adenosyltransferase and Its Downstream Target, Methylmalonyl-CoA Mutase." Journal of the American Chemical Society 127, no. 2 (January 2005): 526–27. http://dx.doi.org/10.1021/ja044365l.

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36

Chowdhury, Shantanu, and Ruma Banerjee. "Role of the Dimethylbenzimidazole Tail in the Reaction Catalyzed by Coenzyme B12-Dependent Methylmalonyl-CoA Mutase†." Biochemistry 38, no. 46 (November 1999): 15287–94. http://dx.doi.org/10.1021/bi9914762.

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37

Korotkova, Natalia, Ludmila Chistoserdova, Vladimir Kuksa, and Mary E. Lidstrom. "Glyoxylate Regeneration Pathway in the Methylotroph Methylobacterium extorquens AM1." Journal of Bacteriology 184, no. 6 (March 15, 2002): 1750–58. http://dx.doi.org/10.1128/jb.184.6.1750-1758.2002.

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ABSTRACT Most serine cycle methylotrophic bacteria lack isocitrate lyase and convert acetyl coenzyme A (acetyl-CoA) to glyoxylate via a novel pathway thought to involve butyryl-CoA and propionyl-CoA as intermediates. In this study we have used a genome analysis approach followed by mutation to test a number of genes for involvement in this novel pathway. We show that methylmalonyl-CoA mutase, an R-specific crotonase, isobutyryl-CoA dehydrogenase, and a GTPase are involved in glyoxylate regeneration. We also monitored the fate of 14C-labeled carbon originating from acetate, butyrate, or bicarbonate in mutants defective in glyoxylate regeneration and identified new potential intermediates in the pathway: ethylmalonyl-CoA, methylsuccinyl-CoA, isobutyryl-CoA, methacrylyl-CoA, and β-hydroxyisobutyryl-CoA. A new scheme for the pathway is proposed based on these data.

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38

Cordes, Thekla, and Christian M. Metallo. "Itaconate Alters Succinate and Coenzyme A Metabolism via Inhibition of Mitochondrial Complex II and Methylmalonyl-CoA Mutase." Metabolites 11, no. 2 (February 18, 2021): 117. http://dx.doi.org/10.3390/metabo11020117.

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Itaconate is a small molecule metabolite that is endogenously produced by cis-aconitate decarboxylase-1 (ACOD1) in mammalian cells and influences numerous cellular processes. The metabolic consequences of itaconate in cells are diverse and contribute to its regulatory function. Here, we have applied isotope tracing and mass spectrometry approaches to explore how itaconate impacts various metabolic pathways in cultured cells. Itaconate is a competitive and reversible inhibitor of Complex II/succinate dehydrogenase (SDH) that alters tricarboxylic acid (TCA) cycle metabolism leading to succinate accumulation. Upon activation with coenzyme A (CoA), itaconyl-CoA inhibits adenosylcobalamin-mediated methylmalonyl-CoA (MUT) activity and, thus, indirectly impacts branched-chain amino acid (BCAA) metabolism and fatty acid diversity. Itaconate, therefore, alters the balance of CoA species in mitochondria through its impacts on TCA, amino acid, vitamin B12, and CoA metabolism. Our results highlight the diverse metabolic pathways regulated by itaconate and provide a roadmap to link these metabolites to potential downstream biological functions.

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39

Gotoh, Kana, Yoko Nakajima, Go Tajima, Yuji Hotta, Tomoya Kataoka, Yoshihiro Kawade, Naruji Sugiyama, Tetsuya Ito, Kazunori Kimura, and Yasuhiro Maeda. "Assay for methylmalonyl coenzyme A mutase activity based on determination of succinyl coenzyme A by ultrahigh-performance liquid chromatography tandem mass spectrometry." Analytical and Bioanalytical Chemistry 407, no. 18 (May 28, 2015): 5281–86. http://dx.doi.org/10.1007/s00216-015-8753-8.

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40

Michenfelder, Martina, and János Rétey. "Methylmalonylcarba(dethia)-Coenzyme A as Substrate of the Coenzyme B12-Dependent Methylmalonyl-CoA Mutase: Enzymatic Rearrangement of aβ- to aγ-Keto Acid." Angewandte Chemie International Edition in English 25, no. 4 (April 1986): 366–67. http://dx.doi.org/10.1002/anie.198603661.

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41

Dong, Shoulian, Raghavakaimal Padmakumar, Ruma Banerjee, and Thomas G. Spiro. "Co−C Bond Activation in B12-Dependent Enzymes: Cryogenic Resonance Raman Studies of Methylmalonyl-Coenzyme A Mutase." Journal of the American Chemical Society 121, no. 30 (August 1999): 7063–70. http://dx.doi.org/10.1021/ja982753f.

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42

Smith, David M., Bernard T. Golding, and Leo Radom. "Facilitation of Enzyme-Catalyzed Reactions by Partial Proton Transfer: Application to Coenzyme-B12-Dependent Methylmalonyl-CoA Mutase." Journal of the American Chemical Society 121, no. 6 (February 1999): 1383–84. http://dx.doi.org/10.1021/ja983512a.

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43

Chowdhury, Shantanu, and Ruma Banerjee. "Thermodynamic and Kinetic Characterization of Co−C Bond Homolysis Catalyzed by Coenzyme B12-Dependent Methylmalonyl-CoA Mutase†." Biochemistry 39, no. 27 (July 2000): 7998–8006. http://dx.doi.org/10.1021/bi992535e.

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44

Harrington, Dominic J. "Laboratory assessment of vitamin B12 status." Journal of Clinical Pathology 70, no. 2 (May 11, 2016): 168–73. http://dx.doi.org/10.1136/jclinpath-2015-203502.

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The detection and correction of vitamin B12 (B12) deficiency prevents megaloblastic anaemia and potentially irreversible neuropathy and neuropsychiatric changes. B12 status is commonly estimated using the abundance of the vitamin in serum, with ∼148 pmol/L (200 ng/L) typically set as the threshold for diagnosing deficiency. Serum B12 assays measure the sum of haptocorrin-bound and transcobalamin-bound (known as holotranscobalamin) B12. It is only holotranscobalamin that is taken up by cells to meet metabolic demand. Although receiver operator characteristic curves show holotranscobalamin measurement to be a moderately more reliable marker of B12 status than serum B12, both assays have an indeterminate range. Biochemical evidence of metabolic abnormalities consistent with B12 insufficiency is frequently detected despite an apparently sufficient abundance of the vitamin. Laboratory B12 status markers that reflect cellular utilisation rather than abundance are available. Two forms of B12 act as coenzymes for two different reactions. Methionine synthase requires methylcobalamin for the remethylation of methionine from homocysteine. A homocysteine concentration >20 µmol/L may suggest B12 deficiency in folate-replete patients. In the second B12-dependent reaction, methylmalonyl-CoA mutase uses adenosylcobalamin to convert methylmalonyl-CoA to succinyl-CoA. In B12 deficiency excess methylmalonyl-CoA is hydrolysed to methylmalonic acid. A serum concentration >280 nmol/L may suggest suboptimal status in young patients with normal renal function. No single laboratory marker is suitable for the assessment of B12 status in all patients. Sequential assay selection algorithms or the combination of multiple markers into a single diagnostic indicator are both approaches that can be used to mitigate inherent limitations of each marker when used independently.

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45

Ghosh, Arghya Pratim, Megan J. Toda, and Pawel M. Kozlowski. "What Triggers the Cleavage of the Co–C5′ Bond in Coenzyme B12-Dependent Itaconyl-CoA Methylmalonyl-CoA Mutase?" ACS Catalysis 11, no. 13 (June 16, 2021): 7943–55. http://dx.doi.org/10.1021/acscatal.1c00291.

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46

Maiti, Nilesh, Lusiana Widjaja, and Ruma Banerjee. "Proton Transfer from Histidine 244 May Facilitate the 1,2 Rearrangement Reaction in Coenzyme B12-dependent Methylmalonyl-CoA Mutase." Journal of Biological Chemistry 274, no. 46 (November 12, 1999): 32733–37. http://dx.doi.org/10.1074/jbc.274.46.32733.

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47

Gaire, D. "Comparison of two methods for the measurement of rat liver methylmalonyl-coenzyme A mutase activity: HPLC and radioisotopic assays." Journal of Nutritional Biochemistry 10, no. 1 (January 1999): 56–62. http://dx.doi.org/10.1016/s0955-2863(98)00083-7.

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48

Chowdhury, Shantanu, Michael G. Thomas, Jorge C. Escalante-Semerena, and Ruma Banerjee. "The Coenzyme B12Analog 5′-Deoxyadenosylcobinamide-GDP Supports Catalysis by Methylmalonyl-CoA Mutase in the Absence of Trans-ligand Coordination." Journal of Biological Chemistry 276, no. 2 (October 12, 2000): 1015–19. http://dx.doi.org/10.1074/jbc.m006842200.

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49

Dong, Shoulian, Raghavakaimal Padmakumar, Nilesh Maiti, Ruma Banerjee, and Thomas G. Spiro. "Resonance Raman Spectra Show That Coenzyme B12Binding to Methylmalonyl-Coenzyme A Mutase Changes the Corrin Ring Conformation but Leaves the Co−C Bond Essentially Unaffected." Journal of the American Chemical Society 120, no. 38 (September 1998): 9947–48. http://dx.doi.org/10.1021/ja981584w.

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50

Michenfelder, Martina, and János Rétey. "Methylmalonyl-cara(dethia)-Coenzym-A als Substrat der Coenzym-B,12-abhängigen Methylmalonyl-CoA-Mutase: Enzymatische Umlagerung einer β- zu einer γ-Ketosäure." Angewandte Chemie 98, no. 4 (April 1986): 337–38. http://dx.doi.org/10.1002/ange.19860980408.

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