Relevant bibliographies by topics / Methylmalonyl coenzyme A mutase

Academic literature on the topic 'Methylmalonyl coenzyme A mutase'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Contents

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Methylmalonyl coenzyme A mutase.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Methylmalonyl coenzyme A mutase"

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.

Full text
Abstract:
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.
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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.
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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.
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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.
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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.
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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.
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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.
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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.
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "Methylmalonyl coenzyme A mutase"

1

Roy, Ipsita. "Studies on methylmalonyl-CoA mutase." Thesis, University of Cambridge, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.240978.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Farah, Rita S. "Intragenic complementation in methylmalonyl CoA mutase." Thesis, McGill University, 1994. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=55444.

Full text
Abstract:
Methylmalonic aciduria (MMA) is an autosomal recessive metabolic disorder with an incidence of 1 in 48,000, which may be due to a defect in the mitochondrial homodimeric enzyme methylmalonyl CoA mutase (mut MMA). mut MMA is subdivided into $mut sp circ$ and $mut sp-$ subclasses on the basis of complementation analysis; $mut sp circ$ cell lines have very low incorporation of ($ sp{14}$C) from propionate into acid precipitable material while incorporation in $mut sp-$ cells is increased when cells are incubated in cobalamin. Intragenic complementation was first observed with WG 1130, a $mut sp circ$ fibroblast line with a homozygous R93H mutation, that is capable of complementing MCM activity when fused with some $mut sp circ$ and some $mut sp-$ cells (1). Extensive intragenic complementation in mut MMA was subsequently observed. Fibroblasts cultured from thirteen unrelated patients (6 $mut sp-$, 7 $mut sp circ$) were fused in all possible pairwise combination and MCM activity was assayed in the heterokaryons by measuring the incorporation of ($ sp{14}$C) from propionate into acid precipitable material. Intragenic complementation, indicated by stimulation of ($ sp{14}$C) -propionate incorporation following cell fusion with polyethylene glycol, was observed in fusions involving twelve of the thirteen strains. Of these thirteen strains, mutations have been identified in six; four have a homozygous mutation (WG 1130 (R93H), WG 1511 (H678R), WG 1610 (G717V), WG 1609 (G630E)), and two cell lines are compound heterozygous (WG 1681 (G623R and G703R), WG 1607 (W105R and A377E)); the remainders are yet to be determined. These intragenic complementations will provide information for grouping the mutations in defined domains in order to correlate structure and function of MCM.
APA, Harvard, Vancouver, ISO, and other styles
3

McKie, Norman. "Methylmalonyl CoA mutase from Saccharopolyspora erythraea." Thesis, University of Cambridge, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.259763.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Thomä, Nicolas Holger. "The mechanism of methylmalonyl-CoA mutase." Thesis, University of Cambridge, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.624301.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Mancia, Filippo. "The crystal structure of methylmalonyl-CoA mutase." Thesis, University of Cambridge, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.627037.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Kannan, Suresh M. "Studies on methylmalonyl-CoA mutase from Escherichia coli." Thesis, University of Westminster, 2008. https://westminsterresearch.westminster.ac.uk/item/91652/studies-on-methylmalonyl-coa-mutase-from-escherichia-coli.

Full text
Abstract:
Methylmalonyl-CoA mutase (MCM, E.C. 5.4.99.2), a coenzyme B12-dependent enzyme, catalyses the inter conversion of succinyl-CoA and methylmalonyl- CoA. The gene (sbm) encoding this enzyme is found in Escherichia coli (E. coli) at 62.3min on the E. coli chromosome. However, the metabolic role of this enzyme in the organism is not known. This project involves an investigation into this metabolic obscurity. The sbm gene is part of a four gene operon which also includes argK (or ygfD) that codes for a protein kinase catalysing the phosphorylation of two periplasmic binding proteins involved in cationic amino acid transport, ygfG that codes for methylmalonyl-CoA decarboxylase and ygfH that codes for propionyl-CoA: succinyl-CoA transferase. From existing literature we suspect that this operon, including the sbm gene, could be involved in the utilisation of unusual carbon sources such as succinate and propionate. An insertion mutant of the sbm gene created by transposon mediated mutagenesis was used for investigating the role of this gene. The wild type E. coli K12 strain, E. coli TR6524 and the mutant E. coli K12 (sbm::MudJ) were used in this study. Growth of the two strains (E. coli TR6524 and FA1P1) in minimal media with three different concentrations (0.05, 0.5, 5.0μg/mL) of vitamin B12 and in the presence succinate, propionate or glucose as the sole source of carbon, was studied. Growth was typical in media with glucose with no major differences in the growth pattern of the wild type and mutant strain. However, the two strains exhibited a differential growth pattern in media containing succinate, with the wild type growing faster than the mutant, indicating the role of the sbm gene in the utilisation of this carbon source. Growth in media containing propionate as the sole carbon source indicated only marginal differences in the growth pattern of the wild type and mutant strain. This result possibly suggests that the other pathways for propionate utilisation in E. coli compensate for the lack of a functional Sbm protein in the mutant strain. Promoter analysis indicated the presence of a promoter induced by σS, a transcription factor involved in the expression of proteins under stress or stationary phase growth conditions. Reverse transcription polymerase chain reaction (RT-PCR) studies of the genes of the sbm operon (sbm-argK-ygfGygfH) under the same growth conditions were carried out. Densitometric analysis of the PCR products suggested that the transcription level of sbm was higher in E. coli grown in succinate as compared to when grown in glucose and not as much when grown in propionate indicating a transcriptional level control of the sbm gene expression during the utilisation of succinate. RT-PCR studies also indicated a higher level of transcription of the gene in the stationary phase of the culture during the utilisation of succinate. Real time reverse transcription PCR (QPCR) analysis was used for the absolute quantification of the transcription of the genes of the sbm operon. An increase in the mRNA levels corresponding to the sbm, argK and ygfG genes was observed as E. coli TR6524 growth reached stationary phase, in the presence of succinate or propionate as the sole source of carbon as compared to glucose, In contrast, the highest mRNA levels corresponding to the ygfH gene were observed in the early log-phase of growth. This indicated a differential transcriptional level control of the genes within the operon. This study further established the possible role of this operon in the utilisation of succinate and propionate. The MCM enzyme activity measurement in the whole cell extracts of the wild type E. coli K12, grown under the above mentioned conditions, led to the first ever measurement of MCM activity in wild type E. coli. These measurements also revealed a four fold increase of the MCM specific activity in the case of growth in succinate (4.76x10-3U/mg) and a two fold increase for growth in propionate (2.79x10-3U/mg) compared to that observed with growth in glucose (1.37x10-3U/mg), indicating a significant level of involvement of the enzyme in succinate utilisation, and to a lesser extent in propionate utilisation. The proteomic analysis to understand the gene expression pattern of E. coli TR6524 was carried out using cells harvested at the stationary phase. The results showed that growth conditions induced the expression of transport related (HisJ, DppA) and energy generating proteins (PckA, AceF) required by E. coli to cope with the stressful growth conditions. However, Sbm was not identified among the limited protein spots that were analysed. Finally, E. coli K12 sbm gene was successfully cloned into B. cereus SPV leading to the development of a metabolically engineered polyhydroxyalkanoate producing strain of B. cereus. The intention was to provide the bacteria with a natural intracellular source of propionyl-CoA, leading to the production of the P(3HB-co-3HV) copolymer from structurally non related carbon sources like glucose. Hence, this work has initiated investigation into the metabolic role of the sbm gene product in E. coli. In addition, it has also led to the use of this gene product in metabolic engineering applications.
APA, Harvard, Vancouver, ISO, and other styles
7

Keep, Nicholas herbert. "Studies on the structure and mechanisms of methylmalonyl-CoA mutase." Thesis, University of Cambridge, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.259593.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Darley, Daniel James. "Mechanistic investigations into coenzyme B←1←2 dependent enzymes." Thesis, University of Newcastle Upon Tyne, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.364804.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Qureshi, Amber A. (Amber Ateef). "The molecular characterization of mutations at the methylmalonyl CoA mutase locus involved in interallelic complementation /." Thesis, McGill University, 1993. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=69686.

Full text
Abstract:
Methylmalonic aciduria is an autosomal recessive metabolic disorder, which may be due to a defect in the methylmalonyl CoA mutase (MCM) apoenzyme. The mut$ sp circ$ mutation is characterized by undetectable enzyme activity in cell extracts, and by the low incorporation of ($ sp{14}$C) propionate in the presence of hydroxocobalamin in culture. A mut$ sp circ$ fibroblast cell line, WG 1681, from an African-American male infant was shown to complement another mut$ sp circ$ cell line, WG 1130. Subsequent cloning and sequencing of cDNA from WG 1681 identified two previously described homozygous polymorphisms: H532R and V671I(1). In addition, compound heterozygosity was observed for two novel changes at highly conserved sites: G623R and G703R. Hybridization of allele specific oligonucleotides to PCR amplified MCM exons from WG 1681 and family members identified a clinically normal mother, sister and half-brother as carriers of the G703R change in cis with both polymorphisms. The putative father was not identified as a carrier of the G623R change. transfection of each change, singly and in cis with both polymorphisms, into GM1673 cells demonstrated a lack of stimulation of ($ sp{14}$C) propionate uptake in the absence and presence of OH-Cbl, in comparison to controls. Co-transfection of each separate mutation with the previously identified R93H mutation of WG 1130 (2) stimulated propionate uptake. These results indicate that G623R and G703R are novel mutations responsible for deficient MCM activity and the mut$ sp circ$ phenotype in WG 1681, and both mutations are independently capable of complementing the R93H mutation of WG 1130.
APA, Harvard, Vancouver, ISO, and other styles
10

Marsh, Edward Neil. "A structural investigation of a B←1←2-dependent enzyme : methylmalonyl-CoA mutase from Propionibacterium shermanii." Thesis, University of Cambridge, 1988. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.303288.

Full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Book chapters on the topic "Methylmalonyl coenzyme A mutase"

1

Thomä, Nicolas H., Thomas W. Meier, and Peter F. Leadlay. "Tritium Isotope Effects and Site-Directed Mutagenesis as Probes of the Reaction Catalysed by Methylmalonyl-CoA Mutase." In Vitamin B12 and B12 -Proteins, 227–36. Weinheim, Germany: Wiley-VCH Verlag GmbH, 2007. http://dx.doi.org/10.1002/9783527612192.ch14.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Morrison, Harry. "Methylmalonyl coenzyme A mutase." In Enzyme Active Sites and their Reaction Mechanisms, 135–43. Elsevier, 2021. http://dx.doi.org/10.1016/b978-0-12-821067-3.00024-6.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Fred Kolhouse, J., Sally P. Stabler, and Robert H. Allen. "[51] l-Methylmalonyl-CoA mutase from human placenta." In Methods in Enzymology, 407–14. Elsevier, 1988. http://dx.doi.org/10.1016/s0076-6879(88)66053-8.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Mascarenhas, Romila, Harsha Gouda, Markus Ruetz, and Ruma Banerjee. "Human B12-dependent enzymes: Methionine synthase and Methylmalonyl-CoA mutase." In Methods in Enzymology. Elsevier, 2022. http://dx.doi.org/10.1016/bs.mie.2021.12.012.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "Methylmalonyl coenzyme A mutase"

1

DILLI, DILEK, DILARA DAG, MUSTAFA KILIC, SERDAR CEYLANER, AHMET OZYAZICI, and AYSEGUL ZENCIROGLU. "P49 A novel p.v438sfs*3 (c.1311_1312insa) mutation in methylmalonyl-coa mutase gene in a newborn with severe methylmalonic acidemia." In 8th Europaediatrics Congress jointly held with, The 13th National Congress of Romanian Pediatrics Society, 7–10 June 2017, Palace of Parliament, Romania, Paediatrics building bridges across Europe. BMJ Publishing Group Ltd and Royal College of Paediatrics and Child Health, 2017. http://dx.doi.org/10.1136/archdischild-2017-313273.137.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'Methylmalonyl coenzyme A mutase' for particular source types:
Journal articles Dissertations / Theses
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography