Crystal structure of fatty acid‐CoA racemase from <i>Mycobacterium tuberculosis</i> H37Rv

Lee, Ki Seog; Park, Seon Mi; Rhee, Kyu-Nam; Bang, Won-Gi; Hwang, Kwang Yeon; Min, Young

doi:10.1002/prot.21029

Cited by 9 publications

(7 citation statements)

References 28 publications

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“…Mcr Mtub harbors four highly conserved amino acid residues (Arg91, His126, Asp156, and Glu241), which are also found in Mcr Nf (Arg56, His134, Asp164, and Glu249) and Mcr VH2 (Arg105, His140, Asp170, and Glu255) (22). Amino acid sequence comparisons showed that both racemases-Mcr VH2 and Mcr Nfbelong to the family III CoA transferases, which are divided into groups of racemases and CoA transferases (13). The conserved Glu residue occurs only in racemase enzymes (22) and confirms Mcr VH2 and Mcr Nf to be racemases also on the basis of comparisons of aa sequences.…”

Section: Disruption Of Mcrmentioning

confidence: 94%

Cloning and Characterization of α-Methylacyl Coenzyme A Racemase from Gordonia polyisoprenivorans VH2

Arenskötter

Heller

Dietz

et al. 2008

Appl Environ Microbiol

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The mcr gene of Gordonia polyisoprenivorans VH2 is not clustered with genes required for rubber degradation. Its disruption by insertion of a kanamycin resistance cassette impaired growth on methyl-branched isoprenoids but not on linear hydrocarbons. Intact mcr from this bacterium or from Nocardia farcinica IFM 10152 complemented the mutant. Reverse transcription analysis showed similar mcr VH2 expression results during cultivation with poly(cis-1,4-isoprene) and propionate. Additional genes coding for a putative cytochrome P450 monooxygenase and a short-chain dehydrogenase/reductase involved in ␤-oxidation and poly(cis-1,4-isoprene) degradation were also characterized.

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Section: Disruption Of Mcrmentioning

confidence: 94%

Cloning and Characterization of α-Methylacyl Coenzyme A Racemase from Gordonia polyisoprenivorans VH2

Arenskötter

Heller

Dietz

et al. 2008

Appl Environ Microbiol

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“…These enzymes are dimers whose structures consist of two interlinked rings. Most recently, X‐ray crystal structures of M. tuberculosis homologues of AMACR, MCR [90] and FAR [95], have been reported, which possessed the same overall fold. The structure of MCR was reported in conjunction with a site‐directed mutagenesis study that identified some of the catalytic residues [90].…”

Section: Biochemistry Of Amacrmentioning

confidence: 99%

α‐Methylacyl‐CoA racemase – an ‘obscure’ metabolic enzyme takes centre stage

et al. 2008

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Branched‐chain lipids are important components of the human diet and are used as drug molecules, e.g. ibuprofen. Owing to the presence of methyl groups on their carbon chains, they cannot be metabolized in mitochondria, and instead are processed and degraded in peroxisomes. Several different oxidative degradation pathways for these lipids are known, including α‐oxidation, β‐oxidation, and ω‐oxidation. Dietary branched‐chain lipids (especially phytanic acid) have attracted much attention in recent years, due to their link with prostate, breast, colon and other cancers as well as their role in neurological disease. A central role in all the metabolic pathways is played by α‐methylacyl‐CoA racemase (AMACR), which regulates metabolism of these lipids and drugs. AMACR catalyses the chiral inversion of a diverse number of 2‐methyl acids (as their CoA esters), and regulates the entry of branched‐chain lipids into the peroxisomal and mitochondrial β‐oxidation pathways. This review brings together advances in the different disciplines, and considers new research in both the metabolism of branched‐chain lipids and their role in cancer, with particular emphasis on the crucial role played by AMACR. These recent advances enable new preventative and treatment strategies for cancer.

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“…12 The importance of this racemase activity for M. tuberculosis is emphasized by the observation that several homologues are present in this species. 13,14 The structural data of MCR 11 have shown that this enzyme belongs to the superfamily of type III CoA transferases. 15 The structure of MCR is the only known structure of a CoA racemase of this new superfamily.…”

Section: Introductionmentioning

confidence: 99%

The Catalysis of the 1,1-Proton Transfer by α-Methyl-acyl-CoA Racemase Is Coupled to a Movement of the Fatty Acyl Moiety Over a Hydrophobic, Methionine-rich Surface

Bhaumik

Schmitz

Hassinen

et al. 2007

Journal of Molecular Biology

100

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Crystal structure of fatty acid‐CoA racemase from Mycobacterium tuberculosis H37Rv

Cited by 9 publications

References 28 publications

Cloning and Characterization of α-Methylacyl Coenzyme A Racemase from Gordonia polyisoprenivorans VH2

Cloning and Characterization of α-Methylacyl Coenzyme A Racemase from Gordonia polyisoprenivorans VH2

α‐Methylacyl‐CoA racemase – an ‘obscure’ metabolic enzyme takes centre stage

The Catalysis of the 1,1-Proton Transfer by α-Methyl-acyl-CoA Racemase Is Coupled to a Movement of the Fatty Acyl Moiety Over a Hydrophobic, Methionine-rich Surface

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