The absolute configuration of methylmalonyl CoA and stereochemistry of the methylmalonyl CoA mutase reaction

Sprecher, Milon; Clark, M.J.; Sprinson, David B.

doi:10.1016/0006-291x(64)90508-x

Cited by 39 publications

(7 citation statements)

References 12 publications

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“…Retention of Configuration during HCM Catalysis-As already found with MCM and ECM, only converting (R)-methylmalonyl-and (R)-ethylmalonyl-CoA (10,27), respectively, HCM catalysis is stereospecific, favoring the rearrangement of (S)-3-hydroxybutyryl-CoA versus the (R)-enantiomer. This specificity of catalysis may also shed light on the orientation of the hydroxyacyl substrate at the catalytic site of HCM.…”

Section: Subunit and Substratementioning

confidence: 61%

Bacterial Acyl-CoA Mutase Specifically Catalyzes Coenzyme B12-dependent Isomerization of 2-Hydroxyisobutyryl-CoA and (S)-3-Hydroxybutyryl-CoA

Yaneva

Schuster

Schäfer

et al. 2012

Journal of Biological Chemistry

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Section: Subunit and Substratementioning

confidence: 61%

Bacterial Acyl-CoA Mutase Specifically Catalyzes Coenzyme B12-dependent Isomerization of 2-Hydroxyisobutyryl-CoA and (S)-3-Hydroxybutyryl-CoA

Yaneva

Schuster

Schäfer

et al. 2012

Journal of Biological Chemistry

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“…Since the ester and amide derivatives of carboxylic acids have been shown to migrate during aromatization of arene-1,2-oxides, it is probable that thioesters would behave in a similar manner. Indeed, Dagli et al (17) reported that thioesters have very high "migratory aptitudes" in reactions involving the nonenzymatic rearrangement of epoxides, and intramolecular migration of a CoAthioester group (COSCoA) during enzyme-mediated conversion of methylmalonyl-CoA to succinyl-CoA has also been demonstrated (61). With this in mind, it is postulated that the substrate for the 1-hydroxylase enzyme implicated in the 4HBA pathway in Haloarcula sp.…”

Section: Discussionmentioning

confidence: 99%

Aerobic Metabolism of 4-Hydroxybenzoic Acid in Archaea via an Unusual Pathway Involving an Intramolecular Migration (NIH Shift)

Fairley

Boyd

Sharma

et al. 2002

Appl Environ Microbiol

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A novel haloarchaeal strain, Haloarcula sp. strain D1, grew aerobically on 4-hydroxybenzoic acid (4HBA) as a sole carbon and energy source and is the first member of the domain Archaea reported to do so. Unusually, D1 metabolized 4HBA via gentisic acid rather than via protocatechuic acid, hydroquinone, or catechol. Gentisate was detected in 4HBA-grown cultures, and gentisate 1,2-dioxygenase activity was induced in 4HBA-grown cells. Stoichiometric accumulation of gentisate from 4HBA was demonstrated in 4HBA-grown cell suspensions containing 2,2-dipyridyl (which strongly inhibits gentisate 1,2-dioxygenase). To establish whether initial 1-hydroxylation of 4HBA with concomitant 1,2-carboxyl group migration to yield gentisate occurred, 2,6-dideutero-4HBA was synthesized and used as a substrate. Deuterated gentisate was recovered from cell suspensions and identified as 3-deutero-gentisate, using gas chromatography-mass spectrometry and proton nuclear magnetic resonance spectroscopy. This structural isomer would be expected only if a 1,2-carboxyl group migration had taken place, and it provides compelling evidence that the 4HBA pathway in Haloarcula sp. strain D1 involves a hydroxylation-induced intramolecular migration. To our knowledge, this is the first report of a pathway which involves such a transformation (called an NIH shift) in the domain Archaea.

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“…Precedence for opposite steric courses is found in the coenzyme B 12 ‐dependent carbon skeleton rearrangements. Methylmalonyl‐CoA mutase operates with retention [24, 25], methylene glutarate mutase [26]and glutamate mutases [27]with inversion of configuration. Even the same enzyme, the coenzyme B 12 ‐dependent ethanolamine ammonia‐lyase, operates with opposite steric courses, inversion and retention with (2 R )‐ and (2 S )‐propanolamines, respectively [28].…”

Section: Discussionmentioning

confidence: 99%

The role and source of 5′‐deoxyadenosyl radical in a carbon skeleton rearrangement catalyzed by a plant enzyme

1998

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The last step in the biosynthesis of tropane alkaloids is the carbon skeleton rearrangement of littorine to hyoscyamine. The reaction is catalyzed by a cell-free extract prepared from cultured hairy roots of Datura stramonium. Adenosylmethionine stimulated the rearrangement 10^20-fold and showed saturation kinetics with an apparent K m of 25 W WM. It is proposed that S-adenosylmethionine is the source of a 5P-deoxyadenosyl radical which initiates the rearrangement in a similar manner as it does in analogous rearrangements catalyzed by coenzyme B IPdependent enzymes. Possible roles of S-adenosylmethionine as a radical source in higher plants are discussed.z 1998 Federation of European Biochemical Societies.

show abstract

The absolute configuration of methylmalonyl CoA and stereochemistry of the methylmalonyl CoA mutase reaction

Cited by 39 publications

References 12 publications

Bacterial Acyl-CoA Mutase Specifically Catalyzes Coenzyme B12-dependent Isomerization of 2-Hydroxyisobutyryl-CoA and (S)-3-Hydroxybutyryl-CoA

Bacterial Acyl-CoA Mutase Specifically Catalyzes Coenzyme B12-dependent Isomerization of 2-Hydroxyisobutyryl-CoA and (S)-3-Hydroxybutyryl-CoA

Aerobic Metabolism of 4-Hydroxybenzoic Acid in Archaea via an Unusual Pathway Involving an Intramolecular Migration (NIH Shift)

The role and source of 5′‐deoxyadenosyl radical in a carbon skeleton rearrangement catalyzed by a plant enzyme

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