Acyl‐CoA dehydrogenases and acyl‐CoA oxidases

Kim, Jung‐Ja P.; Miura, Retsu

doi:10.1046/j.1432-1033.2003.03948.x

Cited by 169 publications

(236 citation statements)

References 40 publications

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“…1 B and C) (reviewed in ref. 8). However, AidB contains unique features that distinguish it functionally from the ACAD enzymes.…”

Section: Resultsmentioning

confidence: 99%

“…Proteins within the ACAD superfamily share conserved features inside their FAD active sites (8). The FAD binds in an extended conformation at the A/B subunit interface, with the isoalloxazine ring buried within a central cavity that contains catalytic residues (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…3) (10). It has been proposed that the glycine in this position in IVD allows for binding branched acyl chains (8,18). In addition to the Trp-424 steric block, the 5-Å displacement of the Glu-425 carboxylate from its normal position in ACADs (Fig.…”

Section: Discussionmentioning

confidence: 99%

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Structure and DNA binding of alkylation response protein AidB

Bowles

Metz

O'Quin

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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Exposure of Escherichia coli to alkylating agents activates expression of AidB in addition to DNA repair proteins Ada, AlkA, and AlkB. AidB was recently shown to possess a flavin adenine dinucleotide (FAD) cofactor and to bind to dsDNA, implicating it as a flavindependent DNA repair enzyme. However, the molecular mechanism by which AidB acts to reduce the mutagenic effects of specific DNA alkylators is unknown. We present a 1.7-Å crystal structure of AidB, which bears superficial resemblance to the acyl-CoA dehydrogenase superfamily of flavoproteins. The structure reveals a unique quaternary organization and a distinctive FAD active site that provides a rationale for AidB's limited dehydrogenase activity. A highly electropositive C-terminal domain not present in structural homologs was identified by mutational analysis as the DNA binding site. Structural analysis of the DNA and FAD binding sites provides evidence against AidB-catalyzed DNA repair and supports a model in which AidB acts to prevent alkylation damage by protecting DNA and destroying alkylating agents that have yet to reach their DNA target.acyl-CoA dehydrogenase ͉ adaptive response ͉ DNA repair ͉ flavin adenine dinucleotide

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“…1 B and C) (reviewed in ref. 8). However, AidB contains unique features that distinguish it functionally from the ACAD enzymes.…”

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Structure and DNA binding of alkylation response protein AidB

Bowles

Metz

O'Quin

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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“…2A). This interaction also includes a weak ionic interaction between Lys 21 and Glu␤ 73 in addition to the hydrogen bond between Glu 22 and Thr␤ 77 . However, these residues are not conserved, suggesting this interaction is specific to the ETF⅐MCAD complex.…”

Section: Resultsmentioning

confidence: 99%

Extensive Domain Motion and Electron Transfer in the Human Electron Transferring Flavoprotein·Medium Chain Acyl-CoA Dehydrogenase Complex

Toogood

Thiel

Basran

et al. 2004

Journal of Biological Chemistry

137

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The crystal structure of the human electron transferring flavoprotein (ETF)⅐medium chain acyl-CoA dehydrogenase (MCAD) complex reveals a dual mode of protein-protein interaction, imparting both specificity and promiscuity in the interaction of ETF with a range of structurally distinct primary dehydrogenases. ETF partitions the functions of partner binding and electron transfer between (i) the recognition loop, which acts as a static anchor at the ETF⅐MCAD interface, and (ii) the highly mobile redox active FAD domain. Together, these enable the FAD domain of ETF to sample a range of conformations, some compatible with fast interprotein electron transfer. Disorders in amino acid or fatty acid catabolism can be attributed to mutations at the protein-protein interface. Crucially, complex formation triggers mobility of the FAD domain, an induced disorder that contrasts with general models of protein-protein interaction by induced fit mechanisms. The subsequent interfacial motion in the MCAD⅐ETF complex is the basis for the interaction of ETF with structurally diverse protein partners. Solution studies using ETF and MCAD with mutations at the protein-protein interface support this dynamic model and indicate ionic interactions between MCAD Glu 212 and ETF Arg␣ 249 are likely to transiently stabilize productive conformations of the FAD domain leading to enhanced electron transfer rates between both partners.

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“…The Bcd/EtfAB complex from C. kluyveri has been purified from the soluble cell fraction and was shown to catalyze reaction 5 (36). Both the butyryl-CoA dehydrogenase (Bcd) (37) and the electrontransfer proteins (EtfAB) contain FAD (38,39). Also, the presence of the RnfA-G complex in the membrane fraction from C. kluyveri could be demonstrated.…”

Section: Ethanol Dehydrogenases and Acetaldehyde Dehydrogenases In Amentioning

confidence: 98%

The genome ofClostridium kluyveri, a strict anaerobe with unique metabolic features

Seedorf

Fricke

Veith

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

421

386

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Clostridium kluyveri is unique among the clostridia; it grows anaerobically on ethanol and acetate as sole energy sources. Fermentation products are butyrate, caproate, and H2. We report here the genome sequence of C. kluyveri, which revealed new insights into the metabolic capabilities of this well studied organism. A membrane-bound energy-converting NADH:ferredoxin oxidoreductase (RnfCDGEAB) and a cytoplasmic butyryl-CoA dehydrogenase complex (Bcd/EtfAB) coupling the reduction of crotonyl-CoA to butyryl-CoA with the reduction of ferredoxin represent a new energy-conserving module in anaerobes. The genes for NAD-dependent ethanol dehydrogenase and NAD(P)-dependent acetaldehyde dehydrogenase are located next to genes for microcompartment proteins, suggesting that the two enzymes, which are isolated together in a macromolecular complex, form a carboxysome-like structure. Unique for a strict anaerobe, C. kluyveri harbors three sets of genes predicted to encode for polyketide/nonribosomal peptide synthetase hybrides and one set for a nonribosomal peptide synthetase. The latter is predicted to catalyze the synthesis of a new siderophore, which is formed under iron-deficient growth conditions. butyryl-CoA dehydrogenase ͉ electron transfer flavoproteins ͉ genome sequence ͉ Rnf-dependent energy conservation

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Acyl‐CoA dehydrogenases and acyl‐CoA oxidases

Cited by 169 publications

References 40 publications

Structure and DNA binding of alkylation response protein AidB

Structure and DNA binding of alkylation response protein AidB

Extensive Domain Motion and Electron Transfer in the Human Electron Transferring Flavoprotein·Medium Chain Acyl-CoA Dehydrogenase Complex

The genome ofClostridium kluyveri, a strict anaerobe with unique metabolic features

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